|
Name |
Accession |
Description |
Interval |
E-value |
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-258 |
9.81e-142 |
|
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: 398.26 E-value: 9.81e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 5 AISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAIL 84
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 85 PQGPSAPEGLTVHQLVKQGRYPYQNWLKQWSKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIIL 164
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGRYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 165 LDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEVITCDLVQNVFSMNCQ 244
Cdd:COG1120 161 LDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVYGVEAR 240
|
250
....*....|....
gi 499189069 245 VTQDPLFGTPLCIP 258
Cdd:COG1120 241 VIEDPVTGRPLVLP 254
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
6-257 |
5.96e-117 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 335.83 E-value: 5.96e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAILP 85
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 86 QGPSAPEGLTVHQLVKQGRYPYQNWLKQWSKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILL 165
Cdd:PRK11231 83 QHHLTPEGITVRELVAYGRSPWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 166 DEPTTYLDMTHQIEILDLLFELNEkEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEVITCDLVQNVFSMNCQV 245
Cdd:PRK11231 163 DEPTTYLDINHQVELMRLMRELNT-QGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVFDVEAEI 241
|
250
....*....|..
gi 499189069 246 TQDPLFGTPLCI 257
Cdd:PRK11231 242 HPEPVSGTPMCV 253
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
9-261 |
1.96e-111 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 322.32 E-value: 1.96e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 9 ETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAILPQGP 88
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 89 SAPEGLTVHQLVKQGRYPYQNWLKQWSKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEP 168
Cdd:PRK10253 91 TTPGDITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 169 TTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEVITCDLVQNVFSMNCQVTQD 248
Cdd:PRK10253 171 TTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYGLRCMIIDD 250
|
250
....*....|...
gi 499189069 249 PLFGTPLCIPHGR 261
Cdd:PRK10253 251 PVAGTPLVVPLGR 263
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
6-260 |
6.67e-102 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 297.38 E-value: 6.67e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAILP 85
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 86 QGPSAPEGLTVHQLVKQGRYPY-QNWLkqwSKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIIL 164
Cdd:COG4604 82 QENHINSRLTVRELVAFGRFPYsKGRL---TAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 165 LDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEVITCDLVQNVFSMNCQ 244
Cdd:COG4604 159 LDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEVLSDIYDTDIE 238
|
250
....*....|....*.
gi 499189069 245 VTQDPlfGTPLCIPHG 260
Cdd:COG4604 239 VEEID--GKRICVYFR 252
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-224 |
9.58e-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: 9.58e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 7 STETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAILPQ 86
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 87 gpsapegltvhqlvkqgrypyqnwlkqwskedeeaverALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLD 166
Cdd:cd03214 81 --------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499189069 167 EPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEG 224
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-241 |
2.95e-79 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 239.61 E-value: 2.95e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 1 MGMSAISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRaiaklPTKEVAKE 80
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK-----PPRRARRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 81 LAILPQGPSAPEG--LTVHQLVKQGRYPYQNWLKQWSKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQ 158
Cdd:COG1121 77 IGYVPQRAEVDWDfpITVRDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 159 ETDIILLDEPTTYLDMTHQIEILDLLFELNeKEDRTIVMVLHDLNLACRYAHHLVAIkDKRIYAEGRPEEVITCDLVQNV 238
Cdd:COG1121 157 DPDLLLLDEPFAGVDAATEEALYELLRELR-REGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLTPENLSRA 234
|
...
gi 499189069 239 FSM 241
Cdd:COG1121 235 YGG 237
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-260 |
1.12e-73 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 225.77 E-value: 1.12e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAILP 85
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 86 QGPSAPEGLTVHQLVKQGRYPYQnwlkQWSKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQ------- 158
Cdd:COG4559 82 QHSSLAFPFTVEEVVALGRAPHG----SSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQlwepvdg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 159 ETDIILLDEPTTYLDMTHQIEILDLLFELNEkEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEVITCDLVQNV 238
Cdd:COG4559 158 GPRWLFLDEPTSALDLAHQHAVLRLARQLAR-RGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELLERV 236
|
250 260
....*....|....*....|..
gi 499189069 239 FSMNCQVTQDPLFGTPLCIPHG 260
Cdd:COG4559 237 YGADLRVLAHPEGGCPQVLPRA 258
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
9-255 |
1.49e-73 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 225.82 E-value: 1.49e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 9 ETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAILPQGP 88
Cdd:PRK10575 15 RNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 89 SAPEGLTVHQLVKQGRYPYQNWLKQWSKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEP 168
Cdd:PRK10575 95 PAAEGMTVRELVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 169 TTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEVITCDLVQNVFSMNCQVTQD 248
Cdd:PRK10575 175 TSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIYGIPMGILPH 254
|
....*..
gi 499189069 249 PLFGTPL 255
Cdd:PRK10575 255 PAGAAPV 261
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
5-259 |
1.24e-71 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 220.80 E-value: 1.24e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 5 AISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAIL 84
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 85 PQGPSAPEGLTVHQLVKQGRYPYQnwlkQWSKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQ------ 158
Cdd:PRK13548 82 PQHSSLSFPFTVEEVVAMGRAPHG----LSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepdg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 159 ETDIILLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEVITCDLVQNV 238
Cdd:PRK13548 158 PPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPETLRRV 237
|
250 260
....*....|....*....|.
gi 499189069 239 FSMNCQVTQDPLFGTPLCIPH 259
Cdd:PRK13548 238 YGADVLVQPHPETGAPLVLPR 258
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
3-258 |
2.01e-71 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 224.72 E-value: 2.01e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 3 MSAISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELA 82
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 83 ILPQGPSAPEGLTVHQLVKQGRYPYQNWLKQWSKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDI 162
Cdd:PRK09536 81 SVPQDTSLSFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 163 ILLDEPTTYLDMTHQIEILDLLFELNEkEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEVITCDLVQNVFSMN 242
Cdd:PRK09536 161 LLLDEPTASLDINHQVRTLELVRRLVD-DGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFDAR 239
|
250
....*....|....*.
gi 499189069 243 CQVTQDPLFGTPLCIP 258
Cdd:PRK09536 240 TAVGTDPATGAPTVTP 255
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-224 |
1.87e-66 |
|
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: 205.84 E-value: 1.87e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 7 STETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRaiaklPTKEVAKELAILPQ 86
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK-----PLEKERKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 87 GPSAPEG--LTVHQLVKQGRYPYQNWLKQWSKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIIL 164
Cdd:cd03235 76 RRSIDRDfpISVRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 165 LDEPTTYLDMTHQIEILDLLFELNEKEdRTIVMVLHDLNLACRYAHHLVAIkDKRIYAEG 224
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELRREG-MTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-229 |
8.41e-62 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 195.28 E-value: 8.41e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 4 SAISTETLSLGY-GDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAK--- 79
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRlrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 80 ELAILPQGPSAPEGLTVHQLVKQGRYPY----QNWLKQWSKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMT 155
Cdd:COG3638 81 RIGMIFQQFNLVPRLSVLTNVLAGRLGRtstwRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499189069 156 LAQETDIILLDEPTTYLD-MTHQiEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEV 229
Cdd:COG3638 161 LVQEPKLILADEPVASLDpKTAR-QVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-231 |
4.48e-61 |
|
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: 192.55 E-value: 4.48e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDAV-IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAIL 84
Cdd:COG1122 1 IELENLSFSYPGGTpALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 85 PQGPSapegltvHQLVKQ--------GrypyqnwLKQ--WSKED-EEAVERALKATKLEDMADRAVDSLSGGQRQRAWIA 153
Cdd:COG1122 81 FQNPD-------DQLFAPtveedvafG-------PENlgLPREEiRERVEEALELVGLEHLADRPPHELSGGQKQRVAIA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499189069 154 MTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNeKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEVIT 231
Cdd:COG1122 147 GVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLN-KEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFS 223
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-230 |
1.57e-57 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 183.73 E-value: 1.57e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPtKEVAKELAILP 85
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDP-AEVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 86 QGPSAPEGLTVHQLVKqgrypYQNWLKQWSK-EDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIIL 164
Cdd:COG1131 80 QEPALYPDLTVRENLR-----FFARLYGLPRkEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499189069 165 LDEPTTYLDMTHQIEILDLLFELNEkEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEVI 230
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRELAA-EGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELK 219
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-236 |
1.18e-55 |
|
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: 179.30 E-value: 1.18e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDAV-IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKE---VAKEL 81
Cdd:cd03256 1 IEVENLSKTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 82 AILPQGPSAPEGLTVHQLVKQGRYPY----QNWLKQWSKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLA 157
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRLGRrstwRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499189069 158 QETDIILLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEVITCDLVQ 236
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEVLDE 239
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-219 |
2.85e-52 |
|
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: 169.57 E-value: 2.85e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 7 STETLSLGYGDA--VIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAIL 84
Cdd:cd03225 1 ELKNLSFSYPDGarPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 85 PQgpsAPE----GLTVHQLVKQGryPYQNWLKQwsKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQET 160
Cdd:cd03225 81 FQ---NPDdqffGPTVEEEVAFG--LENLGLPE--EEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499189069 161 DIILLDEPTTYLDMTHQIEILDLLFELNEkEDRTIVMVLHDLNLACRYAHHLVAIKDKR 219
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKA-EGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
6-229 |
3.50e-52 |
|
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: 170.56 E-value: 3.50e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDAV-IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKE---VAKEL 81
Cdd:TIGR02315 2 LEVENLSKVYPNGKqALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrkLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 82 AILPQGPSAPEGLTVHQLVKQGRYPYQN----WLKQWSKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLA 157
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVLHGRLGYKPtwrsLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499189069 158 QETDIILLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEV 229
Cdd:TIGR02315 162 QQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
14-207 |
7.55e-52 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 167.80 E-value: 7.55e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 14 GYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVllegraiaklpTKEVAKELAILPQGPSAPEG 93
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----------RRAGGARVAYVPQRSEVPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 94 L--TVHQLVKQGRYPYQNWLKQWSKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTY 171
Cdd:NF040873 70 LplTVRDLVAMGRWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 499189069 172 LDMTHQIEILDLLFELNEkEDRTIVMVLHDLNLACR 207
Cdd:NF040873 150 LDAESRERIIALLAEEHA-RGATVVVVTHDLELVRR 184
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-233 |
9.98e-52 |
|
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: 169.00 E-value: 9.98e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 1 MGMSAISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKE---V 77
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyeL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 78 AKELAILPQGpsapeG-----LTVhqlvkqgrypYQN---WLKQWSK--EDE--EAVERALKATKLEDMADRAVDSLSGG 145
Cdd:COG1127 81 RRRIGMLFQG-----GalfdsLTV----------FENvafPLREHTDlsEAEirELVLEKLELVGLPGAADKMPSELSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 146 QRQRAWIAMTLAQETDIILLDEPTTYLD--MThqIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAE 223
Cdd:COG1127 146 MRKRVALARALALDPEILLYDEPTAGLDpiTS--AVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAE 223
|
250
....*....|
gi 499189069 224 GRPEEVITCD 233
Cdd:COG1127 224 GTPEELLASD 233
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-233 |
3.33e-50 |
|
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: 164.98 E-value: 3.33e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKE---VAKELA 82
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 83 ILPQGPSAPEGLTVhqlvkqgrypYQN---WLKQWSKEDEEAVER----ALKATKLEDMADRAVDSLSGGQRQRAWIAMT 155
Cdd:cd03261 81 MLFQSGALFDSLTV----------FENvafPLREHTRLSEEEIREivleKLEAVGLRGAEDLYPAELSGGMKKRVALARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 156 LAQETDIILLDEPTTYLD--MTHQIEilDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEVITCD 233
Cdd:cd03261 151 LALDPELLLYDEPTAGLDpiASGVID--DLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASD 228
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-229 |
3.41e-50 |
|
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: 165.42 E-value: 3.41e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPtKEVAKELAILP 85
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP-REARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 86 QGPSAPEGLTVHQLVKqgrypYQNWLKQ-WSKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIIL 164
Cdd:COG4555 81 DERGLYDRLTVRENIR-----YFAELYGlFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499189069 165 LDEPTTYLDMTHQIEILDLLFELNeKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEV 229
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRALK-KEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
10-224 |
5.69e-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: 5.69e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 10 TLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVA---KELAILPQ 86
Cdd:cd03257 10 SFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKirrKEIQMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 87 GPSA---PeGLTV-HQLVKqgryPYQNWLKQWSKEDEEAVErALKATKL---EDMADRAVDSLSGGQRQRAWIAMTLAQE 159
Cdd:cd03257 90 DPMSslnP-RMTIgEQIAE----PLRIHGKLSKKEARKEAV-LLLLVGVglpEEVLNRYPHELSGGQRQRVAIARALALN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499189069 160 TDIILLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEG 224
Cdd:cd03257 164 PKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-231 |
5.88e-50 |
|
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: 171.62 E-value: 5.88e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 3 MS-AISTETLSLGY--GDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRG---GSVLLEGRAIAKLPTKE 76
Cdd:COG1123 1 MTpLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 77 VAKELAILPQGP-SAPEGLTV-HQLVKQGRypyqnwLKQWSKED-EEAVERALKATKLEDMADRAVDSLSGGQRQRAWIA 153
Cdd:COG1123 81 RGRRIGMVFQDPmTQLNPVTVgDQIAEALE------NLGLSRAEaRARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499189069 154 MTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEVIT 231
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
16-231 |
7.17e-50 |
|
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: 171.62 E-value: 7.17e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 16 GDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLP---TKEVAKELAILPQGPSA-- 90
Cdd:COG1123 276 GGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLRELRRRVQMVFQDPYSsl 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 91 -P---------EGLTVHQLVKQgrypyqnwlkqwsKEDEEAVERALKATKL-EDMADRAVDSLSGGQRQRAWIAMTLAQE 159
Cdd:COG1123 356 nPrmtvgdiiaEPLRLHGLLSR-------------AERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALALE 422
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499189069 160 TDIILLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEVIT 231
Cdd:COG1123 423 PKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFA 494
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-220 |
6.26e-47 |
|
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: 154.48 E-value: 6.26e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPtKEVAKELAILP 85
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP-EEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 86 QGPSAPEGLTVHQLVKqgrypyqnwlkqwskedeeaveralkatkledmadravdsLSGGQRQRAWIAMTLAQETDIILL 165
Cdd:cd03230 80 EEPSLYENLTVRENLK----------------------------------------LSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499189069 166 DEPTTYLDMTHQIEILDLLFELNeKEDRTIVMVLHDLNLACRYAHHLVAIKDKRI 220
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELK-KEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-231 |
1.60e-46 |
|
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: 155.67 E-value: 1.60e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKeLAILP 85
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIAR-LGIGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 86 --QGPSAPEGLTVHQLVK---QGRYPYQNWLKQWSKEDEEAVERA---LKATKLEDMADRAVDSLSGGQRQRAWIAMTLA 157
Cdd:cd03219 80 tfQIPRLFPELTVLENVMvaaQARTGSGLLLARARREEREARERAeelLERVGLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499189069 158 QETDIILLDEPTTYLDMTHQIEILDLLFELNEKeDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEVIT 231
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-220 |
5.17e-46 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 153.43 E-value: 5.17e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAILP 85
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 86 QGPSAPEGlTV-HQLvkqgRYPYQNWLKQWskeDEEAVERALKATKL-EDMADRAVDSLSGGQRQRAWIAMTLAQETDII 163
Cdd:COG4619 81 QEPALWGG-TVrDNL----PFPFQLRERKF---DRERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499189069 164 LLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRI 220
Cdd:COG4619 153 LLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
19-220 |
1.63e-45 |
|
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: 152.26 E-value: 1.63e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 19 VIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVA----KELAILPQGPSAPEGL 94
Cdd:cd03255 18 QALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafrrRHIGFVFQSFNLLPDL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 95 TVhqlvkqgrypYQN------WLKQWSKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEP 168
Cdd:cd03255 98 TA----------LENvelpllLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499189069 169 TTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLAcRYAHHLVAIKDKRI 220
Cdd:cd03255 168 TGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
11-220 |
2.22e-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: 151.90 E-value: 2.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 11 LSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEvaKELAILPQGPSA 90
Cdd:cd03259 6 LSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER--RNIGMVFQDYAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 91 PEGLTVHQ-----LVKQGrypyqnwlkqWSKEDEEA-VERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIIL 164
Cdd:cd03259 84 FPHLTVAEniafgLKLRG----------VPKAEIRArVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499189069 165 LDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRI 220
Cdd:cd03259 154 LDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
14-225 |
7.10e-45 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 150.96 E-value: 7.10e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 14 GYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAK----ELAILPQG-- 87
Cdd:COG1136 17 GEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARlrrrHIGFVFQFfn 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 88 --PSapegLTVHQ-----LVKQGRYPyqnwlkqwsKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQET 160
Cdd:COG1136 97 llPE----LTALEnvalpLLLAGVSR---------KERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499189069 161 DIILLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLAcRYAHHLVAIKDKRIYAEGR 225
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELA-ARADRVIRLRDGRIVSDER 227
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-229 |
1.44e-44 |
|
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: 151.11 E-value: 1.44e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 5 AISTETLSLGYG----DAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKE 80
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 81 LAILPQGP--SAPEGLTVHQLVKQgryPYQNwlkQWSKEDEEAVERALKATKL-EDMADRAVDSLSGGQRQRAWIAMTLA 157
Cdd:COG1124 81 VQMVFQDPyaSLHPRHTVDRILAE---PLRI---HGLPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499189069 158 QETDIILLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEV 229
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADL 226
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
11-219 |
5.71e-44 |
|
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: 146.62 E-value: 5.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 11 LSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAILPQgpsa 90
Cdd:cd00267 5 LSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 91 pegltvhqlvkqgrypyqnwlkqwskedeeaveralkatkledmadravdsLSGGQRQRAWIAMTLAQETDIILLDEPTT 170
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499189069 171 YLDMTHQIEILDLLFELNEkEDRTIVMVLHDLNLACRYAHHLVAIKDKR 219
Cdd:cd00267 110 GLDPASRERLLELLRELAE-EGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-229 |
1.16e-43 |
|
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: 1.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 1 MGMSAISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKE---- 76
Cdd:COG3842 1 MAMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKrnvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 77 -VAKELAILPQgpsapegLTVHQLVKQGrypyqnwLKQ--WSKED-EEAVERALKATKLEDMADRAVDSLSGGQRQRAWI 152
Cdd:COG3842 81 mVFQDYALFPH-------LTVAENVAFG-------LRMrgVPKAEiRARVAELLELVGLEGLADRYPHQLSGGQQQRVAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499189069 153 AMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEV 229
Cdd:COG3842 147 ARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
2-229 |
1.31e-43 |
|
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: 148.65 E-value: 1.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 2 GMSAISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKE- 80
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 81 LAILPQGPSAPEGLTV--------HQLVKQGRYPYQNWLKQWSKEDEEAVERA---LKATKLEDMADRAVDSLSGGQRQR 149
Cdd:COG0411 81 IARTFQNPRLFPELTVlenvlvaaHARLGRGLLAALLRLPRARREEREARERAeelLERVGLADRADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 150 AWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEV 229
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEV 240
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-229 |
2.10e-42 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 144.50 E-value: 2.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKE-LAIL 84
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 85 PQGPSAPEGLTVHQLVKQGRYPYQNwlkqwsKEDEEAVERALKA-TKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDII 163
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRR------AKRKARLERVYELfPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499189069 164 LLDEPTTYLDMTHQIEILDLLFELNEkEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEV 229
Cdd:cd03224 155 LLDEPSEGLAPKIVEEIFEAIRELRD-EGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-229 |
4.33e-42 |
|
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: 143.86 E-value: 4.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARL-----MKPRGGSVLLEGRAIAKLPTK--EVA 78
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDvlELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 79 KELAILPQGPSaPEGLTVHQLVkqgRYPYQNWLKQWSKEDEEAVERALKATKL-EDMADRA-VDSLSGGQRQRAWIAMTL 156
Cdd:cd03260 81 RRVGMVFQKPN-PFPGSIYDNV---AYGLRLHGIKLKEELDERVEEALRKAALwDEVKDRLhALGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499189069 157 AQETDIILLDEPTTYLD--MTHQIEilDLLFELneKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEV 229
Cdd:cd03260 157 ANEPEVLLLDEPTSALDpiSTAKIE--ELIAEL--KKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-234 |
6.16e-42 |
|
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: 143.38 E-value: 6.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDA----VIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAklptkEVAKEL 81
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT-----GPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 82 AILPQGPSAPEGLTVHQLVkqgRYPYQnwLKQWSK-EDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQET 160
Cdd:cd03293 76 GYVFQQDALLPWLTVLDNV---ALGLE--LQGVPKaEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499189069 161 DIILLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRiyaeGRPEEVITCDL 234
Cdd:cd03293 151 DVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSARP----GRIVAEVEVDL 220
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
16-215 |
2.23e-41 |
|
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: 144.81 E-value: 2.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 16 GDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRG---GSVLLEGRAIAKLPTKEV----AKELAILPQGP 88
Cdd:COG0444 16 GVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLLKLSEKELrkirGREIQMIFQDP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 89 SA---P---------EGLTVHQLVKqgrypyqnwlkqwSKEDEEAVERALKATKLEDmADRAVDS----LSGGQRQRAWI 152
Cdd:COG0444 96 MTslnPvmtvgdqiaEPLRIHGGLS-------------KAEARERAIELLERVGLPD-PERRLDRypheLSGGMRQRVMI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499189069 153 AMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHlVAI 215
Cdd:COG0444 162 ARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADR-VAV 223
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
25-231 |
3.13e-40 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 140.47 E-value: 3.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 25 NLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKE-----------VAKELAILPQgPSAPE- 92
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrkkismVFQSFALLPH-RTVLEn 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 93 ---GLTVHQLVKQGRypyqnwlkqwskedEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPT 169
Cdd:cd03294 123 vafGLEVQGVPRAER--------------EERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499189069 170 TYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEVIT 231
Cdd:cd03294 189 SALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
21-229 |
3.68e-40 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the 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: 140.28 E-value: 3.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 21 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIA---KLPTKEVAKELAILPQgpsAPEgltvH 97
Cdd:TIGR04521 21 LDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITakkKKKLKDLRKKVGLVFQ---FPE----H 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 98 QLVKQGRY------PyqnwlKQWSKEDEEAVERALKATKL----EDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDE 167
Cdd:TIGR04521 94 QLFEETVYkdiafgP-----KNLGLSEEEAEERVKEALELvgldEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499189069 168 PTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEV 229
Cdd:TIGR04521 169 PTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREV 230
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
19-258 |
4.04e-40 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 140.35 E-value: 4.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 19 VIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLM----KPRG----GSVLLEGRAIAKLPTKEVAKELAILPQGPSA 90
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggAPRGarvtGDVTLNGEPLAAIDAPRLARLRAVLPQAAQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 91 PEGLTVHQLVKQGRYPYQNWLKQWSKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQ---------ETD 161
Cdd:PRK13547 95 AFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaqPPR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 162 IILLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEVITCDLVQNVFSM 241
Cdd:PRK13547 175 YLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLTPAHIARCYGF 254
|
250
....*....|....*..
gi 499189069 242 NCQVTQDPLFGTPLCIP 258
Cdd:PRK13547 255 AVRLVDAGDGVPPVIVP 271
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
24-242 |
4.23e-40 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 139.21 E-value: 4.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 24 LNLTIPKGEITVFIGSNGCGKSTLLRSLARLMkPRGGSVLLEGRAIAKLPTKEVAKELAILPQGPSAPEGLTVHQLVKqg 103
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAYLSQQQSPPFAMPVFQYLA-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 104 rypyqnwLKQWSKEDEEAVERAL----KATKLEDMADRAVDSLSGGQRQRAWIAMTLAQ-------ETDIILLDEPTTYL 172
Cdd:COG4138 92 -------LHQPAGASSEAVEQLLaqlaEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 173 DMTHQIEILDLLFELNEkEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEVITCDLVQNVFSMN 242
Cdd:COG4138 165 DVAQQAALDRLLRELCQ-QGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVFGVK 233
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-228 |
9.07e-40 |
|
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: 137.89 E-value: 9.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTkEVAKELAILP 85
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPR-EVRRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 86 QGPSAPEGLTVHQ-LVKQGR-YPYQNwlkqwsKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDII 163
Cdd:cd03265 80 QDLSVDDELTGWEnLYIHARlYGVPG------AERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499189069 164 LLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEE 228
Cdd:cd03265 154 FLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
6-201 |
2.20e-39 |
|
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: 136.07 E-value: 2.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTkEVAKELAILP 85
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARE-DYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 86 QGPSAPEGLTVHQLVkqgrypyQNWLKQW-SKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIIL 164
Cdd:COG4133 82 HADGLKPELTVRENL-------RFWAALYgLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 499189069 165 LDEPTTYLDmTHQIEILDLLFELNEKEDRTIVMVLHD 201
Cdd:COG4133 155 LDEPFTALD-AAGVALLAELIAAHLARGGAVLLTTHQ 190
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-170 |
2.60e-39 |
|
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: 134.31 E-value: 2.60e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 21 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAILPQGPSAPEGLTVHQLV 100
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499189069 101 KQGRYPyQNWLKQWSKEDeeaVERALKATKLEDMADRAVD----SLSGGQRQRAWIAMTLAQETDIILLDEPTT 170
Cdd:pfam00005 81 RLGLLL-KGLSKREKDAR---AEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
3-229 |
4.42e-39 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 139.44 E-value: 4.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 3 MSAISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKE-----V 77
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDrniamV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 78 AKELAILPQgpsapegLTVhqlvkqgrypYQN-----WLKQWSKED-EEAVERALKATKLEDMADRAVDSLSGGQRQRAW 151
Cdd:COG3839 81 FQSYALYPH-------MTV----------YENiafplKLRKVPKAEiDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 152 IAMTLAQETDIILLDEPTTYLD------MthQIEILDLLFELNekedRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGR 225
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLDaklrveM--RAEIKRLHRRLG----TTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGT 217
|
....
gi 499189069 226 PEEV 229
Cdd:COG3839 218 PEEL 221
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
6-231 |
6.11e-39 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 135.89 E-value: 6.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAkLPTKEVAK---ELA 82
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKlrrKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 83 ILPQG----PSapegLTVhqLvkqgrypyQN------WLKQWSKEdeEAVERA---LKATKLEDMADRAVDSLSGGQRQR 149
Cdd:COG1126 81 MVFQQfnlfPH----LTV--L--------ENvtlapiKVKKMSKA--EAEERAmelLERVGLADKADAYPAQLSGGQQQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 150 AWIAMTLAQETDIILLDEPTTYLD--MTHqiEILDLLFELnEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPE 227
Cdd:COG1126 145 VAIARALAMEPKVMLFDEPTSALDpeLVG--EVLDVMRDL-AKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPE 221
|
....
gi 499189069 228 EVIT 231
Cdd:COG1126 222 EFFE 225
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-202 |
7.62e-39 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 136.37 E-value: 7.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 1 MGMSAISTETLSLGY----GDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTke 76
Cdd:COG1116 3 AAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 77 vakELAILPQGPSAPEGLTVHQ-----LVKQGRYPyqnwlkqwsKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAW 151
Cdd:COG1116 81 ---DRGVVFQEPALLPWLTVLDnvalgLELRGVPK---------AERRERARELLELVGLAGFEDAYPHQLSGGMRQRVA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499189069 152 IAMTLAQETDIILLDEPTTYLD-MThQIEILDLLFELNEKEDRTIVMVLHDL 202
Cdd:COG1116 149 IARALANDPEVLLMDEPFGALDaLT-RERLQDELLRLWQETGKTVLFVTHDV 199
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6-231 |
1.62e-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: 135.12 E-value: 1.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGD-AVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAIL 84
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 85 PQGPsapeGLTVHQLVKQ--GRYPYqnwLKQWSKEdeEAVERALKATKLEDM-----ADRAVDSLSGGQRQRAWIAMTLA 157
Cdd:cd03295 81 IQQI----GLFPHMTVEEniALVPK---LLKWPKE--KIRERADELLALVGLdpaefADRYPHELSGGQQQRVGVARALA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499189069 158 QETDIILLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEVIT 231
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
11-217 |
3.97e-38 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 131.93 E-value: 3.97e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 11 LSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKL--PTKEVAKELAILPQGP 88
Cdd:cd03229 6 VSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLedELPPLRRRIGMVFQDF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 89 SAPEGLTVhqlvkqgrypYQNwlkqwskedeeaveRALkatkledmadravdSLSGGQRQRAWIAMTLAQETDIILLDEP 168
Cdd:cd03229 86 ALFPHLTV----------LEN--------------IAL--------------GLSGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499189069 169 TTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKD 217
Cdd:cd03229 128 TSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-207 |
1.07e-37 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 133.24 E-value: 1.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 4 SAISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARL--------MKprgGSVLLEGRAI--AKLP 73
Cdd:COG1117 10 PKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndlipgarVE---GEILLDGEDIydPDVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 74 TKEVAKELAILPQGP-----SAPE----GLTVHQLVKQgrypyqnwlkqwsKEDEEAVERALKATKL-EDMADR----AV 139
Cdd:COG1117 87 VVELRRRVGMVFQKPnpfpkSIYDnvayGLRLHGIKSK-------------SELDEIVEESLRKAALwDEVKDRlkksAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 140 dSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLD--MTHQIEilDLLFELneKEDRTIVMVLHDLNLACR 207
Cdd:COG1117 154 -GLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpiSTAKIE--ELILEL--KKDYTIVIVTHNMQQAAR 218
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
5-236 |
1.98e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 133.32 E-value: 1.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 5 AISTETLSLGYGDAV-IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAI 83
Cdd:PRK13647 4 IIEVEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 84 LPQGPSAPE-GLTVHQLVKQGryPYQNWLKQwsKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDI 162
Cdd:PRK13647 84 VFQDPDDQVfSSTVWDDVAFG--PVNMGLDK--DEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499189069 163 ILLDEPTTYLDMTHQIEILDLLFELNeKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEVITCDLVQ 236
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRLH-NQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIVE 232
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-228 |
4.02e-37 |
|
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: 137.97 E-value: 4.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 4 SAISTETLSLGYGDA-VIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELA 82
Cdd:COG4988 335 PSIELEDVSFSYPGGrPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 83 ILPQGPSAPEGlTVHQLVKQGRypyqnwlkqwSKEDEEAVERALKATKLEDMADRAVD-----------SLSGGQRQRAW 151
Cdd:COG4988 415 WVPQNPYLFAG-TIRENLRLGR----------PDASDEELEAALEAAGLDEFVAALPDgldtplgeggrGLSGGQAQRLA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499189069 152 IAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELneKEDRTIVMVLHDLNLACRYAHHLVaIKDKRIYAEGRPEE 228
Cdd:COG4988 484 LARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL--AKGRTVILITHRLALLAQADRILV-LDDGRIVEQGTHEE 557
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
7-220 |
7.59e-37 |
|
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: 129.68 E-value: 7.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 7 STETLSLGYGDAV-IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRaiaKLPTKEVAKELAILP 85
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGK---PIKAKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 86 QGPSapegltvHQL----VKQGRYPYqnwLKQWSkEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETD 161
Cdd:cd03226 78 QDVD-------YQLftdsVREELLLG---LKELD-AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499189069 162 IILLDEPTTYLDMTHQIEILDLLFELnEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRI 220
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVGELIREL-AAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
3-229 |
1.95e-36 |
|
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: 129.33 E-value: 1.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 3 MSAISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKE-L 81
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 82 AILPQG----PSapegLTVHQLVKQGRYPyqnwlKQWSKEDEEAVERALKA-TKLEDMADRAVDSLSGGQRQRAWIAMTL 156
Cdd:COG0410 81 GYVPEGrrifPS----LTVEENLLLGAYA-----RRDRAEVRADLERVYELfPRLKERRRQRAGTLSGGEQQMLAIGRAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499189069 157 AQETDIILLDEPTTYL--DMTHqiEILDLLFELNEkEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEV 229
Cdd:COG0410 152 MSRPKLLLLDEPSLGLapLIVE--EIFEIIRRLNR-EGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
14-228 |
2.05e-36 |
|
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: 128.78 E-value: 2.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 14 GYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPtKEVAKELAILPQGPSAPEG 93
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDR-KAARQSLGYCPQFDALFDE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 94 LTVHQLVKqgrypYQNWLKQWSKEDEEA-VERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYL 172
Cdd:cd03263 90 LTVREHLR-----FYARLKGLPKSEIKEeVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499189069 173 DMTHQIEILDLLfeLNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEE 228
Cdd:cd03263 165 DPASRRAIWDLI--LEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-231 |
3.49e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 129.26 E-value: 3.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 3 MSAISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLM----KPR-GGSVLLEGRAIAKLPTKEV 77
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypEARvSGEVYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 78 AKELAILPQGPSAPEGLTVHQLVKQGryPYQNWLKQWSKEDEEAVERALKATKL-EDMADR---AVDSLSGGQRQRAWIA 153
Cdd:PRK14247 81 RRRVQMVFQIPNPIPNLSIFENVALG--LKLNRLVKSKKELQERVRWALEKAQLwDEVKDRldaPAGKLSGGQQQRLCIA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499189069 154 MTLAQETDIILLDEPTTYLDMTHQIEILDLLFELneKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEVIT 231
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLDPENTAKIESLFLEL--KKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFT 234
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-224 |
4.44e-36 |
|
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: 127.69 E-value: 4.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDAVIIDELNLTIPKGeITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKeVAKELAILP 85
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-LRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 86 QGPSAPEGLTVHQLVKqgrypYQNWLKQW-SKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIIL 164
Cdd:cd03264 79 QEFGVYPNFTVREFLD-----YIAWLKGIpSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499189069 165 LDEPTTYLDMTHQIEILDLLFELNekEDRTIVMVLH---DLNLACryaHHLVAIKDKRIYAEG 224
Cdd:cd03264 154 VDEPTAGLDPEERIRFRNLLSELG--EDRIVILSTHiveDVESLC---NQVAVLNKGKLVFEG 211
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
8-230 |
6.00e-36 |
|
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: 128.08 E-value: 6.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 8 TETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEV---AKELAIL 84
Cdd:cd03258 8 SKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaRRRIGMI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 85 PQGPSAPEGLTVHQLVKqgrYPYQnwLKQWSKED-EEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDII 163
Cdd:cd03258 88 FQHFNLLSSRTVFENVA---LPLE--IAGVPKAEiEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499189069 164 LLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEVI 230
Cdd:cd03258 163 LCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVF 229
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
12-228 |
8.35e-36 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 127.48 E-value: 8.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 12 SLGY-GDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAK----------E 80
Cdd:COG2884 8 SKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYlrrrigvvfqD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 81 LAILPQgpsapegLTVHQ-----LVKQGRYPyqnwlkqwsKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMT 155
Cdd:COG2884 88 FRLLPD-------RTVYEnvalpLRVTGKSR---------KEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499189069 156 LAQETDIILLDEPTTYLDMTHQIEILDLLFELNeKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEE 228
Cdd:COG2884 152 LVNRPELLLADEPTGNLDPETSWEIMELLEEIN-RRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEARGV 223
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-219 |
9.87e-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: 125.57 E-value: 9.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGD--AVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAI 83
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 84 LPQGPsapegltvhqlvkqgrypyqnWLkqwskedeeaveraLKATKLEDMadravdsLSGGQRQRAWIAMTLAQETDII 163
Cdd:cd03228 81 VPQDP---------------------FL--------------FSGTIRENI-------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499189069 164 LLDEPTTYLDMTHQIEILDLLFELneKEDRTIVMVLHDLNLAcRYAHHLVAIKDKR 219
Cdd:cd03228 119 ILDEATSALDPETEALILEALRAL--AKGKTVIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
25-228 |
2.70e-35 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 126.41 E-value: 2.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 25 NLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPtkeVAKE-LAILPQgpsapEG-----LTVHQ 98
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP---PAERpVSMLFQ-----ENnlfphLTVAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 99 LVKQGRYPYqnwLKqWSKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQI 178
Cdd:COG3840 91 NIGLGLRPG---LK-LTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQ 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499189069 179 EILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEE 228
Cdd:COG3840 167 EMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAA 216
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
6-231 |
2.77e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 127.50 E-value: 2.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGD-AVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIA--KLPTKEVAKELA 82
Cdd:PRK13639 2 LETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydKKSLLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 83 ILPQGPS----APeglTVHQLVKQGryPYQNWLKQwsKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQ 158
Cdd:PRK13639 82 IVFQNPDdqlfAP---TVEEDVAFG--PLNLGLSK--EEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499189069 159 ETDIILLDEPTTYLDMTHQIEILDLLFELNeKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEVIT 231
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLN-KEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFS 226
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
26-229 |
4.49e-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: 125.73 E-value: 4.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 26 LTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRaiaklPTKEVAKELAILPQ----GPSAPegLTVHQLVK 101
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGA-----SPGKGWRHIGYVPQrhefAWDFP--ISVAHTVM 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 102 QGRYPYQNWLKQWSKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEIL 181
Cdd:TIGR03771 74 SGRTGHIGWLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLT 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499189069 182 DLLFELnEKEDRTIVMVLHDLNLACRYAHHLVAIkDKRIYAEGRPEEV 229
Cdd:TIGR03771 154 ELFIEL-AGAGTAILMTTHDLAQAMATCDRVVLL-NGRVIADGTPQQL 199
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-220 |
5.88e-35 |
|
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: 124.95 E-value: 5.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAI--AKLPTKEVAKELAI 83
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 84 LPQGPSAPEGLTVHQLVKQGrypyQNWLKQWSKedEEAVERALKATK---LEDMADRAVDSLSGGQRQRAWIAMTLAQET 160
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLA----PIKVKGMSK--AEAEERALELLEkvgLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499189069 161 DIILLDEPTTYLD--MTHqiEILDLLFELnEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRI 220
Cdd:cd03262 155 KVMLFDEPTSALDpeLVG--EVLDVMKDL-AEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5-230 |
7.25e-35 |
|
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: 132.65 E-value: 7.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 5 AISTETLSLGYGDAV--IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELA 82
Cdd:COG2274 473 DIELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 83 ILPQGPSAPEGlTVhqlvkqgrypYQNwLKQWSKE-DEEAVERALKATKLED------------MADRAVdSLSGGQRQR 149
Cdd:COG2274 553 VVLQDVFLFSG-TI----------REN-ITLGDPDaTDEEIIEAARLAGLHDfiealpmgydtvVGEGGS-NLSGGQRQR 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 150 AWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELneKEDRTIVMVLHDLNLAcRYAHHLVAIKDKRIYAEGRPEEV 229
Cdd:COG2274 620 LAIARALLRNPRILILDEATSALDAETEAIILENLRRL--LKGRTVIIIAHRLSTI-RLADRIIVLDKGRIVEDGTHEEL 696
|
.
gi 499189069 230 I 230
Cdd:COG2274 697 L 697
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
15-248 |
8.27e-35 |
|
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: 125.58 E-value: 8.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 15 YGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKP-RGGSVLLEGRAIAKLPTKEVAKELAILpqgpSA--- 90
Cdd:COG1119 13 RGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPtYGNDVRLFGERRGGEDVWELRKRIGLV----SPalq 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 91 ---PEGLTVHQLVKQGRY----PYQnwlkQWSKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDII 163
Cdd:COG1119 89 lrfPRDETVLDVVLSGFFdsigLYR----EPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 164 LLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEVITCDLVQNVFSMNC 243
Cdd:COG1119 165 ILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLTSENLSEAFGLPV 244
|
....*
gi 499189069 244 QVTQD 248
Cdd:COG1119 245 EVERR 249
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-229 |
1.04e-34 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 126.28 E-value: 1.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 1 MGMSAISTETLSLGYGDA--VIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVA 78
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 79 KELAILPQGPSAP-EGLTVHQLVKQGrypyqnwLKQWSKEDEEAVER---ALKATKLEDMADRAVDSLSGGQRQRAWIAM 154
Cdd:PRK13635 81 RQVGMVFQNPDNQfVGATVQDDVAFG-------LENIGVPREEMVERvdqALRQVGMEDFLNREPHRLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499189069 155 TLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRyAHHLVAIKDKRIYAEGRPEEV 229
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEI 227
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
3-229 |
2.05e-34 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 127.19 E-value: 2.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 3 MSaISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGR-AIAKLPTKE----- 76
Cdd:COG1118 1 MS-IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRdLFTNLPPRErrvgf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 77 VAKELAILPQgpsapegLTVHQLVKQGrypyqnwL--KQWSKEDEEA-VERALKATKLEDMADRAVDSLSGGQRQRAWIA 153
Cdd:COG1118 80 VFQHYALFPH-------MTVAENIAFG-------LrvRPPSKAEIRArVEELLELVQLEGLADRYPSQLSGGQRQRVALA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499189069 154 MTLAQETDIILLDEPTTYLDmTH---QIEilDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEV 229
Cdd:COG1118 146 RALAVEPEVLLLDEPFGALD-AKvrkELR--RWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-229 |
5.39e-34 |
|
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: 123.12 E-value: 5.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKE-----VAKE 80
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKrpvntVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 81 LAILPQgpsapegLTVHQLVKqgrYPYQnwLKQWSKED-EEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQE 159
Cdd:cd03300 81 YALFPH-------LTVFENIA---FGLR--LKKLPKAEiKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNE 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499189069 160 TDIILLDEPTTYLDMTHQieiLDLLFELNEKEDR---TIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEV 229
Cdd:cd03300 149 PKVLLLDEPLGALDLKLR---KDMQLELKRLQKElgiTFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
5-230 |
4.02e-33 |
|
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: 126.80 E-value: 4.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 5 AISTETLSLGYGDAV--IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELA 82
Cdd:COG4987 333 SLELEDVSFRYPGAGrpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 83 ILPQGP---SApeglTVHQ---LVKQGrypyqnwlkqwskEDEEAVERALKATKLEDMADRAVD-----------SLSGG 145
Cdd:COG4987 413 VVPQRPhlfDT----TLREnlrLARPD-------------ATDEELWAALERVGLGDWLAALPDgldtwlgeggrRLSGG 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 146 QRQRAWIAMTLAQETDIILLDEPTTYLD-MTHQiEILDLLFELNekEDRTIVMVLHDLNLAcRYAHHLVAIKDKRIYAEG 224
Cdd:COG4987 476 ERRRLALARALLRDAPILLLDEPTEGLDaATEQ-ALLADLLEAL--AGRTVLLITHRLAGL-ERMDRILVLEDGRIVEQG 551
|
....*.
gi 499189069 225 RPEEVI 230
Cdd:COG4987 552 THEELL 557
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-229 |
5.80e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 121.10 E-value: 5.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 3 MSAISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRG-----GSVLLEGRAI--AKLPTK 75
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIysPDVDPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 76 EVAKELAILPQGPSAPEGLTVHQLVKQG-RYpyqNWLKQWSKEDEEAVERALKATKL-EDMADRAVD---SLSGGQRQRA 150
Cdd:PRK14267 82 EVRREVGMVFQYPNPFPHLTIYDNVAIGvKL---NGLVKSKKELDERVEWALKKAALwDEVKDRLNDypsNLSGGQRQRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499189069 151 WIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELneKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEV 229
Cdd:PRK14267 159 VIARALAMKPKILLMDEPTANIDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKV 235
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
4-231 |
2.82e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 119.71 E-value: 2.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 4 SAISTETLSLGYGDAV--IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKEL 81
Cdd:PRK13632 6 VMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 82 AILPQGP-SAPEGLTVHQLVKQG----RYPyqnwlkqwSKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTL 156
Cdd:PRK13632 86 GIIFQNPdNQFIGATVEDDIAFGlenkKVP--------PKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499189069 157 AQETDIILLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRyAHHLVAIKDKRIYAEGRPEEVIT 231
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILN 231
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-207 |
5.56e-32 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 118.34 E-value: 5.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 1 MGMSAISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARL--MKPR---GGSVLLEGRAI--AKLP 73
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIysPRTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 74 TKEVAKELAILPQGPSaPEGLTVHQLVKQG-RYpyqNWLKQWSKEDEeAVERALKATKL-EDMADRAVDS---LSGGQRQ 148
Cdd:PRK14239 81 TVDLRKEIGMVFQQPN-PFPMSIYENVVYGlRL---KGIKDKQVLDE-AVEKSLKGASIwDEVKDRLHDSalgLSGGQQQ 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499189069 149 RAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELneKEDRTIVMVLHDLNLACR 207
Cdd:PRK14239 156 RVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL--KDDYTMLLVTRSMQQASR 212
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
6-229 |
9.08e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 118.80 E-value: 9.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDAV-IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAI--AKLPTKEVAKELA 82
Cdd:PRK13636 6 LKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdySRKGLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 83 ILPQGPSapegltvHQLVKQGRYPYQNW----LKQWSKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQ 158
Cdd:PRK13636 86 MVFQDPD-------NQLFSASVYQDVSFgavnLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499189069 159 ETDIILLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEV 229
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
18-232 |
1.26e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 117.93 E-value: 1.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 18 AVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAILPQGPsapEGLTVH 97
Cdd:PRK13648 22 SFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQNP---DNQFVG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 98 QLVKqgrYPYQNWLKQWSKEDEEAVERALKATKLEDMADRAVD---SLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDM 174
Cdd:PRK13648 99 SIVK---YDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYepnALSGGQKQRVAIAGVLALNPSVIILDEATSMLDP 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499189069 175 THQIEILDLLFELNEKEDRTIVMVLHDLNLACRyAHHLVAIKDKRIYAEGRPEEVITC 232
Cdd:PRK13648 176 DARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
15-220 |
1.80e-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: 115.81 E-value: 1.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 15 YGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKE-----VAKELAILPQgps 89
Cdd:cd03301 10 FGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDrdiamVFQNYALYPH--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 90 apegLTVhqlvkqgrypYQNW-----LKQWSKED-EEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDII 163
Cdd:cd03301 87 ----MTV----------YDNIafglkLRKVPKDEiDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVF 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499189069 164 LLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRI 220
Cdd:cd03301 153 LMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
9-229 |
2.31e-31 |
|
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: 116.09 E-value: 2.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 9 ETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKE-VAKELAILPQG 87
Cdd:TIGR03410 4 SNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHErARAGIAYVPQG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 88 PSAPEGLTVHQLVKQGRYPyqnwLKQWSKE-DEEAVER--ALKatkleDMADRAVDSLSGGQRQRAWIAMTLAQETDIIL 164
Cdd:TIGR03410 84 REIFPRLTVEENLLTGLAA----LPRRSRKiPDEIYELfpVLK-----EMLGRRGGDLSGGQQQQLAIARALVTRPKLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499189069 165 LDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEV 229
Cdd:TIGR03410 155 LDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
5-229 |
2.47e-31 |
|
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: 116.28 E-value: 2.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 5 AISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEvaKELAIL 84
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 85 PQGPSAPEGLTVHQLVKQGRYPYQNWLKQWSKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIIL 164
Cdd:cd03296 80 FQHYALFRHMTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499189069 165 LDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEV 229
Cdd:cd03296 160 LDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
23-229 |
2.63e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 117.43 E-value: 2.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 23 ELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIA------KLptKEVAKELAILPQGPSapegltv 96
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkknkKL--KPLRKKVGIVFQFPE------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 97 HQLV-----KQGRYPYQNWlkqwSKEDEEAVERALKATKL----EDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDE 167
Cdd:PRK13634 96 HQLFeetveKDICFGPMNF----GVSEEDAKQKAREMIELvglpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499189069 168 PTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEV 229
Cdd:PRK13634 172 PTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
24-224 |
3.17e-31 |
|
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: 115.28 E-value: 3.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 24 LNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEvaKELAILPQGPSAPEGLTVHQLVKQG 103
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSMLFQENNLFAHLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 104 RYPYqnwLKqWSKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDL 183
Cdd:cd03298 95 LSPG---LK-LTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499189069 184 LFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEG 224
Cdd:cd03298 171 VLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-201 |
4.95e-31 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 116.11 E-value: 4.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 3 MSAISTETLSLGYGDAV----IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIaklptkeva 78
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 79 kelailpQGPSAPEGLtVHQlvKQGRYPYQN---------WLKQWSKEDEEAV-ERALKATKLEDMADRAVDSLSGGQRQ 148
Cdd:COG4525 72 -------TGPGADRGV-VFQ--KDALLPWLNvldnvafglRLRGVPKAERRARaEELLALVGLADFARRRIWQLSGGMRQ 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499189069 149 RAWIAMTLAQETDIILLDEPTTYLD-MTHQiEILDLLFELNEKEDRTIVMVLHD 201
Cdd:COG4525 142 RVGIARALAADPRFLLMDEPFGALDaLTRE-QMQELLLDVWQRTGKGVFLITHS 194
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
3-231 |
2.76e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 114.51 E-value: 2.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 3 MSAISTETLSLGY-GDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKEL 81
Cdd:PRK13652 1 MHLIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 82 AILPQGPS----APeglTVHQLVKQGryPYQNWLkqwskeDEEA----VERALKATKLEDMADRAVDSLSGGQRQRAWIA 153
Cdd:PRK13652 81 GLVFQNPDdqifSP---TVEQDIAFG--PINLGL------DEETvahrVSSALHMLGLEELRDRVPHHLSGGEKKRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499189069 154 MTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEVIT 231
Cdd:PRK13652 150 GVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFL 227
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-240 |
2.84e-30 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 114.59 E-value: 2.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 1 MGMSAISTETLSLGYGDA-VIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVllegrAIAKLPTKEVAK 79
Cdd:PRK15056 2 MQQAGIVVNDVTVTWRNGhTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKI-----SILGQPTRQALQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 80 E--LAILPQGP----SAPegLTVHQLVKQGRYPYQNWLKQWSKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIA 153
Cdd:PRK15056 77 KnlVAYVPQSEevdwSFP--VLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 154 MTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEkEDRTIVMVLHDLNLACRYAHHLVAIKDKrIYAEGRPEEVITCD 233
Cdd:PRK15056 155 RAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRD-EGKTMLVSTHNLGSVTEFCDYTVMVKGT-VLASGPTETTFTAE 232
|
....*..
gi 499189069 234 LVQNVFS 240
Cdd:PRK15056 233 NLELAFS 239
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
15-229 |
3.87e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 114.44 E-value: 3.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 15 YGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIaklpTKEVAKELAILpqgpsaPE-- 92
Cdd:COG4152 11 FGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL----DPEDRRRIGYL------PEer 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 93 GL----TV-HQLVKQGRypyqnwLKQWSKED-EEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLD 166
Cdd:COG4152 81 GLypkmKVgEQLVYLAR------LKGLSKAEaKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499189069 167 EPTTYLDMTHQIEILDLLFELNEKeDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEV 229
Cdd:COG4152 155 EPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
6-248 |
6.64e-30 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 113.34 E-value: 6.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARL--MKPRG---GSVLLEGRAI--AKLPTKEVA 78
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGFrveGKVTFHGKNLyaPDVDPVEVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 79 KELAILPQGPSaPEGLTVHQLVKQGryPYQNWLKqwsKEDEEAVERALKATKLED-MADRAVDS---LSGGQRQRAWIAM 154
Cdd:PRK14243 91 RRIGMVFQKPN-PFPKSIYDNIAYG--ARINGYK---GDMDELVERSLRQAALWDeVKDKLKQSglsLSGGQQQRLCIAR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 155 TLAQETDIILLDEPTTYLDMTHQIEILDLLFELneKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEVITCDL 234
Cdd:PRK14243 165 AIAVQPEVILMDEPCSALDPISTLRIEELMHEL--KEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGGRYGYLVEFDR 242
|
250
....*....|....*
gi 499189069 235 VQNVF-SMNCQVTQD 248
Cdd:PRK14243 243 TEKIFnSPQQQATRD 257
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
20-222 |
8.24e-30 |
|
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: 111.67 E-value: 8.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 20 IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAK----ELAILPQ------GPS 89
Cdd:TIGR02211 20 VLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKlrnkKLGFIYQfhhllpDFT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 90 APEGLTVHQLVKqgrypyqnwlKQWSKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPT 169
Cdd:TIGR02211 100 ALENVAMPLLIG----------KKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499189069 170 TYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVaIKDKRIYA 222
Cdd:TIGR02211 170 GNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLE-MKDGQLFN 221
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-224 |
8.68e-30 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 111.60 E-value: 8.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIaklpTKEVAKELAILP 85
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL----DIAARNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 86 QgpsaPEGL-----TVHQLVKQGRypyqnwLKQWSKED-EEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQE 159
Cdd:cd03269 77 E----ERGLypkmkVIDQLVYLAQ------LKGLKKEEaRRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499189069 160 TDIILLDEPTTYLDMTHQIEILDLLFELNEKEdRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEG 224
Cdd:cd03269 147 PELLILDEPFSGLDPVNVELLKDVIRELARAG-KTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
6-202 |
1.70e-29 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 116.31 E-value: 1.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGY-GDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAIL 84
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 85 PQGPSApEGLTVHQLVKQGRypyqnwlkqwSKEDEEAVERALKATKLEDMADRAVD-----------SLSGGQRQRAWIA 153
Cdd:TIGR02868 415 AQDAHL-FDTTVRENLRLAR----------PDATDEELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALA 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499189069 154 MTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEKedRTIVMVLHDL 202
Cdd:TIGR02868 484 RALLADAPILLLDEPTEHLDAETADELLEDLLAALSG--RTVVLITHHL 530
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
15-231 |
2.24e-29 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 111.34 E-value: 2.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 15 YGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEG------RAIAKLPTKE---VAKELAILP 85
Cdd:PRK09493 11 FGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkvndpKVDERLIRQEagmVFQQFYLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 86 QgpsapegLTVHQLVKQGryPYQnwLKQWSKEDEEAVERALKA-TKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIIL 164
Cdd:PRK09493 91 H-------LTALENVMFG--PLR--VRGASKEEAEKQARELLAkVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLML 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499189069 165 LDEPTTYLDMTHQIEILDLLFELNEkEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEVIT 231
Cdd:PRK09493 160 FDEPTSALDPELRHEVLKVMQDLAE-EGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIK 225
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-215 |
2.83e-29 |
|
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: 115.85 E-value: 2.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 4 SAISTETLSLGYGDA-VIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELA 82
Cdd:TIGR02857 320 SSLEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 83 ILPQGPSAPEGlTVHQLVKQGRyPYQnwlkqwskeDEEAVERALKATKLEDMA-------DRAVDS----LSGGQRQRAW 151
Cdd:TIGR02857 400 WVPQHPFLFAG-TIAENIRLAR-PDA---------SDAEIREALERAGLDEFVaalpqglDTPIGEggagLSGGQAQRLA 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499189069 152 IAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELneKEDRTIVMVLHDLNLACRyAHHLVAI 215
Cdd:TIGR02857 469 LARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL--AQGRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
21-229 |
5.44e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 111.29 E-value: 5.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 21 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIA--KLPTKEVAKELAILPQGPSapegltvHQ 98
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIRKKVGLVFQYPE-------YQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 99 LVKQGRY------PYQNWLKQwsKEDEEAVERALKATKL--EDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTT 170
Cdd:PRK13637 96 LFEETIEkdiafgPINLGLSE--EEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499189069 171 YLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEV 229
Cdd:PRK13637 174 GLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
9-230 |
6.22e-29 |
|
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: 109.73 E-value: 6.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 9 ETLSLGYGDAVIiDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEvaKELAILPQGP 88
Cdd:cd03299 4 ENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK--RDISYVPQNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 89 SAPEGLTVHQLVKQGrypyQNWLKQWSKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEP 168
Cdd:cd03299 81 ALFPHMTVYKNIAYG----LKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499189069 169 TTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEVI 230
Cdd:cd03299 157 FSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
21-229 |
1.27e-28 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 112.24 E-value: 1.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 21 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKE-----VAKELAILPQgpsapegLT 95
Cdd:PRK11607 35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQrpinmMFQSYALFPH-------MT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 96 VHQLV----KQGRYPyqnwlkqwSKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTY 171
Cdd:PRK11607 108 VEQNIafglKQDKLP--------KAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499189069 172 LDMT----HQIEILDLLfelnEKEDRTIVMVLHDLNLACRYAHHlVAIKDKRIYAE-GRPEEV 229
Cdd:PRK11607 180 LDKKlrdrMQLEVVDIL----ERVGVTCVMVTHDQEEAMTMAGR-IAIMNRGKFVQiGEPEEI 237
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
18-229 |
1.38e-28 |
|
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: 113.63 E-value: 1.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 18 AViiDELNLTIPKGEiTVFI-GSNGCGKSTLLRSLARLMkPRGGSVLLEGRAIAKLPTKE---VAKELAILPQGPSA--- 90
Cdd:COG4172 301 AV--DGVSLTLRRGE-TLGLvGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRAlrpLRRRMQVVFQDPFGsls 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 91 P---------EGLTVHQLvkqgrypyqnwlkQWSKED-EEAVERALKATKL-EDMADRAVDSLSGGQRQRAWIAMTLAQE 159
Cdd:COG4172 377 PrmtvgqiiaEGLRVHGP-------------GLSAAErRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILE 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499189069 160 TDIILLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLAcRY-AHHLVAIKDKRIYAEGRPEEV 229
Cdd:COG4172 444 PKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVV-RAlAHRVMVMKDGKVVEQGPTEQV 513
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
16-231 |
2.00e-28 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 110.94 E-value: 2.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 16 GDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVA---KELAILPQGPSAPE 92
Cdd:COG1135 16 GPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRaarRKIGMIFQHFNLLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 93 GLTVHQLVkqgRYPyqnwLKQ--WSKEDEEA-VERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPT 169
Cdd:COG1135 96 SRTVAENV---ALP----LEIagVPKAEIRKrVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499189069 170 TYLD--MTHQieILDLLFELNEKEDRTIVMVLHDLNLACRYAHHlVAIKDK-RIYAEGRPEEVIT 231
Cdd:COG1135 169 SALDpeTTRS--ILDLLKDINRELGLTIVLITHEMDVVRRICDR-VAVLENgRIVEQGPVLDVFA 230
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-231 |
2.09e-28 |
|
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: 113.24 E-value: 2.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 1 MGMSAISTETLSLGYGDA----VIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPR----GGSVLLEGRAIAKL 72
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQGggtvEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPaahpSGSILFDGQDLLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 73 PTKEVAK----ELAILPQGP-SA--P---------EGLTVHQLVKqgrypyqnwlkqwskeDEEAVERA---LKATKLED 133
Cdd:COG4172 82 SERELRRirgnRIAMIFQEPmTSlnPlhtigkqiaEVLRLHRGLS----------------GAAARARAlelLERVGIPD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 134 MADRaVDS----LSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYA 209
Cdd:COG4172 146 PERR-LDAyphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFA 224
|
250 260
....*....|....*....|..
gi 499189069 210 HHLVAIKDKRIYAEGRPEEVIT 231
Cdd:COG4172 225 DRVAVMRQGEIVEQGPTAELFA 246
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
11-230 |
2.72e-28 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 113.34 E-value: 2.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 11 LSLGY-GDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAILPQGPS 89
Cdd:COG1132 345 VSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTF 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 90 apegL---TVHQLVKQGRypyqnwlkqwSKEDEEAVERALKATKLEDM------------ADRAVdSLSGGQRQRAWIAM 154
Cdd:COG1132 425 ----LfsgTIRENIRYGR----------PDATDEEVEEAAKAAQAHEFiealpdgydtvvGERGV-NLSGGQRQRIAIAR 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499189069 155 TLAQETDIILLDEPTTYLDMTHQIEILDLLFELneKEDRTIVMVLHDLNlACRYAHHLVAIKDKRIYAEGRPEEVI 230
Cdd:COG1132 490 ALLKDPPILILDEATSALDTETEALIQEALERL--MKGRTTIVIAHRLS-TIRNADRILVLDDGRIVEQGTHEELL 562
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
24-244 |
3.32e-28 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 108.10 E-value: 3.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 24 LNLTIPKGEITVFIGSNGCGKSTLLRSLARLMkPRGGSVLLEGRAIAKLPTKEVAKELAILPQGPSAPEGLTVHQLVKQG 103
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 104 RYPYQNwlkqwSKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQ-------ETDIILLDEPTTYLDMTH 176
Cdd:PRK03695 94 QPDKTR-----TEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDVAQ 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499189069 177 QIeILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEVITCDLVQNVFSMNCQ 244
Cdd:PRK03695 169 QA-ALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVFGVNFR 235
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
9-203 |
7.58e-28 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 106.41 E-value: 7.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 9 ETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPR---GGSVLLEGRAIAKLPTKevAKELAILP 85
Cdd:COG4136 5 ENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAE--QRRIGILF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 86 QGPSAPEGLTVhqlvkqgrypYQNWL----KQWSKED-EEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQET 160
Cdd:COG4136 83 QDDLLFPHLSV----------GENLAfalpPTIGRAQrRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499189069 161 DIILLDEPTTYLDMTHQIEILDLLFElnEKEDRTI--VMVLHDLN 203
Cdd:COG4136 153 RALLLDEPFSKLDAALRAQFREFVFE--QIRQRGIpaLLVTHDEE 195
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-224 |
1.13e-27 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 105.09 E-value: 1.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYG--DAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLpTKEVAKELAI 83
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL-EKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 84 LPQGPsapegltvhqlvkqgrYPYQnwlkqwskedeeaveralkATKLEDMADRavdsLSGGQRQRAWIAMTLAQETDII 163
Cdd:cd03247 80 LNQRP----------------YLFD-------------------TTLRNNLGRR----FSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499189069 164 LLDEPTTYLDMTHQIEILDLLFElnEKEDRTIVMVLHDLnLACRYAHHLVAIKDKRIYAEG 224
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFE--VLKDKTLIWITHHL-TGIEHMDKILFLENGKIIMQG 178
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
11-174 |
1.53e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 110.92 E-value: 1.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 11 LSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAiaklptkevakELAILPQGPSA 90
Cdd:COG0488 4 LSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL-----------RIGYLPQEPPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 91 PEGLTVHQLVKQGRYPYQNWLKQWSK-----EDEEA-----------------------VERALKATKL-EDMADRAVDS 141
Cdd:COG0488 73 DDDLTVLDTVLDGDAELRALEAELEEleaklAEPDEdlerlaelqeefealggweaearAEEILSGLGFpEEDLDRPVSE 152
|
170 180 190
....*....|....*....|....*....|...
gi 499189069 142 LSGGQRQRAWIAMTLAQETDIILLDEPTTYLDM 174
Cdd:COG0488 153 LSGGWRRRVALARALLSEPDLLLLDEPTNHLDL 185
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-229 |
2.73e-27 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 108.50 E-value: 2.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 1 MGMSAISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKE---- 76
Cdd:PRK09452 10 SLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENrhvn 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 77 -VAKELAILPQgpsapegLTVHQLVKQGrypyqnwL---KQWSKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWI 152
Cdd:PRK09452 90 tVFQSYALFPH-------MTVFENVAFG-------LrmqKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 153 AMTLAQETDIILLDEPTTYLD------MthQIEILDLLFELNekedRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRP 226
Cdd:PRK09452 156 ARAVVNKPKVLLLDESLSALDyklrkqM--QNELKALQRKLG----ITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTP 229
|
...
gi 499189069 227 EEV 229
Cdd:PRK09452 230 REI 232
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-224 |
4.22e-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: 104.22 E-value: 4.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLptKEVAKELAILP 85
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKN--IEALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 86 QGP------SAPEGLTVHQLVKQGRYpyqnwlkqwskedeEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQE 159
Cdd:cd03268 79 EAPgfypnlTARENLRLLARLLGIRK--------------KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGN 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499189069 160 TDIILLDEPTTYLDMTHQIEILDLLFELNeKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEG 224
Cdd:cd03268 145 PDLLILDEPTNGLDPDGIKELRELILSLR-DQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
23-220 |
6.05e-27 |
|
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: 104.17 E-value: 6.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 23 ELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEvaKELAILPQGPSAPEGLTVHQLVKQ 102
Cdd:TIGR01277 16 EFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQ--RPVSMLFQENNLFAHLTVRQNIGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 103 GRYPYqnwLKqWSKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILD 182
Cdd:TIGR01277 94 GLHPG---LK-LNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLA 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 499189069 183 LLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRI 220
Cdd:TIGR01277 170 LVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-220 |
9.18e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 108.61 E-value: 9.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLeGRAIaklptkevakELAILP 85
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------KIGYFD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 86 QGPSA-PEGLTVHQlvkqgrypyqnWLKQWSKEDEEAVERALkatkLE------DMADRAVDSLSGGQRQRAWIAMTLAQ 158
Cdd:COG0488 385 QHQEElDPDKTVLD-----------ELRDGAPGGTEQEVRGY----LGrflfsgDDAFKPVGVLSGGEKARLALAKLLLS 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499189069 159 ETDIILLDEPTTYLDmthqIEILDLLFELNEKEDRTIVMVLHDlnlacRY-----AHHLVAIKDKRI 220
Cdd:COG0488 450 PPNVLLLDEPTNHLD----IETLEALEEALDDFPGTVLLVSHD-----RYfldrvATRILEFEDGGV 507
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
11-230 |
1.28e-26 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 107.04 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 11 LSLGYGDAviidelNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVA----KELAILPQ 86
Cdd:PRK10070 40 LSLGVKDA------SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 87 GPSAPEGLTVHQLVKQGrypyQNWLKQWSKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLD 166
Cdd:PRK10070 114 SFALMPHMTVLDNTAFG----MELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMD 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499189069 167 EPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEVI 230
Cdd:PRK10070 190 EAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
21-224 |
1.62e-26 |
|
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: 103.05 E-value: 1.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 21 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAILPQGPSAPEGlTVHQLV 100
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQDVTLFYG-TLRDNI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 101 KQGRyPYQnwlkqwskeDEEAVERALKATKLEDMA-------DRAV----DSLSGGQRQRAWIAMTLAQETDIILLDEPT 169
Cdd:cd03245 99 TLGA-PLA---------DDERILRAAELAGVTDFVnkhpnglDLQIgergRGLSGGQRQAVALARALLNDPPILLLDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499189069 170 TYLDMTHQIEILDLLFELneKEDRTIVMVLHD---LNLACRyahhLVAIKDKRIYAEG 224
Cdd:cd03245 169 SAMDMNSEERLKERLRQL--LGDKTLIIITHRpslLDLVDR----IIVMDSGRIVADG 220
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
18-203 |
5.00e-26 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 104.04 E-value: 5.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 18 AViiDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVA---KELAILPQGPSA---P 91
Cdd:COG4608 33 AV--DGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRplrRRMQMVFQDPYAslnP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 92 ---------EGLTVHQLVKQgrypyqnwlkqwsKEDEEAVERALKATKL-EDMADRAVDSLSGGQRQRAWIAMTLAQETD 161
Cdd:COG4608 111 rmtvgdiiaEPLRIHGLASK-------------AERRERVAELLELVGLrPEHADRYPHEFSGGQRQRIGIARALALNPK 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499189069 162 IILLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLN 203
Cdd:COG4608 178 LIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLS 219
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
3-226 |
5.50e-26 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 102.84 E-value: 5.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 3 MSAISTETLSLGYGDA---------VIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLp 73
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGglsgkhqhqTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 74 TKEVAKEL-----AILPQGPSA--PEGlTVHQLVkqgRYPYQNWLKQWSKEDEEAVERALKATKLED-MADRAVDSLSGG 145
Cdd:PRK10419 80 NRAQRKAFrrdiqMVFQDSISAvnPRK-TVREII---REPLRHLLSLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 146 QRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIyAEGR 225
Cdd:PRK10419 156 QLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI-VETQ 234
|
.
gi 499189069 226 P 226
Cdd:PRK10419 235 P 235
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-236 |
6.35e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 103.73 E-value: 6.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 1 MGMSAISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKlPTKEVAKE 80
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 81 LAILPQGPSAPEGLTVHQ-LVKQGRYpyqnwLKQWSKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQE 159
Cdd:PRK13537 82 VGVVPQFDNLDPDFTVREnLLVFGRY-----FGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVND 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 160 TDIILLDEPTTYLDMTHQIEILDLLFELNEKeDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEVIT----CDLV 235
Cdd:PRK13537 157 PDVLVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIEseigCDVI 235
|
.
gi 499189069 236 Q 236
Cdd:PRK13537 236 E 236
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
6-230 |
1.08e-25 |
|
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: 101.15 E-value: 1.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDAV--IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAI 83
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 84 LPQGPSAPEGlTVHQLVKQGRypyqnwlkqwSKEDEEAVERALKA-------TKLED-----MADRAVdSLSGGQRQRAW 151
Cdd:cd03251 81 VSQDVFLFND-TVAENIAYGR----------PGATREEVEEAARAanahefiMELPEgydtvIGERGV-KLSGGQRQRIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499189069 152 IAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELneKEDRTIVMVLHDLNlACRYAHHLVAIKDKRIYAEGRPEEVI 230
Cdd:cd03251 149 IARALLKDPPILILDEATSALDTESERLVQAALERL--MKNRTTFVIAHRLS-TIENADRIVVLEDGKIVERGTHEELL 224
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
6-224 |
1.27e-25 |
|
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: 100.52 E-value: 1.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDA----VIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPtKEVAKEL 81
Cdd:cd03266 2 ITADALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEP-AEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 82 AILPQGPSAPEGLTVHQLVkqGRYPYQNWLKQwsKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETD 161
Cdd:cd03266 81 GFVSDSTGLYDRLTARENL--EYFAGLYGLKG--DELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499189069 162 IILLDEPTTYLDMTHQIEILDLLFELNEkEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEG 224
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQLRA-LGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
16-223 |
2.10e-25 |
|
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: 101.42 E-value: 2.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 16 GDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKL---PTKEVAKELAILPQ-GPSA- 90
Cdd:TIGR02769 22 QRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdrkQRRAFRRDVQLVFQdSPSAv 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 91 -PEgLTVHQLVKQgryPYQNWLKQWSKEDEEAVERALKATKLE-DMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEP 168
Cdd:TIGR02769 102 nPR-MTVRQIIGE---PLRHLTSLDESEQKARIAELLDMVGLRsEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499189069 169 TTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAE 223
Cdd:TIGR02769 178 VSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEE 232
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-229 |
2.21e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 101.42 E-value: 2.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 1 MGMSAISTETLSLGYGDA--VIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGS---VLLEGRAIAKLPTK 75
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPDSkkPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 76 EVAKELAILPQGPSAP-EGLTVHQLVKQG----RYPYQNWLKqwskedeeAVERALKATKLEDMADRAVDSLSGGQRQRA 150
Cdd:PRK13640 81 DIREKVGIVFQNPDNQfVGATVGDDVAFGlenrAVPRPEMIK--------IVRDVLADVGMLDYIDSEPANLSGGQKQRV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499189069 151 WIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLAcRYAHHLVAIKDKRIYAEGRPEEV 229
Cdd:PRK13640 153 AIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEI 230
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
21-230 |
2.80e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 101.70 E-value: 2.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 21 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSV--LLEGRAIAKLP-TKEVAKELAILpQGPSAPEGLTVH 97
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewIFKDEKNKKKTkEKEKVLEKLVI-QKTRFKKIKKIK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 98 QLVKQGRYPYQ----NWLKQWSKED------------EEAVERALKATKL----EDMADRAVDSLSGGQRQRAWIAMTLA 157
Cdd:PRK13651 102 EIRRRVGVVFQfaeyQLFEQTIEKDiifgpvsmgvskEEAKKRAAKYIELvgldESYLQRSPFELSGGQKRRVALAGILA 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499189069 158 QETDIILLDEPTTYLDMTHQIEILDLLFELNeKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEVI 230
Cdd:PRK13651 182 MEPDFLVFDEPTAGLDPQGVKEILEIFDNLN-KQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDIL 253
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
6-230 |
2.86e-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: 100.00 E-value: 2.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDAV-IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAIL 84
Cdd:cd03253 1 IEFENVTFAYDPGRpVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 85 PQGPSapegL---TVHQLVKQGRypyqnwlkqWSKEDEEaVERALKATKLEDMADRAVDS-----------LSGGQRQRA 150
Cdd:cd03253 81 PQDTV----LfndTIGYNIRYGR---------PDATDEE-VIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 151 WIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELneKEDRTIVMVLHDLNLACRyAHHLVAIKDKRIYAEGRPEEVI 230
Cdd:cd03253 147 AIARAILKNPPILLLDEATSALDTHTEREIQAALRDV--SKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELL 223
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
6-231 |
3.37e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 100.83 E-value: 3.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDAV-IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGR---AIAKLPtkEVAKEL 81
Cdd:PRK13644 2 IRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIdtgDFSKLQ--GIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 82 AILPQGPSAP-EGLTVHQLVKQGryPYQNWLKqwSKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQET 160
Cdd:PRK13644 80 GIVFQNPETQfVGRTVEEDLAFG--PENLCLP--PIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499189069 161 DIILLDEPTTYLDMTHQIEILDLLFELNEKeDRTIVMVLHDLNlACRYAHHLVAIKDKRIYAEGRPEEVIT 231
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
11-229 |
4.18e-25 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 100.06 E-value: 4.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 11 LSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVA------------ 78
Cdd:PRK11300 11 LMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIArmgvvrtfqhvr 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 79 --KELAILpqgpsapEGLTV--HQLVKQGRYPYQNWLKQWSKEDEEAVERA---LKATKLEDMADRAVDSLSGGQRQRAW 151
Cdd:PRK11300 91 lfREMTVI-------ENLLVaqHQQLKTGLFSGLLKTPAFRRAESEALDRAatwLERVGLLEHANRQAGNLAYGQQRRLE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499189069 152 IAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEV 229
Cdd:PRK11300 164 IARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 241
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
5-224 |
5.52e-25 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 99.70 E-value: 5.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 5 AISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVllegraiaklptkEVAKELAIL 84
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTL-------------NIAGNHFDF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 85 PQGPSAPEGLTVHQLVKQGRYPYQNW-------------LKQWSKEDEEAVERA---LKATKLEDMADRAVDSLSGGQRQ 148
Cdd:PRK11124 69 SKTPSDKAIRELRRNVGMVFQQYNLWphltvqqnlieapCRVLGLSKDQALARAeklLERLRLKPYADRFPLHLSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499189069 149 RAWIAMTLAQETDIILLDEPTTYLD--MTHQieILDLLFELNEKeDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEG 224
Cdd:PRK11124 149 RVAIARALMMEPQVLLFDEPTAALDpeITAQ--IVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
3-228 |
5.92e-25 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 102.03 E-value: 5.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 3 MSAISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKE-----V 77
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAErgvgmV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 78 AKELAILPQgpsapegLTVHQLVKQGrypyqnwLKQWSKEDEEA---VERALKATKLEDMADRAVDSLSGGQRQRAWIAM 154
Cdd:PRK11000 81 FQSYALYPH-------LSVAENMSFG-------LKLAGAKKEEInqrVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499189069 155 TLAQETDIILLDEPTTYLD----MTHQIEILdllfELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEE 228
Cdd:PRK11000 147 TLVAEPSVFLLDEPLSNLDaalrVQMRIEIS----RLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLE 220
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
16-220 |
6.54e-25 |
|
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: 98.63 E-value: 6.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 16 GDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAK---ELAILPQGPSAPE 92
Cdd:cd03292 12 NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYlrrKIGVVFQDFRLLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 93 GLTVHQLVKQGRYPYQNWLKQWSKEdeeaVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYL 172
Cdd:cd03292 92 DRNVYENVAFALEVTGVPPREIRKR----VPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499189069 173 DMTHQIEILDLLFELNeKEDRTIVMVLHDLNLACRYAHHLVAIKDKRI 220
Cdd:cd03292 168 DPDTTWEIMNLLKKIN-KAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
15-228 |
8.59e-25 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 101.33 E-value: 8.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 15 YGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKE-----VAKELAILPQ--- 86
Cdd:PRK11432 16 FGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQrdicmVFQSYALFPHmsl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 87 GPSAPEGLTVhqlvkQGRypyqnwlkqwSKED-EEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILL 165
Cdd:PRK11432 96 GENVGYGLKM-----LGV----------PKEErKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499189069 166 DEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEE 228
Cdd:PRK11432 161 DEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQE 223
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
6-229 |
9.56e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 99.78 E-value: 9.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDA------VIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGraiakLPTK---- 75
Cdd:PRK13633 5 IKCKNVSYKYESNeestekLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG-----LDTSdeen 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 76 --EVAKELAILPQGPS--------------APEGLTVHQlvkqgrypyqnwlkqwsKEDEEAVERALKATKLEDMADRAV 139
Cdd:PRK13633 80 lwDIRNKAGMVFQNPDnqivativeedvafGPENLGIPP-----------------EEIRERVDESLKKVGMYEYRRHAP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 140 DSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRyAHHLVAIKDKR 219
Cdd:PRK13633 143 HLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGK 221
|
250
....*....|
gi 499189069 220 IYAEGRPEEV 229
Cdd:PRK13633 222 VVMEGTPKEI 231
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
17-230 |
9.78e-25 |
|
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: 98.77 E-value: 9.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 17 DAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAILPQGPSAPEGlTV 96
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLFDG-TI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 97 HQLVKQGRYPyqnwlkqwsKEDEEAVERALKA------TKLED-----MADRAVdSLSGGQRQRAWIAMTLAQETDIILL 165
Cdd:cd03249 94 AENIRYGKPD---------ATDEEVEEAAKKAnihdfiMSLPDgydtlVGERGS-QLSGGQKQRIAIARALLRNPKILLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499189069 166 DEPTTYLDMTHQIEILDLLFELneKEDRTIVMVLHDLNlACRYAHHLVAIKDKRIYAEGRPEEVI 230
Cdd:cd03249 164 DEATSALDAESEKLVQEALDRA--MKGRTTIVIAHRLS-TIRNADLIAVLQNGQVVEQGTHDELM 225
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-239 |
1.01e-24 |
|
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: 98.77 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKeLAI-- 83
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRAR-LGIgy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 84 LPQGPSAPEGLTVHQ---LVKQGRYPYqnwlkqwSKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQET 160
Cdd:cd03218 80 LPQEASIFRKLTVEEnilAVLEIRGLS-------KKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 161 DIILLDEPTTYLDMTHQIEILDLLFELNekeDRTIVMVLHDLNlacryAHHLVAIKDK-------RIYAEGRPEEVITCD 233
Cdd:cd03218 153 KFLLLDEPFAGVDPIAVQDIQKIIKILK---DRGIGVLITDHN-----VRETLSITDRayiiyegKVLAEGTPEEIAANE 224
|
....*.
gi 499189069 234 LVQNVF 239
Cdd:cd03218 225 LVRKVY 230
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
3-224 |
1.12e-24 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 98.93 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 3 MSaISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVllegraiaklptkEVAKELA 82
Cdd:COG4161 1 MS-IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQL-------------NIAGHQF 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 83 ILPQGPSAPEGLTVHQLVKQGRYPYQNW----------------LKQwSKEdeEAVERA---LKATKLEDMADRAVDSLS 143
Cdd:COG4161 67 DFSQKPSEKAIRLLRQKVGMVFQQYNLWphltvmenlieapckvLGL-SKE--QAREKAmklLARLRLTDKADRFPLHLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 144 GGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEKEdRTIVMVLHDLNLACRYAHHLVAIKDKRIYAE 223
Cdd:COG4161 144 GGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTG-ITQVIVTHEVEFARKVASQVVYMEKGRIIEQ 222
|
.
gi 499189069 224 G 224
Cdd:COG4161 223 G 223
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-224 |
1.24e-24 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 99.32 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 4 SAISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLM---KPRGGSVLLEGRAI------AKLPT 74
Cdd:PRK09984 3 TIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVqregrlARDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 75 KEVAKELAILPQGpSAPEGLTVHQLV---KQGRYPYQNWLKQW-SKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRA 150
Cdd:PRK09984 83 KSRANTGYIFQQF-NLVNRLSVLENVligALGSTPFWRTCFSWfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499189069 151 WIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEG 224
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDG 235
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
15-220 |
1.31e-24 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 98.98 E-value: 1.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 15 YGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSvLLEGRAI---AKLPTKEVAKELAILPQGpsap 91
Cdd:PRK11247 22 YGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-LLAGTAPlaeAREDTRLMFQDARLLPWK---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 92 eglTVHQLVKQGrypyqnwLK-QWskedEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTT 170
Cdd:PRK11247 97 ---KVIDNVGLG-------LKgQW----RDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 499189069 171 YLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRI 220
Cdd:PRK11247 163 ALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-213 |
1.75e-24 |
|
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: 98.25 E-value: 1.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 27 TIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKevakelaILPQGPSAPEGLTVHQLVKQGRYP 106
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQY-------IKADYEGTVRDLLSSITKDFYTHP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 107 YqnwlkqWSKEdeeaverALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFE 186
Cdd:cd03237 94 Y------FKTE-------IAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRR 160
|
170 180
....*....|....*....|....*..
gi 499189069 187 LNEKEDRTIVMVLHDLNLACRYAHHLV 213
Cdd:cd03237 161 FAENNEKTAFVVEHDIIMIDYLADRLI 187
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-231 |
2.04e-24 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 97.73 E-value: 2.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 25 NLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEvaKELAILPQGPSAPEGLTVHQLVKQGR 104
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR--RPVSMLFQENNLFSHLTVAQNIGLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 105 YPyqnWLKqWSKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLL 184
Cdd:PRK10771 97 NP---GLK-LNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499189069 185 FELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEVIT 231
Cdd:PRK10771 173 SQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
22-240 |
2.70e-24 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 99.88 E-value: 2.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 22 DELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKE---LAILPQgpsapegltvHQ 98
Cdd:PRK11153 22 NNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKArrqIGMIFQ----------HF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 99 LVKQGRYPYQNW-----LKQWSKEDEEA-VERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYL 172
Cdd:PRK11153 92 NLLSSRTVFDNValpleLAGTPKAEIKArVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSAL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499189069 173 D--MTHQieILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEG-------RPEEVITCDLVQNVFS 240
Cdd:PRK11153 172 DpaTTRS--ILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGtvsevfsHPKHPLTREFIQSTLH 246
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-220 |
3.58e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 97.85 E-value: 3.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 19 VIIDELNLTIPKGE-ITVfIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAILPQGPS---APeGL 94
Cdd:COG1101 20 RALDGLNLTIEEGDfVTV-IGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVFQDPMmgtAP-SM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 95 TVHQ-----LVKQGRYPYQNWLkqwSKEDEEAVERALKATK--LEDMADRAVDSLSGGQRQrawiAMTLAQET----DII 163
Cdd:COG1101 98 TIEEnlalaYRRGKRRGLRRGL---TKKRRELFRELLATLGlgLENRLDTKVGLLSGGQRQ----ALSLLMATltkpKLL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499189069 164 LLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRI 220
Cdd:COG1101 171 LLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
15-224 |
3.66e-24 |
|
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: 97.40 E-value: 3.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 15 YGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAILPQGP------ 88
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKTqlwwdl 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 89 SAPEGLTVHQL---VKQGRYpyqnwlkqwskedEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILL 165
Cdd:cd03267 111 PVIDSFYLLAAiydLPPARF-------------KKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 499189069 166 DEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEG 224
Cdd:cd03267 178 DEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-236 |
4.42e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 99.13 E-value: 4.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 1 MGMSAISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGraiAKLPTKEVA-- 78
Cdd:PRK13536 37 MSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG---VPVPARARLar 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 79 KELAILPQGPSAPEGLTVHQ-LVKQGRYpyqnwLKQWSKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLA 157
Cdd:PRK13536 114 ARIGVVPQFDNLDLEFTVREnLLVFGRY-----FGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALI 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 158 QETDIILLDEPTTYLDMTHQIEILDLLFELNEKeDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRP----EEVITCD 233
Cdd:PRK13536 189 NDPQLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPhaliDEHIGCQ 267
|
...
gi 499189069 234 LVQ 236
Cdd:PRK13536 268 VIE 270
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
23-229 |
5.49e-24 |
|
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: 99.03 E-value: 5.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 23 ELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAK------LPTKEvaKELAILPQGPSapegLTV 96
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPEK--RRIGYVFQEAR----LFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 97 HQLVKQG-RYPYQNWLKQWSKEDEEAVERALKatkLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMT 175
Cdd:TIGR02142 89 HLSVRGNlRYGMKRARPSERRISFERVIELLG---IGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499189069 176 HQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEV 229
Cdd:TIGR02142 166 RKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-213 |
5.78e-24 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 96.77 E-value: 5.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 21 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKlPTKE---VAKELAILPQgpsapegLTVH 97
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE-PGPDrmvVFQNYSLLPW-------LTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 98 QLVKqgrYPYQNWLKQWSKEDEEA-VERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTH 176
Cdd:TIGR01184 73 ENIA---LAVDRVLPDLSKSERRAiVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180 190
....*....|....*....|....*....|....*..
gi 499189069 177 QIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLV 213
Cdd:TIGR01184 150 RGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVV 186
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
5-231 |
6.82e-24 |
|
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: 100.71 E-value: 6.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 5 AISTETLSLGYGDAVI--IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELA 82
Cdd:TIGR03375 463 EIEFRNVSFAYPGQETpaLDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNIG 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 83 ILPQGPSAPEGlTVHQLVKQGRyPYQnwlkqwskeDEEAVERALKATKLEDMA-------DRAV----DSLSGGQRQRAW 151
Cdd:TIGR03375 543 YVPQDPRLFYG-TLRDNIALGA-PYA---------DDEEILRAAELAGVTEFVrrhpdglDMQIgergRSLSGGQRQAVA 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 152 IAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELneKEDRTIVMVLHD---LNLACRyahhLVAIKDKRIYAEGRPEE 228
Cdd:TIGR03375 612 LARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRW--LAGKTLVLVTHRtslLDLVDR----IIVMDNGRIVADGPKDQ 685
|
...
gi 499189069 229 VIT 231
Cdd:TIGR03375 686 VLE 688
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
6-230 |
1.34e-23 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 95.37 E-value: 1.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDAV-IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAIL 84
Cdd:cd03254 3 IEFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 85 PQGPSAPEGlTVHQLVKQGRypyqnwlkqwSKEDEEAVERALKAT-------KLEDMADRAV----DSLSGGQRQRAWIA 153
Cdd:cd03254 83 LQDTFLFSG-TIMENIRLGR----------PNATDEEVIEAAKEAgahdfimKLPNGYDTVLgengGNLSQGERQLLAIA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499189069 154 MTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNekEDRTIVMVLHDLNlACRYAHHLVAIKDKRIYAEGRPEEVI 230
Cdd:cd03254 152 RAMLRDPKILILDEATSNIDTETEKLIQEALEKLM--KGRTSIIIAHRLS-TIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
11-229 |
1.96e-23 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 95.99 E-value: 1.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 11 LSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTK---EVAKELAILPQG 87
Cdd:PRK11831 13 VSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSrlyTVRKRMSMLFQS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 88 PSAPEGLTVHQLVKqgrYPyqnwLKQWSKEDEE----AVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDII 163
Cdd:PRK11831 93 GALFTDMNVFDNVA---YP----LREHTQLPAPllhsTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499189069 164 LLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEV 229
Cdd:PRK11831 166 MFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
10-230 |
2.03e-23 |
|
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: 99.43 E-value: 2.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 10 TLSLGYGDAvIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAILPQGPS 89
Cdd:TIGR01193 480 SYSYGYGSN-ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPY 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 90 APEGLTVHQLVKQGrypyqnwlKQWSKEDE--EAVERALKATKLEDM-----ADRAVD--SLSGGQRQRAWIAMTLAQET 160
Cdd:TIGR01193 559 IFSGSILENLLLGA--------KENVSQDEiwAACEIAEIKDDIENMplgyqTELSEEgsSISGGQKQRIALARALLTDS 630
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 161 DIILLDEPTTYLDMTHQIEILDLLFELNEKedrTIVMVLHDLNLACRyAHHLVAIKDKRIYAEGRPEEVI 230
Cdd:TIGR01193 631 KVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDELL 696
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
37-229 |
2.90e-23 |
|
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: 96.79 E-value: 2.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 37 IGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKE-----VAKELAILPQgpsapegLTVHQLVKQGrypyqnwL 111
Cdd:TIGR01187 2 LGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLrhinmVFQSYALFPH-------MTVEENVAFG-------L 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 112 KQWSKEDEEAVER---ALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMT----HQIEILDLL 184
Cdd:TIGR01187 68 KMRKVPRAEIKPRvleALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKlrdqMQLELKTIQ 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499189069 185 FELNekedRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEV 229
Cdd:TIGR01187 148 EQLG----ITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
21-229 |
2.99e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 96.00 E-value: 2.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 21 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAI-AKLPTKE---VAKELAILPQGPSApegltv 96
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITItHKTKDKYirpVRKRIGMVFQFPES------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 97 hQLVkqgrypyqnwlkqwskedEEAVERALK------ATKLEDMADRAVDSL-----------------SGGQRQRAWIA 153
Cdd:PRK13646 97 -QLF------------------EDTVEREIIfgpknfKMNLDEVKNYAHRLLmdlgfsrdvmsqspfqmSGGQMRKIAIV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499189069 154 MTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEV 229
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-228 |
3.24e-23 |
|
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: 94.42 E-value: 3.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 4 SAISTETLSLGYGDA----VIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAK 79
Cdd:COG4181 7 PIIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 80 ELA-----------ILPqgpsapeGLTVHQLVK-----QGRypyqnwlkqwsKEDEEAVERALKATKLEDMADRAVDSLS 143
Cdd:COG4181 87 LRArhvgfvfqsfqLLP-------TLTALENVMlplelAGR-----------RDARARARALLERVGLGHRLDHYPAQLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 144 GGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRyAHHLVAIKDKRIYAE 223
Cdd:COG4181 149 GGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVED 227
|
....*
gi 499189069 224 GRPEE 228
Cdd:COG4181 228 TAATA 232
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
15-220 |
3.64e-23 |
|
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: 92.49 E-value: 3.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 15 YGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEvAKELAIlpqgpsapegL 94
Cdd:cd03216 10 FGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD-ARRAGI----------A 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 95 TVHQlvkqgrypyqnwlkqwskedeeaveralkatkledmadravdsLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDm 174
Cdd:cd03216 79 MVYQ-------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALT- 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499189069 175 THQIEIL-DLLFELnEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRI 220
Cdd:cd03216 115 PAEVERLfKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
4-229 |
3.65e-23 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 95.15 E-value: 3.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 4 SAISTETLSLgYGDAVIIDELNLTIPKGEITVFIGSNGCGKStlLRSLARL-MKPRG-----GSVLLEGRAIAklPTKEV 77
Cdd:PRK10418 3 QQIELRNIAL-QAAQPLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALgILPAGvrqtaGRVLLDGKPVA--PCALR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 78 AKELAILPQGP-SA--PegltVHQLVKQGRypyqNWLKQWSKEDEEAV-ERALKATKLEDmADRAVDS----LSGGQRQR 149
Cdd:PRK10418 78 GRKIATIMQNPrSAfnP----LHTMHTHAR----ETCLALGKPADDATlTAALEAVGLEN-AARVLKLypfeMSGGMLQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 150 AWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEV 229
Cdd:PRK10418 149 MMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
16-202 |
3.81e-23 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 96.33 E-value: 3.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 16 GDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRG---GSVLLEGRAIAKLPTKEV----AKELAILPQGP 88
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPEKELnklrAEQISMIFQDP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 89 SAP------------EGLTVHqlvkqgrypyqnwlKQWSKED--EEAVeRALKATKLEDMADRAV---DSLSGGQRQRAW 151
Cdd:PRK09473 107 MTSlnpymrvgeqlmEVLMLH--------------KGMSKAEafEESV-RMLDAVKMPEARKRMKmypHEFSGGMRQRVM 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499189069 152 IAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDL 202
Cdd:PRK09473 172 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDL 222
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
17-200 |
4.15e-23 |
|
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: 94.26 E-value: 4.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 17 DAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRG---GSVLLEGRAIAKlptKEVAKELAILPQGPSAPEG 93
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKP---DQFQKCVAYVRQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 94 LTVHQLVK---QGRYPYQNWLKQWSKEDEEAVERALKatkLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTT 170
Cdd:cd03234 96 LTVRETLTytaILRLPRKSSDAIRKKRVEDVLLRDLA---LTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTS 172
|
170 180 190
....*....|....*....|....*....|
gi 499189069 171 YLDMTHQIEILDLLFELnEKEDRTIVMVLH 200
Cdd:cd03234 173 GLDSFTALNLVSTLSQL-ARRNRIVILTIH 201
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
9-213 |
4.43e-23 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 94.77 E-value: 4.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 9 ETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIaklptkevakelailpQGP 88
Cdd:PRK11248 5 SHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV----------------EGP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 89 SAPEGLTVHQlvkQGRYPYQN---------WLKQWSKEDEEAVER-ALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQ 158
Cdd:PRK11248 69 GAERGVVFQN---EGLLPWRNvqdnvafglQLAGVEKMQRLEIAHqMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAA 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499189069 159 ETDIILLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLV 213
Cdd:PRK11248 146 NPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELV 200
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-202 |
6.53e-23 |
|
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: 94.36 E-value: 6.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 26 LTIPK-GEITVFIGSNGCGKSTLLRSLARLMKPRGGS---------VLLE--GRAIAKLPTKEVAKEL--AILPQG---- 87
Cdd:cd03236 20 LPVPReGQVLGLVGPNGIGKSTALKILAGKLKPNLGKfddppdwdeILDEfrGSELQNYFTKLLEGDVkvIVKPQYvdli 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 88 PSAPEGlTVHQLVKQgrypyqnwlkqwsKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDE 167
Cdd:cd03236 100 PKAVKG-KVGELLKK-------------KDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDE 165
|
170 180 190
....*....|....*....|....*....|....*
gi 499189069 168 PTTYLDMTHQIEILDLLFELNEkEDRTIVMVLHDL 202
Cdd:cd03236 166 PSSYLDIKQRLNAARLIRELAE-DDNYVLVVEHDL 199
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-229 |
1.15e-22 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 93.88 E-value: 1.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 1 MGMSAISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKE---- 76
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDgqlk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 77 ---------VAKELAILPQGPSAPEGLTVHQLVKQGryPYQnwLKQWSKEdeEAVERALKATKLEDMADRAVDS----LS 143
Cdd:PRK10619 81 vadknqlrlLRTRLTMVFQHFNLWSHMTVLENVMEA--PIQ--VLGLSKQ--EARERAVKYLAKVGIDERAQGKypvhLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 144 GGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEkEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAE 223
Cdd:PRK10619 155 GGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAE-EGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEE 233
|
....*.
gi 499189069 224 GRPEEV 229
Cdd:PRK10619 234 GAPEQL 239
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
20-223 |
1.26e-22 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 92.96 E-value: 1.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 20 IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAK----ELAILPQgpsapeglt 95
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAElrnqKLGFIYQ--------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 96 VHQLVkqgryPYQNWLKQWS-------KEDEEAVERA---LKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILL 165
Cdd:PRK11629 95 FHHLL-----PDFTALENVAmplligkKKPAEINSRAlemLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499189069 166 DEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYaHHLVAIKDKRIYAE 223
Cdd:PRK11629 170 DEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTAE 226
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
3-229 |
1.37e-22 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 93.28 E-value: 1.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 3 MSAISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIaklptkEVAKELa 82
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITI------DTARSL- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 83 ilpqgpSAPEGLtVHQLVKQGRYPYQNW------------------LKQWSKEDEEAVERALKA-TKLEDMADRAVDSLS 143
Cdd:PRK11264 74 ------SQQKGL-IRQLRQHVGFVFQNFnlfphrtvleniiegpviVKGEPKEEATARARELLAkVGLAGKETSYPRRLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 144 GGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEkEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAE 223
Cdd:PRK11264 147 GGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQ-EKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQ 225
|
....*.
gi 499189069 224 GRPEEV 229
Cdd:PRK11264 226 GPAKAL 231
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
3-229 |
2.13e-22 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 92.94 E-value: 2.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 3 MSAISTETLSL-----GYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTK-- 75
Cdd:COG4598 1 MTDTAPPALEVrdlhkSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRdg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 76 --EVAK---------ELAILPQGPSAPEGLTVHQLVKQGryPYQnWLKQwSKEdeEAVERA---LKATKLEDMADRAVDS 141
Cdd:COG4598 81 elVPADrrqlqrirtRLGMVFQSFNLWSHMTVLENVIEA--PVH-VLGR-PKA--EAIERAealLAKVGLADKRDAYPAH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 142 LSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEkEDRTIVMVLHDLNLACRYAHHLVAIKDKRIY 221
Cdd:COG4598 155 LSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAE-EGRTMLVVTHEMGFARDVSSHVVFLHQGRIE 233
|
....*...
gi 499189069 222 AEGRPEEV 229
Cdd:COG4598 234 EQGPPAEV 241
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
23-231 |
2.71e-22 |
|
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: 94.40 E-value: 2.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 23 ELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPR------GGSVLLEGRAIAKLPTKevAKELAILPQGPSAPEGLTV 96
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDsgrirlGGEVLQDSARGIFLPPH--RRRIGYVFQEARLFPHLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 97 HQLVkqgRYPYQNWLKQWSKED-EEAVERalkaTKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMT 175
Cdd:COG4148 95 RGNL---LYGRKRAPRAERRISfDEVVEL----LGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499189069 176 HQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEVIT 231
Cdd:COG4148 168 RKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLS 223
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
21-231 |
2.78e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 93.36 E-value: 2.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 21 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAI----AKLPTKEVAKELAILPQGPSAP--EGl 94
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetGNKNLKKLRKKVSLVFQFPEAQlfEN- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 95 TVHQLVKQGryPyqnwlKQWSKEDEEAVERALKATKL----EDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTT 170
Cdd:PRK13641 102 TVLKDVEFG--P-----KNFGFSEDEAKEKALKWLKKvglsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499189069 171 YLDMTHQIEILDlLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEVIT 231
Cdd:PRK13641 175 GLDPEGRKEMMQ-LFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFS 234
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
21-232 |
3.19e-22 |
|
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: 96.24 E-value: 3.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 21 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIaKLPTKEVAKELAILPQgpsapEGLTVHQLV 100
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQ-----HNILFHHLT 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 101 KQGRYPYQNWLKQWSKEDEE-AVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIE 179
Cdd:TIGR01257 1020 VAEHILFYAQLKGRSWEEAQlEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRS 1099
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 499189069 180 ILDLLfeLNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEVITC 232
Cdd:TIGR01257 1100 IWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNC 1150
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
3-229 |
4.16e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 93.65 E-value: 4.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 3 MSAISTETLSLGYGDAVI----IDELNLTIPKGEITVFIGSNGCGKStlLRSLArLM-------KPRGGSVLLEGRAIAK 71
Cdd:PRK11022 1 MALLNVDKLSVHFGDESApfraVDRISYSVKQGEVVGIVGESGSGKS--VSSLA-IMglidypgRVMAEKLEFNGQDLQR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 72 LPTKE----VAKELAILPQGP--SAPEGLTVHQLVKQGRYPYQNWLKQWSKEdeEAVErALKATKLEDMADRaVD----S 141
Cdd:PRK11022 78 ISEKErrnlVGAEVAMIFQDPmtSLNPCYTVGFQIMEAIKVHQGGNKKTRRQ--RAID-LLNQVGIPDPASR-LDvyphQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 142 LSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIY 221
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVV 233
|
....*...
gi 499189069 222 AEGRPEEV 229
Cdd:PRK11022 234 ETGKAHDI 241
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
16-203 |
5.58e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 91.31 E-value: 5.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 16 GDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAILPQGPSApEGLT 95
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTL-FGDT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 96 VHQLVKqgrYPYQnwLKQwSKEDEEAVERALKATKL-EDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDM 174
Cdd:PRK10247 97 VYDNLI---FPWQ--IRN-QQPDPAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDE 170
|
170 180
....*....|....*....|....*....
gi 499189069 175 THQIEILDLLFELNEKEDRTIVMVLHDLN 203
Cdd:PRK10247 171 SNKHNVNEIIHRYVREQNIAVLWVTHDKD 199
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-231 |
1.05e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 91.26 E-value: 1.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 11 LSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMK------PRGGSVLLEGRAIAKLPTKEVAKELAIL 84
Cdd:PRK14246 16 LYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGMV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 85 PQGPSAPEGLTVHQLVKqgrYPYQNWLKQWSKEDEEAVERALKATKL----EDMADRAVDSLSGGQRQRAWIAMTLAQET 160
Cdd:PRK14246 96 FQQPNPFPHLSIYDNIA---YPLKSHGIKEKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKP 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499189069 161 DIILLDEPTTYLDMTHQIEILDLLFELneKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEVIT 231
Cdd:PRK14246 173 KVLLMDEPTSMIDIVNSQAIEKLITEL--KNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFT 241
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-201 |
1.34e-21 |
|
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: 87.89 E-value: 1.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVllegraiaklptkevakelailp 85
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 86 qgpsapeglTVHQLVKQGRYPyQnwlkqwskedeeaveralkatkledmadravdsLSGGQRQRAWIAMTLAQETDIILL 165
Cdd:cd03221 58 ---------TWGSTVKIGYFE-Q---------------------------------LSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190
....*....|....*....|....*....|....*.
gi 499189069 166 DEPTTYLDMTHQIEILDLLfelnEKEDRTIVMVLHD 201
Cdd:cd03221 95 DEPTNHLDLESIEALEEAL----KEYPGTVILVSHD 126
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
6-217 |
3.77e-21 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 88.30 E-value: 3.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDAV-----IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRaiaklptkevake 80
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 81 LAILPQGPSAPEGlTVHQlvkqgrypyqNWLkqWSKE-DEEAVERALKATKLE-DMA-----------DRAVdSLSGGQR 147
Cdd:cd03250 68 IAYVSQEPWIQNG-TIRE----------NIL--FGKPfDEERYEKVIKACALEpDLEilpdgdlteigEKGI-NLSGGQK 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499189069 148 QRAWIAMTLAQETDIILLDEPTTYLDM---THQIE--ILDLLfelneKEDRTIVMVLHDLNLaCRYAHHLVAIKD 217
Cdd:cd03250 134 QRISLARAVYSDADIYLLDDPLSAVDAhvgRHIFEncILGLL-----LNNKTRILVTHQLQL-LPHADQIVVLDN 202
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
23-229 |
4.38e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 89.80 E-value: 4.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 23 ELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPT----KEVAKELAILPQGPSAPegLTVHQ 98
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdiKQIRKKVGLVFQFPESQ--LFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 99 LVKQGRYPYQNWlkQWSKEDEEAVERAlkatKL------EDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYL 172
Cdd:PRK13649 103 VLKDVAFGPQNF--GVSQEEAEALARE----KLalvgisESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499189069 173 DMTHQIEILDLLFELNEKeDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEV 229
Cdd:PRK13649 177 DPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-200 |
5.60e-21 |
|
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: 87.27 E-value: 5.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDA--VIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAI 83
Cdd:cd03246 1 LEVENVSFRYPGAepPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 84 LPQgpsapegltvhqlvkqgrypyqnwlkqwskEDEeaverALKATKLEDMadravdsLSGGQRQRAWIAMTLAQETDII 163
Cdd:cd03246 81 LPQ------------------------------DDE-----LFSGSIAENI-------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190
....*....|....*....|....*....|....*..
gi 499189069 164 LLDEPTTYLDMTHQIEILDLLFELNeKEDRTIVMVLH 200
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALK-AAGATRIVIAH 154
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
20-216 |
5.89e-21 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 92.09 E-value: 5.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 20 IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAILPQGPSAPEGlTVHQL 99
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSG-SVREN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 100 VKQGrypyqnwLKQWSKEDEEAVERALKA----TKLEDMADRAVDS----LSGGQRQRAWIAMTLAQETDIILLDEPTTY 171
Cdd:TIGR00958 575 IAYG-------LTDTPDEEIMAAAKAANAhdfiMEFPNGYDTEVGEkgsqLSGGQKQRIAIARALVRKPRVLILDEATSA 647
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499189069 172 LDmthqIEILDLLFELNEKEDRTIVMVLHDLNLaCRYAHHLVAIK 216
Cdd:TIGR00958 648 LD----AECEQLLQESRSRASRTVLLIAHRLST-VERADQILVLK 687
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
6-256 |
5.93e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 89.30 E-value: 5.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAI--AKLPTKEVAKELAI 83
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdySKRGLLALRQQVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 84 LPQGPSapEGLTVHQLVKQGRYPYQNwLKQWSKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDII 163
Cdd:PRK13638 82 VFQDPE--QQIFYTDIDSDIAFSLRN-LGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 164 LLDEPTTYLDMTHQIEILDLLFELNEKEDRtIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEVITCD--LVQNVFSM 241
Cdd:PRK13638 159 LLDEPTAGLDPAGRTQMIAIIRRIVAQGNH-VIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTeaMEQAGLTQ 237
|
250
....*....|....*
gi 499189069 242 NCQVTQDPLFGTPLC 256
Cdd:PRK13638 238 PWLVKLHTQLGLPLC 252
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
23-229 |
8.61e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 89.41 E-value: 8.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 23 ELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLeGRAIAKLPTKE-----VAKELAILPQGPSAPegLTVH 97
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVSSTSKQkeikpVRKKVGVVFQFPESQ--LFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 98 QLVKQGRYPYQNWlkQWSKEDEEAVeralKATKLE------DMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTY 171
Cdd:PRK13643 101 TVLKDVAFGPQNF--GIPKEKAEKI----AAEKLEmvgladEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499189069 172 LDMTHQIEILDlLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEV 229
Cdd:PRK13643 175 LDPKARIEMMQ-LFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDV 231
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
3-229 |
1.38e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 89.76 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 3 MSaISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKE------ 76
Cdd:PRK10851 1 MS-IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDrkvgfv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 77 -----------VAKELAIlpqgpsapeGLTVhqLVKQGRyPYQNWLKQwskedeeAVERALKATKLEDMADRAVDSLSGG 145
Cdd:PRK10851 80 fqhyalfrhmtVFDNIAF---------GLTV--LPRRER-PNAAAIKA-------KVTQLLEMVQLAHLADRYPAQLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 146 QRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGR 225
Cdd:PRK10851 141 QKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGT 220
|
....
gi 499189069 226 PEEV 229
Cdd:PRK10851 221 PDQV 224
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
3-241 |
1.45e-20 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 87.78 E-value: 1.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 3 MSAISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKE-L 81
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 82 AILPQGPSAPEGLTVHQ---LVKQGRYPYqnwlkqwSKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQ 158
Cdd:COG1137 81 GYLPQEASIFRKLTVEDnilAVLELRKLS-------KKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALAT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 159 ETDIILLDEPTTYLDMTHQIEILDLLFELnekEDRTIVMVLHDLN----LA-CRYAHhlvAIKDKRIYAEGRPEEVITCD 233
Cdd:COG1137 154 NPKFILLDEPFAGVDPIAVADIQKIIRHL---KERGIGVLITDHNvretLGiCDRAY---IISEGKVLAEGTPEEILNNP 227
|
250
....*....|...
gi 499189069 234 LVQNV-----FSM 241
Cdd:COG1137 228 LVRKVylgedFRL 240
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
22-203 |
1.59e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 90.46 E-value: 1.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 22 DELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEvAKEL--AILPQGPS-APEgLTVHQ 98
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRD-AQAAgiAIIHQELNlVPN-LSVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 99 LVKQGRYPYQNWLKQWSKEDEEAvERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDmTHQI 178
Cdd:COG1129 99 NIFLGREPRRGGLIDWRAMRRRA-RELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLT-EREV 176
|
170 180
....*....|....*....|....*.
gi 499189069 179 EIL-DLLFELNEkEDRTIVMVLHDLN 203
Cdd:COG1129 177 ERLfRIIRRLKA-QGVAIIYISHRLD 201
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
17-220 |
1.59e-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: 87.14 E-value: 1.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 17 DAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAILPQGPSapegLTV 96
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPV----LFA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 97 HQLVKQGRYPYQnwlkqwSKEDEEAVERALKA------TKLEDMADRAVDS----LSGGQRQRAWIAMTLAQETDIILLD 166
Cdd:cd03248 102 RSLQDNIAYGLQ------SCSFECVKEAAQKAhahsfiSELASGYDTEVGEkgsqLSGGQKQRVAIARALIRNPQVLILD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499189069 167 EPTTYLDMTHQIEILDLLFELNekEDRTIVMVLHDLNLACRyAHHLVAIKDKRI 220
Cdd:cd03248 176 EATSALDAESEQQVQQALYDWP--ERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-231 |
1.79e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 88.23 E-value: 1.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 5 AISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLM-KPRG----GSVLLEGRAIAKL-PTKEVA 78
Cdd:PRK14271 21 AMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNdKVSGyrysGDVLLGGRSIFNYrDVLEFR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 79 KELAILPQGP---------SAPEGLTVHQLVKQgrypyqnwlkqwsKEDEEAVERALKATKLED-MADRAVDS---LSGG 145
Cdd:PRK14271 101 RRVGMLFQRPnpfpmsimdNVLAGVRAHKLVPR-------------KEFRGVAQARLTEVGLWDaVKDRLSDSpfrLSGG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 146 QRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEKedRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGR 225
Cdd:PRK14271 168 QQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGP 245
|
....*.
gi 499189069 226 PEEVIT 231
Cdd:PRK14271 246 TEQLFS 251
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
23-224 |
2.28e-20 |
|
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: 86.58 E-value: 2.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 23 ELNLTIPkGEITVFIGSNGCGKSTLLRSLARLMKPRGG------SVLLEGRAIAKLPTKE-----VAKELAILPQgpsap 91
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGtivlngTVLFDSRKKINLPPQQrkiglVFQQYALFPH----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 92 egLTVHQLVKQGrypyqnwLKQWS-KEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTT 170
Cdd:cd03297 90 --LNVRENLAFG-------LKRKRnREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499189069 171 YLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEG 224
Cdd:cd03297 161 ALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
16-206 |
2.42e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 86.47 E-value: 2.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 16 GDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAilPQGPSAPEgLT 95
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG--HRNAMKPA-LT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 96 VHqlvkqgrypyQNwLKQWSK---EDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYL 172
Cdd:PRK13539 90 VA----------EN-LEFWAAflgGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170 180 190
....*....|....*....|....*....|....*
gi 499189069 173 DmTHQIEILDLLFELNEKEDRTIVMVLH-DLNLAC 206
Cdd:PRK13539 159 D-AAAVALFAELIRAHLAQGGIVIAATHiPLGLPG 192
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
6-236 |
5.18e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 87.07 E-value: 5.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDAVIIDELN---LTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELA 82
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNgvsFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 83 ILPQGPSAP-EGLTVHQLVKQGR----YPYQNWLKQwskedeeaVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLA 157
Cdd:PRK13642 85 MVFQNPDNQfVGATVEDDVAFGMenqgIPREEMIKR--------VDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 158 QETDIILLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRyAHHLVAIKDKRIYAEGRPEEVITC--DLV 235
Cdd:PRK13642 157 LRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATseDMV 235
|
.
gi 499189069 236 Q 236
Cdd:PRK13642 236 E 236
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-203 |
7.29e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 88.73 E-value: 7.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 5 AISTETLSLGYGDA--VIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELA 82
Cdd:PRK11160 338 SLTLNNVSFTYPDQpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 83 ILPQgpsapeglTVHQLVKQGRypyQNWLKQWSKEDEEAVERALKATKLEDMA--DRAVDS--------LSGGQRQRAWI 152
Cdd:PRK11160 418 VVSQ--------RVHLFSATLR---DNLLLAAPNASDEALIEVLQQVGLEKLLedDKGLNAwlgeggrqLSGGEQRRLGI 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499189069 153 AMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELneKEDRTIVMVLHDLN 203
Cdd:PRK11160 487 ARALLHDAPLLLLDEPTEGLDAETERQILELLAEH--AQNKTVLMITHRLT 535
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-271 |
7.40e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 88.69 E-value: 7.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAK-ELAIL 84
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQlGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 85 PQGPSAPEGLTVHQLVKQGRYPYQNWLK----QWSKEDEEAVERALKATKLEDMaDRAVDSLSGGQRQRAWIAMTLAQET 160
Cdd:PRK09700 86 YQELSVIDELTVLENLYIGRHLTKKVCGvniiDWREMRVRAAMMLLRVGLKVDL-DEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 161 DIILLDEPTTYLdMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEVITCDLV----- 235
Cdd:PRK09700 165 KVIIMDEPTSSL-TNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVrlmvg 243
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 499189069 236 ---QNVFSMN----CQVTQDPLFGTPLCIPHGRGRciVQEAAF 271
Cdd:PRK09700 244 relQNRFNAMkenvSNLAHETVFEVRNVTSRDRKK--VRDISF 284
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-239 |
8.39e-20 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 85.70 E-value: 8.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 1 MGMSAISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKE 80
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 81 -LAILPQGPSAPEGLTVHQLVKQG-----RYPYQnwlkqwskedeEAVER--ALKATKLEDMADRAvDSLSGGQRQRAWI 152
Cdd:PRK11614 81 aVAIVPEGRRVFSRMTVEENLAMGgffaeRDQFQ-----------ERIKWvyELFPRLHERRIQRA-GTMSGGEQQMLAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 153 AMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEkEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEVITC 232
Cdd:PRK11614 149 GRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLRE-QGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLAN 227
|
....*..
gi 499189069 233 DLVQNVF 239
Cdd:PRK11614 228 EAVRSAY 234
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-207 |
1.05e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 85.86 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 3 MSAISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARlMKPRGGSVLLEGRAI--------AKLPT 74
Cdd:PRK14258 5 IPAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNR-MNELESEVRVEGRVEffnqniyeRRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 75 KEVAKELAILPQGPSA-PegLTVHQLVKQGRYpyqnwLKQWSK--EDEEAVERALKATKLED-----MADRAVDsLSGGQ 146
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLfP--MSVYDNVAYGVK-----IVGWRPklEIDDIVESALKDADLWDeikhkIHKSALD-LSGGQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499189069 147 RQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACR 207
Cdd:PRK14258 156 QQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSR 216
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-202 |
1.17e-19 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 88.33 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 27 TIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRaiaklptkevakeLAILPQGPSAPEGLTVHQLVKQGRYP 106
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK-------------ISYKPQYIKPDYDGTVEDLLRSITDD 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 107 Y-QNWLKqwskedEEAVERalkaTKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLF 185
Cdd:PRK13409 428 LgSSYYK------SEIIKP----LQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIR 497
|
170
....*....|....*..
gi 499189069 186 ELNEKEDRTIVMVLHDL 202
Cdd:PRK13409 498 RIAEEREATALVVDHDI 514
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-220 |
1.29e-19 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 88.02 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 5 AISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAiaklptkevakELAIL 84
Cdd:PRK15064 319 ALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENA-----------NIGYY 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 85 PQGPSA--PEGLTVHqlvkqgrypyqNWLKQWSKE--DEEAVERALKatKL---EDMADRAVDSLSGGQRQRAWIAMTLA 157
Cdd:PRK15064 388 AQDHAYdfENDLTLF-----------DWMSQWRQEgdDEQAVRGTLG--RLlfsQDDIKKSVKVLSGGEKGRMLFGKLMM 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499189069 158 QETDIILLDEPTTYLDMtHQIEILDLLFelnEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRI 220
Cdd:PRK15064 455 QKPNVLVMDEPTNHMDM-ESIESLNMAL---EKYEGTLIFVSHDREFVSSLATRIIEITPDGV 513
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-226 |
1.40e-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: 87.92 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 27 TIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEgraiAKLPTKevakelailPQGPSAPEGLTVHQLVKQGRYP 106
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED----LKISYK---------PQYISPDYDGTVEEFLRSANTD 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 107 Y--QNWLKqwskedEEAVERalkaTKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLL 184
Cdd:COG1245 429 DfgSSYYK------TEIIKP----LGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAI 498
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499189069 185 FELNEKEDRTIVMVLHDLnlacrYAHHLVAikDKRIYAEGRP 226
Cdd:COG1245 499 RRFAENRGKTAMVVDHDI-----YLIDYIS--DRLMVFEGEP 533
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
20-200 |
1.85e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 84.73 E-value: 1.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 20 IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLA--RLMKPRGGSVLLEGRAIAKLPTKEVAKE---LAIlpQGPSAPEGL 94
Cdd:COG0396 15 ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMghPKYEVTSGSILLDGEDILELSPDERARAgifLAF--QYPVEIPGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 95 TVHQL-------VKQGRYPYQNWLKQwskedeeaVERALKATKL-EDMADRAVD-SLSGGQRQRAWIAMTLAQETDIILL 165
Cdd:COG0396 93 SVSNFlrtalnaRRGEELSAREFLKL--------LKEKMKELGLdEDFLDRYVNeGFSGGEKKRNEILQMLLLEPKLAIL 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 499189069 166 DEPTTYLDmthqIEILDLLFE-LNE--KEDRTIVMVLH 200
Cdd:COG0396 165 DETDSGLD----IDALRIVAEgVNKlrSPDRGILIITH 198
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
4-212 |
4.81e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 86.40 E-value: 4.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 4 SAISTETLSLGYGD-AVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMkPRGgsvllEGRAIakLPTKEvakELA 82
Cdd:COG4178 361 GALALEDLTLRTPDgRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLW-PYG-----SGRIA--RPAGA---RVL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 83 ILPQGPSAPEGLTVHQLVkqgrYPYQNwlkqwSKEDEEAVERALKATKLEDMADRaVDS-------LSGGQRQRAWIAMT 155
Cdd:COG4178 430 FLPQRPYLPLGTLREALL----YPATA-----EAFSDAELREALEAVGLGHLAER-LDEeadwdqvLSLGEQQRLAFARL 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499189069 156 LAQETDIILLDEPTTYLDMTHQIEILDLLfeLNEKEDRTIVMVLHDLNLACRYAHHL 212
Cdd:COG4178 500 LLHKPDWLFLDEATSALDEENEAALYQLL--REELPGTTVISVGHRSTLAAFHDRVL 554
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
8-173 |
5.08e-19 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 82.54 E-value: 5.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 8 TETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKlPTKEVAKELAILPQG 87
Cdd:cd03231 3 ADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDF-QRDSIARGLLYLGHA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 88 PSAPEGLTVhqlvkqgrypYQNwLKQWSKE-DEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLD 166
Cdd:cd03231 82 PGIKTTLSV----------LEN-LRFWHADhSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILD 150
|
....*..
gi 499189069 167 EPTTYLD 173
Cdd:cd03231 151 EPTTALD 157
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
16-229 |
5.17e-19 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 82.57 E-value: 5.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 16 GDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPR--GGSVLLEGRAIAKLPTKEVAKE-LAILPQGPSAPE 92
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKGEDITDLPPEERARLgIFLAFQYPPEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 93 GLTVHQLVkqgrypyqnwlkqwskedeeaveralkatkledmadRAVD-SLSGGQRQRAWIAMTLAQETDIILLDEPTTY 171
Cdd:cd03217 91 GVKNADFL------------------------------------RYVNeGFSGGEKKRNEILQLLLLEPDLAILDEPDSG 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499189069 172 LDmthqIEILDLLFELNEK---EDRTIVMVLHDLNLA----CRYAHHLVaikDKRIYAEGRPEEV 229
Cdd:cd03217 135 LD----IDALRLVAEVINKlreEGKSVLIITHYQRLLdyikPDRVHVLY---DGRIVKSGDKELA 192
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
21-202 |
6.60e-19 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 84.76 E-value: 6.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 21 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTK---EVAKELAILPQGPSA---PEgL 94
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDewrAVRSDIQMIFQDPLAslnPR-M 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 95 TVHQLVKQgryPYQNWLKQWSKED--EEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYL 172
Cdd:PRK15079 116 TIGEIIAE---PLRTYHPKLSRQEvkDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 192
|
170 180 190
....*....|....*....|....*....|
gi 499189069 173 DMTHQIEILDLLFELNEKEDRTIVMVLHDL 202
Cdd:PRK15079 193 DVSIQAQVVNLLQQLQREMGLSLIFIAHDL 222
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
18-230 |
7.95e-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: 85.95 E-value: 7.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 18 AVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAILPQ----------- 86
Cdd:TIGR01846 470 PEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQenvlfsrsird 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 87 -----GPSAPEGLTVHQLVKQGRYPYQNWLKQwsKEDEEAVERALkatkledmadravdSLSGGQRQRAWIAMTLAQETD 161
Cdd:TIGR01846 550 nialcNPGAPFEHVIHAAKLAGAHDFISELPQ--GYNTEVGEKGA--------------NLSGGQRQRIAIARALVGNPR 613
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499189069 162 IILLDEPTTYLDMTHQIEILDLLFELNekEDRTIVMVLHDLNlACRYAHHLVAIKDKRIYAEGRPEEVI 230
Cdd:TIGR01846 614 ILIFDEATSALDYESEALIMRNMREIC--RGRTVIIIAHRLS-TVRACDRIIVLEKGQIAESGRHEELL 679
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
21-231 |
8.34e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 83.90 E-value: 8.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 21 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAI-AKLP----TKEVAKELAILPQGPSapeglt 95
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpANLKkikeVKRLRKEIGLVFQFPE------ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 96 vHQLvkqgrypYQNWLKQ--------WSKEDEEAVERALKATKL----EDMADRAVDSLSGGQRQRAWIAMTLAQETDII 163
Cdd:PRK13645 101 -YQL-------FQETIEKdiafgpvnLGENKQEAYKKVPELLKLvqlpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499189069 164 LLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEVIT 231
Cdd:PRK13645 173 VLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
6-233 |
1.27e-18 |
|
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: 85.15 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYG--DAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAI 83
Cdd:TIGR02203 331 VEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 84 LPQGPSAPEGlTVHQLVKQGRYpyqnwlkqwSKEDEEAVERALKATKLEDMADRAVDS-----------LSGGQRQRAWI 152
Cdd:TIGR02203 411 VSQDVVLFND-TIANNIAYGRT---------EQADRAEIERALAAAYAQDFVDKLPLGldtpigengvlLSGGQRQRLAI 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 153 AMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELneKEDRTIVMVLHDLNlACRYAHHLVAIKDKRIYAEGRPEEVITC 232
Cdd:TIGR02203 481 ARALLKDAPILILDEATSALDNESERLVQAALERL--MQGRTTLVIAHRLS-TIEKADRIVVMDDGRIVERGTHNELLAR 557
|
.
gi 499189069 233 D 233
Cdd:TIGR02203 558 N 558
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
6-173 |
2.09e-18 |
|
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: 80.87 E-value: 2.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLpTKEVAKELAILP 85
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQ-RDEPHENILYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 86 QGPSAPEGLTVHQLVKqgrypyqnWLKQWSKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILL 165
Cdd:TIGR01189 80 HLPGLKPELSALENLH--------FWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWIL 151
|
....*...
gi 499189069 166 DEPTTYLD 173
Cdd:TIGR01189 152 DEPTTALD 159
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
5-230 |
2.83e-18 |
|
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: 84.24 E-value: 2.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 5 AISTETLSLGYGD--AVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELA 82
Cdd:TIGR03797 451 AIEVDRVTFRYRPdgPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLG 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 83 ILPQGpSAPEGLTVHQLVKQGRY--PYQNWlkqwskedeEAVERALKATKLEDMA-------DRAVDSLSGGQRQRAWIA 153
Cdd:TIGR03797 531 VVLQN-GRLMSGSIFENIAGGAPltLDEAW---------EAARMAGLAEDIRAMPmgmhtviSEGGGTLSGGQRQRLLIA 600
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499189069 154 MTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEkedrTIVMVLHDLNlACRYAHHLVAIKDKRIYAEGRPEEVI 230
Cdd:TIGR03797 601 RALVRKPRILLFDEATSALDNRTQAIVSESLERLKV----TRIVIAHRLS-TIRNADRIYVLDAGRVVQQGTYDELM 672
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
20-200 |
4.61e-18 |
|
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: 79.90 E-value: 4.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 20 IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLA-RLMKPR-GGSVLLEGRaiaKLPTKEVAKELAILPQGPSAPEGLTVh 97
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgRRTGLGvSGEVLINGR---PLDKRSFRKIIGYVPQDDILHPTLTV- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 98 qlvkqgrypyqnwlkqwskedEEAVERALKatkledmadraVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQ 177
Cdd:cd03213 100 ---------------------RETLMFAAK-----------LRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180
....*....|....*....|...
gi 499189069 178 IEILDLLFELnEKEDRTIVMVLH 200
Cdd:cd03213 148 LQVMSLLRRL-ADTGRTIICSIH 169
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
14-230 |
4.87e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 80.90 E-value: 4.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 14 GYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRaiaklptkeVAkelAILpqGPSA--- 90
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR---------VS---ALL--ELGAgfh 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 91 PEgLTVHQLVK-QGRypyqnwLKQWSKEDEEAVERALKA-TKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEP 168
Cdd:COG1134 101 PE-LTGRENIYlNGR------LLGLSRKEIDEKFDEIVEfAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499189069 169 TTYLDMTHQIEILDLLFELNEkEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEVI 230
Cdd:COG1134 174 LAVGDAAFQKKCLARIRELRE-SGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVI 234
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
11-217 |
7.07e-18 |
|
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: 83.07 E-value: 7.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 11 LSLGYG--DAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAILPQGP 88
Cdd:TIGR03796 483 ITFGYSplEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDI 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 89 SAPEGlTVHQlvkqgrypyqNwLKQWSKE-DEEAVERALKATKLEDMADRAVD-----------SLSGGQRQRAWIAMTL 156
Cdd:TIGR03796 563 FLFEG-TVRD----------N-LTLWDPTiPDADLVRACKDAAIHDVITSRPGgydaelaeggaNLSGGQRQRLEIARAL 630
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499189069 157 AQETDIILLDEPTTYLDMTHQIEILDLLfelnEKEDRTIVMVlhdlnlacryAHHLVAIKD 217
Cdd:TIGR03796 631 VRNPSILILDEATSALDPETEKIIDDNL----RRRGCTCIIV----------AHRLSTIRD 677
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
14-228 |
8.69e-18 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 82.85 E-value: 8.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 14 GYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAK----ELAILPQGPS 89
Cdd:PRK10535 17 GEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQlrreHFGFIFQRYH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 90 APEGLTVHQLVK-QGRYPyqnwlkqwSKEDEEAVERA---LKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILL 165
Cdd:PRK10535 97 LLSHLTAAQNVEvPAVYA--------GLERKQRLLRAqelLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499189069 166 DEPTTYLDMTHQIEILDLLFELNEKeDRTIVMVLHDLNLACRyAHHLVAIKDKRIYAEGRPEE 228
Cdd:PRK10535 169 DEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPPAQE 229
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-169 |
8.88e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 82.86 E-value: 8.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 5 AISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAklptkevAKELAI- 83
Cdd:NF033858 266 AIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD-------AGDIATr 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 84 -----LPQGPSAPEGLTVHQ-LVKQGRypyqnwLKQWSKED-EEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTL 156
Cdd:NF033858 339 rrvgyMSQAFSLYGELTVRQnLELHAR------LFHLPAAEiAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAV 412
|
170
....*....|...
gi 499189069 157 AQETDIILLDEPT 169
Cdd:NF033858 413 IHKPELLILDEPT 425
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
16-231 |
1.60e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 82.06 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 16 GDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGgSVLLEGRAIAKLPTKE---VAKELAILPQGPSA-- 90
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQG-EIWFDGQPLHNLNRRQllpVRHRIQVVFQDPNSsl 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 91 -PEgLTVHQLVKQGRYPYQNWLKqwSKEDEEAVERALKATKLE-DMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEP 168
Cdd:PRK15134 376 nPR-LNVLQIIEEGLRVHQPTLS--AAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEP 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499189069 169 TTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEVIT 231
Cdd:PRK15134 453 TSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFA 515
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
20-203 |
1.77e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 80.16 E-value: 1.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 20 IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAILPQGPSAP-EGLTVHQ 98
Cdd:PRK13650 22 TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQNPDNQfVGATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 99 -----LVKQGrYPYQnwlkqwskEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLD 173
Cdd:PRK13650 102 dvafgLENKG-IPHE--------EMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLD 172
|
170 180 190
....*....|....*....|....*....|
gi 499189069 174 MTHQIEILDLLFELNEKEDRTIVMVLHDLN 203
Cdd:PRK13650 173 PEGRLELIKTIKGIRDDYQMTVISITHDLD 202
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
16-230 |
2.47e-17 |
|
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: 81.33 E-value: 2.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 16 GDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAILPQGPSAPEGlT 95
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDG-T 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 96 VhqlvKQ--GRYPyqnwlkqwsKEDEEAVERALKATKLEDM-------------ADRAVdsLSGGQRQRAWIAMTLAQET 160
Cdd:COG4618 422 I----AEniARFG---------DADPEKVVAAAKLAGVHEMilrlpdgydtrigEGGAR--LSGGQRQRIGLARALYGDP 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499189069 161 DIILLDEPTTYLD------MTHQIEILdllfelneKED-RTIVMVLHDLNLAcRYAHHLVAIKDKRIYAEGRPEEVI 230
Cdd:COG4618 487 RLVVLDEPNSNLDdegeaaLAAAIRAL--------KARgATVVVITHRPSLL-AAVDKLLVLRDGRVQAFGPRDEVL 554
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
11-230 |
2.87e-17 |
|
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: 79.10 E-value: 2.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 11 LSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRA-----IAKLPTKE----VAKEL 81
Cdd:TIGR02323 9 LSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaeleLYQLSEAErrrlMRTEW 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 82 AILPQGPSAPEGLTV-------HQLVKQGRYPYQNwLKQWSKEDEEAVEraLKATKLEDMADravdSLSGGQRQRAWIAM 154
Cdd:TIGR02323 89 GFVHQNPRDGLRMRVsaganigERLMAIGARHYGN-IRATAQDWLEEVE--IDPTRIDDLPR----AFSGGMQQRLQIAR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499189069 155 TLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEVI 230
Cdd:TIGR02323 162 NLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVL 237
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-203 |
3.35e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 79.75 E-value: 3.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 18 AViiDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLpTKEVAKELAI-----------LPq 86
Cdd:COG4586 37 AV--DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKR-RKEFARRIGVvfgqrsqlwwdLP- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 87 gpsAPEGLTVHQLVkqgrypYQNWLKQWSKEDEEAVERaLKatkLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLD 166
Cdd:COG4586 113 ---AIDSFRLLKAI------YRIPDAEYKKRLDELVEL-LD---LGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLD 179
|
170 180 190
....*....|....*....|....*....|....*..
gi 499189069 167 EPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLN 203
Cdd:COG4586 180 EPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMD 216
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
13-224 |
3.57e-17 |
|
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: 77.96 E-value: 3.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 13 LGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRaiaklptkeVAKELAIlpQGPSAPE 92
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR---------VSSLLGL--GGGFNPE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 93 gLTVHQLVK-QGRypyqnwLKQWSKEDEEAVERALKA-TKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTT 170
Cdd:cd03220 99 -LTGRENIYlNGR------LLGLSRKEIDEKIDEIIEfSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499189069 171 YLDMTHQIEILDLLFELNEKeDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEG 224
Cdd:cd03220 172 VGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-202 |
3.70e-17 |
|
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: 80.98 E-value: 3.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 25 NLTIPK-GEITVFIGSNGCGKSTLLRSLARLMKPRGGSV--------LLE---GRAIAKLPTKEVAKEL--AILPQG--- 87
Cdd:COG1245 92 GLPVPKkGKVTGILGPNGIGKSTALKILSGELKPNLGDYdeepswdeVLKrfrGTELQDYFKKLANGEIkvAHKPQYvdl 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 88 -PSAPEGlTVHQLVKqgrypyqnwlkqwsKEDEE-AVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILL 165
Cdd:COG1245 172 iPKVFKG-TVRELLE--------------KVDERgKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190
....*....|....*....|....*....|....*..
gi 499189069 166 DEPTTYLDMTHQIEILDLLFELNEkEDRTIVMVLHDL 202
Cdd:COG1245 237 DEPSSYLDIYQRLNVARLIRELAE-EGKYVLVVEHDL 272
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
3-239 |
5.81e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 78.01 E-value: 5.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 3 MSAISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKE-L 81
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 82 AILPQGPSAPEGLTVhqlvkqgrypYQNWLKQWS-KEDEEAVERALKATKL------EDMADRAVDSLSGGQRQRAWIAM 154
Cdd:PRK10895 81 GYLPQEASIFRRLSV----------YDNLMAVLQiRDDLSAEQREDRANELmeefhiEHLRDSMGQSLSGGERRRVEIAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 155 TLAQETDIILLDEPTTYLDmthQIEILDLLFELNEKEDRTIVMVLHDLNL-----ACRYAHhlvAIKDKRIYAEGRPEEV 229
Cdd:PRK10895 151 ALAANPKFILLDEPFAGVD---PISVIDIKRIIEHLRDSGLGVLITDHNVretlaVCERAY---IVSQGHLIAHGTPTEI 224
|
250
....*....|
gi 499189069 230 ITCDLVQNVF 239
Cdd:PRK10895 225 LQDEHVKRVY 234
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
16-231 |
6.76e-17 |
|
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: 80.08 E-value: 6.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 16 GDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAILPQGPSAPEGLT 95
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 96 VHQLVKQGRYPyqnwlkqwskEDEEAVERALKA------TKLEDMADRAV----DSLSGGQRQRAWIAMTLAQETDIILL 165
Cdd:TIGR01842 409 AENIARFGENA----------DPEKIIEAAKLAgvheliLRLPDGYDTVIgpggATLSGGQRQRIALARALYGDPKLVVL 478
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499189069 166 DEPTTYLDMTHQIEILDLLFELnEKEDRTIVMVLHDLN-LACryAHHLVAIKDKRIYAEGRPEEVIT 231
Cdd:TIGR01842 479 DEPNSNLDEEGEQALANAIKAL-KARGITVVVITHRPSlLGC--VDKILVLQDGRIARFGERDEVLA 542
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
6-226 |
8.14e-17 |
|
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: 76.68 E-value: 8.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDAV--IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAI 83
Cdd:cd03369 7 IEVENLSVRYAPDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 84 LPQGPSAPEGLTVHQLVKQGRYpyqnwlkqwskeDEEAVERALKATKledmadrAVDSLSGGQRQRAWIAMTLAQETDII 163
Cdd:cd03369 87 IPQDPTLFSGTIRSNLDPFDEY------------SDEEIYGALRVSE-------GGLNLSQGQRQLLCLARALLKRPRVL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499189069 164 LLDEPTTYLDMTHQIEILDLLFElnEKEDRTIVMVLHDLNLACRYAHHLVaIKDKRIYAEGRP 226
Cdd:cd03369 148 VLDEATASIDYATDALIQKTIRE--EFTNSTILTIAHRLRTIIDYDKILV-MDAGEVKEYDHP 207
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
6-229 |
9.02e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 77.46 E-value: 9.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGraiaKLPTKEVAKELAILP 85
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG----KLRIGYVPQKLYLDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 86 QGPsapegLTVHQLVKqgrypyqnwLKQWSKEDEeaVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILL 165
Cdd:PRK09544 81 TLP-----LTVNRFLR---------LRPGTKKED--ILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499189069 166 DEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLnlacryahHLVAIK-------DKRIYAEGRPEEV 229
Cdd:PRK09544 145 DEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDL--------HLVMAKtdevlclNHHICCSGTPEVV 207
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
25-202 |
1.39e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 79.08 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 25 NLTIPK-GEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLE-----------GRAIAKLPTKEVAKEL--AILPQG--- 87
Cdd:PRK13409 92 GLPIPKeGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEpswdevlkrfrGTELQNYFKKLYNGEIkvVHKPQYvdl 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 88 -PSAPEGlTVHQLVKqgrypyqnwlkqwsKEDEEAVERAL-KATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILL 165
Cdd:PRK13409 172 iPKVFKG-KVRELLK--------------KVDERGKLDEVvERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190
....*....|....*....|....*....|....*..
gi 499189069 166 DEPTTYLDMTHQIEILDLLFELNekEDRTIVMVLHDL 202
Cdd:PRK13409 237 DEPTSYLDIRQRLNVARLIRELA--EGKYVLVVEHDL 271
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
19-231 |
2.02e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 77.58 E-value: 2.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 19 VIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSV-----------LLEGRAIAKLPTK-----EVAKELA 82
Cdd:PRK13631 40 VALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyigdkkNNHELITNPYSKKiknfkELRRRVS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 83 ILPQGPSapegltvHQLVKQ--------GryPYQnwLKQwSKEdeEAVERAlkATKLEDMA------DRAVDSLSGGQRQ 148
Cdd:PRK13631 120 MVFQFPE-------YQLFKDtiekdimfG--PVA--LGV-KKS--EAKKLA--KFYLNKMGlddsylERSPFGLSGGQKR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 149 RAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFElNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEE 228
Cdd:PRK13631 184 RVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYE 262
|
...
gi 499189069 229 VIT 231
Cdd:PRK13631 263 IFT 265
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
27-202 |
2.60e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 77.31 E-value: 2.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 27 TIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKlPTKEVAKEL--AIlpqgpsapegltvhQLVKQGR 104
Cdd:PRK11308 37 TLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLK-ADPEAQKLLrqKI--------------QIVFQNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 105 YPYQNWLKQWSKEDEE---------AVERALKAtkLEDMA---------DRAVDSLSGGQRQRAWIAMTLAQETDIILLD 166
Cdd:PRK11308 102 YGSLNPRKKVGQILEEpllintslsAAERREKA--LAMMAkvglrpehyDRYPHMFSGGQRQRIAIARALMLDPDVVVAD 179
|
170 180 190
....*....|....*....|....*....|....*.
gi 499189069 167 EPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDL 202
Cdd:PRK11308 180 EPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDL 215
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
6-203 |
3.18e-16 |
|
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: 75.22 E-value: 3.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGD--AVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAI 83
Cdd:cd03244 3 IEFKNVSLRYRPnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 84 LPQGPSAPEGlTVhqlvkqgRY---PYQNWlkqwskeDEEAVERALKATKLEDMADRAVDSL-----------SGGQRQR 149
Cdd:cd03244 83 IPQDPVLFSG-TI-------RSnldPFGEY-------SDEELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499189069 150 AWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFElnEKEDRTIVMVLHDLN 203
Cdd:cd03244 148 LCLARALLRKSKILVLDEATASVDPETDALIQKTIRE--AFKDCTVLTIAHRLD 199
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
3-229 |
5.73e-16 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 76.42 E-value: 5.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 3 MSAISTETLSLGY-GDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKE----- 76
Cdd:PRK11650 1 MAGLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADrdiam 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 77 VAKELAILPqgpsapegltvHQLVkqgrypYQNW---LK--QWSKED-EEAVERALKATKLEDMADRAVDSLSGGQRQRa 150
Cdd:PRK11650 81 VFQNYALYP-----------HMSV------RENMaygLKirGMPKAEiEERVAEAARILELEPLLDRKPRELSGGQRQR- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 151 wIAMTLA--QETDIILLDEPTTYLD------MthQIEILDLLFELNEkedrTIVMVLHDLNLACRYAHHLVAIKDKRIYA 222
Cdd:PRK11650 143 -VAMGRAivREPAVFLFDEPLSNLDaklrvqM--RLEIQRLHRRLKT----TSLYVTHDQVEAMTLADRVVVMNGGVAEQ 215
|
....*..
gi 499189069 223 EGRPEEV 229
Cdd:PRK11650 216 IGTPVEV 222
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
21-230 |
5.75e-16 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 77.37 E-value: 5.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 21 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAILPQgpsapeglTVH--- 97
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQ--------NVHlfn 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 98 -QLVKQGRYPYQNwlkQWSKEDEEAVERALKAT----KLEDMADRAVD----SLSGGQRQRAWIAMTLAQETDIILLDEP 168
Cdd:PRK11176 431 dTIANNIAYARTE---QYSREQIEEAARMAYAMdfinKMDNGLDTVIGengvLLSGGQRQRIAIARALLRDSPILILDEA 507
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499189069 169 TTYLDMTHQIEILDLLFELneKEDRTIVMVLHDLNlACRYAHHLVAIKDKRIYAEGRPEEVI 230
Cdd:PRK11176 508 TSALDTESERAIQAALDEL--QKNRTSLVIAHRLS-TIEKADEILVVEDGEIVERGTHAELL 566
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
6-230 |
6.77e-16 |
|
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: 74.83 E-value: 6.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYG--DAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAI 83
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 84 LPQG------------PSAPEGLTVHQLVKQGRYPyqnwlkqwskeDEEAVERALKATKLEDMADRAVdSLSGGQRQRAW 151
Cdd:cd03252 81 VLQEnvlfnrsirdniALADPGMSMERVIEAAKLA-----------GAHDFISELPEGYDTIVGEQGA-GLSGGQRQRIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499189069 152 IAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNekEDRTIVMVLHDLNlACRYAHHLVAIKDKRIYAEGRPEEVI 230
Cdd:cd03252 149 IARALIHNPRILIFDEATSALDYESEHAIMRNMHDIC--AGRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDELL 224
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1-214 |
1.63e-15 |
|
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: 76.13 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 1 MGMSAISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLeGRAIaKL-------- 72
Cdd:TIGR03719 318 LGDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV-KLayvdqsrd 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 73 ---PTKEVAKELAilpqgpsapEGLTVHQLvkqGRYpyqnwlkqwskedeEAVERALKAT---KLEDMADRaVDSLSGGQ 146
Cdd:TIGR03719 396 aldPNKTVWEEIS---------GGLDIIKL---GKR--------------EIPSRAYVGRfnfKGSDQQKK-VGQLSGGE 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499189069 147 RQRAWIAMTLAQETDIILLDEPTTYLDmthqIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVA 214
Cdd:TIGR03719 449 RNRVHLAKTLKSGGNVLLLDEPTNDLD----VETLRALEEALLNFAGCAVVISHDRWFLDRIATHILA 512
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-219 |
1.89e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 75.90 E-value: 1.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 1 MGMSAISTETLSLGY--GDAV--IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPR-----GGSVLLEGRAIAK 71
Cdd:PRK15134 1 MTQPLLAIENLSVAFrqQQTVrtVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 72 LPTKEV----AKELAILPQGPSA---PegltVHQLVKQgRYPYQNWLKQWSKEDEEA-VERALKATKLEDMADRAVD--- 140
Cdd:PRK15134 81 ASEQTLrgvrGNKIAMIFQEPMVslnP----LHTLEKQ-LYEVLSLHRGMRREAARGeILNCLDRVGIRQAAKRLTDyph 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499189069 141 SLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKR 219
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
31-227 |
2.15e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 73.37 E-value: 2.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 31 GEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVA---KELAILPQGpsapegltvHQLVKQgRYPY 107
Cdd:PRK10908 28 GEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPflrRQIGMIFQD---------HHLLMD-RTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 108 QN-----WLKQWSKED-EEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEIL 181
Cdd:PRK10908 98 DNvaiplIIAGASGDDiRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGIL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499189069 182 DLLFELNeKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPE 227
Cdd:PRK10908 178 RLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGVGGE 222
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
7-224 |
2.65e-15 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 73.42 E-value: 2.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 7 STETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRA-----IAKLPTKE----V 77
Cdd:PRK11701 8 SVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrdLYALSEAErrrlL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 78 AKELAILPQGPSapEGLTVH---------QLVKQGRYPYQN-------WLkqwskedeEAVEraLKATKLEDmADRAvds 141
Cdd:PRK11701 88 RTEWGFVHQHPR--DGLRMQvsaggnigeRLMAVGARHYGDiratagdWL--------ERVE--IDAARIDD-LPTT--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 142 LSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIY 221
Cdd:PRK11701 152 FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVV 231
|
...
gi 499189069 222 AEG 224
Cdd:PRK11701 232 ESG 234
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
22-229 |
4.51e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 74.68 E-value: 4.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 22 DELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIaKLPTKEVAKELAI--LPQGPSAPEGLTVHQL 99
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV-RIRSPRDAIALGIgmVHQHFMLVPNLTVAEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 100 VKQGRYPYQNWLKQWSKEDEEaVERALKATKLE-DmADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLdmTHQi 178
Cdd:COG3845 101 IVLGLEPTKGGRLDRKAARAR-IRELSERYGLDvD-PDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVL--TPQ- 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499189069 179 EIlDLLFE-LNE--KEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEV 229
Cdd:COG3845 176 EA-DELFEiLRRlaAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAET 228
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
21-217 |
4.53e-15 |
|
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: 72.36 E-value: 4.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 21 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGraiaKLPTKEVAKELAILPQGPSA-----PEGL- 94
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSN----KNESEPSFEATRSRNRYSVAyaaqkPWLLn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 95 -TVHQLVKQGRyPYQnwlKQWSKEDEEAVERA-----LKATKLEDMADRAVDsLSGGQRQRAWIAMTLAQETDIILLDEP 168
Cdd:cd03290 93 aTVEENITFGS-PFN---KQRYKAVTDACSLQpdidlLPFGDQTEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499189069 169 TTYLDM-----THQIEILDLLfelnEKEDRTIVMVLHDLNLaCRYAHHLVAIKD 217
Cdd:cd03290 168 FSALDIhlsdhLMQEGILKFL----QDDKRTLVLVTHKLQY-LPHADWIIAMKD 216
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
21-230 |
7.94e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 74.07 E-value: 7.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 21 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSV----------------LLEGRAiaklptkevAKELAIL 84
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdewvdmtkpgpDGRGRA---------KRYIGIL 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 85 pqgpsapegltvHQlvKQGRYPYQNWLKQWSKE------DEEAVERA---LKAT-----KLEDMADRAVDSLSGGQRQRA 150
Cdd:TIGR03269 371 ------------HQ--EYDLYPHRTVLDNLTEAiglelpDELARMKAvitLKMVgfdeeKAEEILDKYPDELSEGERHRV 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 151 WIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEVI 230
Cdd:TIGR03269 437 ALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-201 |
7.95e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 74.22 E-value: 7.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 3 MSAISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLArlmkprgGSVLL-EGRAIaklptkeVAKEL 81
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILN-------GEVLLdDGRII-------YEQDL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 82 AI--LPQGPSAPEGLTVHQLVKQG---------RY----------PYQNWLKQ-------------WSKEDEeaVERALK 127
Cdd:PRK11147 67 IVarLQQDPPRNVEGTVYDFVAEGieeqaeylkRYhdishlvetdPSEKNLNElaklqeqldhhnlWQLENR--INEVLA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499189069 128 ATKLEdmADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDmthqIEILDLL--FELNEKEdrTIVMVLHD 201
Cdd:PRK11147 145 QLGLD--PDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD----IETIEWLegFLKTFQG--SIIFISHD 212
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
12-207 |
1.16e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 71.35 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 12 SLGYGDAV--IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELA------- 82
Cdd:PRK10584 15 SVGQGEHElsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAkhvgfvf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 83 ---ILPQGPSAPEGLTVHQLVKQGRypyqnwlkqwSKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQE 159
Cdd:PRK10584 95 qsfMLIPTLNALENVELPALLRGES----------SRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499189069 160 TDIILLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACR 207
Cdd:PRK10584 165 PDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAAR 212
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
16-186 |
2.25e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 69.83 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 16 GDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTkEVAKELAILPQGPSAPEGLT 95
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRD-EYHQDLLYLGHQPGIKTELT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 96 vhqlvkqgryPYQN--WLKQWSKE-DEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYL 172
Cdd:PRK13538 91 ----------ALENlrFYQRLHGPgDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAI 160
|
170
....*....|....
gi 499189069 173 DmTHQIEILDLLFE 186
Cdd:PRK13538 161 D-KQGVARLEALLA 173
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
31-220 |
2.38e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 72.58 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 31 GEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKE---VAKELAILPQGPSAP------------EGLT 95
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKlqaLRRDIQFIFQDPYASldprqtvgdsimEPLR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 96 VHQLVkqgrypyqnwlkqwskEDEEAVERA---LKATKLE-DMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTY 171
Cdd:PRK10261 430 VHGLL----------------PGKAAAARVawlLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSA 493
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499189069 172 LDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRI 220
Cdd:PRK10261 494 LDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
6-200 |
4.19e-14 |
|
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: 68.33 E-value: 4.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDA-VIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVllegraiaKLPTKEvakELAIL 84
Cdd:cd03223 1 IELENLSLATPDGrVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI--------GMPEGE---DLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 85 PQGPSAPEGLTVHQLVkqgrYPyqnwlkqWSKEdeeaveralkatkledmadravdsLSGGQRQRAWIAMTLAQETDIIL 164
Cdd:cd03223 70 PQRPYLPLGTLREQLI----YP-------WDDV------------------------LSGGEQQRLAFARLLLHKPKFVF 114
|
170 180 190
....*....|....*....|....*....|....*.
gi 499189069 165 LDEPTTYLDMthqiEILDLLFELNEKEDRTIVMVLH 200
Cdd:cd03223 115 LDEATSALDE----ESEDRLYQLLKELGITVISVGH 146
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-230 |
7.38e-14 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 71.52 E-value: 7.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 19 VIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAILPQGPSAPEGLTVHQ 98
Cdd:TIGR00957 1300 LVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMN 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 99 LVKQGRYpyqnwlkqwskeDEEAVERALKATKLEDMADRAVD-----------SLSGGQRQRAWIAMTLAQETDIILLDE 167
Cdd:TIGR00957 1380 LDPFSQY------------SDEEVWWALELAHLKTFVSALPDkldhecaeggeNLSVGQRQLVCLARALLRKTKILVLDE 1447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499189069 168 PTTYLDMthqiEILDLLFEL--NEKEDRTIVMVLHDLNLACRYAHhlVAIKDKRIYAE-GRPEEVI 230
Cdd:TIGR00957 1448 ATAAVDL----ETDNLIQSTirTQFEDCTVLTIAHRLNTIMDYTR--VIVLDKGEVAEfGAPSNLL 1507
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-173 |
7.76e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 70.92 E-value: 7.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLeGraiaklptkEVAKeLAILP 85
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-G---------ETVK-LAYVD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 86 QGPSA--PEGlTVHQLVKQGrypyQNWLKQWSKEdeeaveralkatkledMADRA---------------VDSLSGGQRQ 148
Cdd:PRK11819 394 QSRDAldPNK-TVWEEISGG----LDIIKVGNRE----------------IPSRAyvgrfnfkggdqqkkVGVLSGGERN 452
|
170 180
....*....|....*....|....*
gi 499189069 149 RAWIAMTLAQETDIILLDEPTTYLD 173
Cdd:PRK11819 453 RLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
13-202 |
8.25e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 71.03 E-value: 8.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 13 LGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGgSVLLEGRAIAKLPTKEVAKELAILPQGPSAPE 92
Cdd:PRK11174 358 LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQG-SLKINGIELRELDPESWRKHLSWVGQNPQLPH 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 93 GlTVHQlvkqgrypyqNWLKQWSKEDEEAVERALKATKLEDMADR---AVDS--------LSGGQRQRAWIAMTLAQETD 161
Cdd:PRK11174 437 G-TLRD----------NVLLGNPDASDEQLQQALENAWVSEFLPLlpqGLDTpigdqaagLSVGQAQRLALARALLQPCQ 505
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499189069 162 IILLDEPTTYLDMTHQIEILDLLfeLNEKEDRTIVMVLHDL 202
Cdd:PRK11174 506 LLLLDEPTASLDAHSEQLVMQAL--NAASRRQTTLMVTHQL 544
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
31-200 |
9.76e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 70.85 E-value: 9.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 31 GEITVFIGSNGCGKSTLLRSLA-RLMK--PRGGSVLLEGRAIAKlptKEVAKELAILPQG----PS--APEGLTVHQLVK 101
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAfRSPKgvKGSGSVLLNGMPIDA---KEMRAISAYVQQDdlfiPTltVREHLMFQAHLR 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 102 QGRYPYQnwlkqwsKEDEEAVERALKATKLEDMAD------RAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMT 175
Cdd:TIGR00955 128 MPRRVTK-------KEKRERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSF 200
|
170 180
....*....|....*....|....*
gi 499189069 176 HQIEILDLLFELNEKeDRTIVMVLH 200
Cdd:TIGR00955 201 MAYSVVQVLKGLAQK-GKTIICTIH 224
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
20-212 |
2.46e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 68.78 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 20 IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPR----------GGSVLLegraiaKLPTKE----VAKELAILP 85
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtadrfrwNGIDLL------KLSPRErrkiIGREIAMIF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 86 QGPSA---PEGLTVHQLVKQ-GRYPYQNWLKQWSKEDEEAVERALKATKLEDmaDRAVDS-----LSGGQRQRAWIAMTL 156
Cdd:COG4170 96 QEPSScldPSAKIGDQLIEAiPSWTFKGKWWQRFKWRKKRAIELLHRVGIKD--HKDIMNsypheLTEGECQKVMIAMAI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499189069 157 AQETDIILLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHL 212
Cdd:COG4170 174 ANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTI 229
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
21-229 |
3.33e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.11 E-value: 3.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 21 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEG-------RAIAKLPTKEVAK-------ELAILPQ 86
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsRQVIELSEQSAAQmrhvrgaDMAMIFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 87 GP--SAPEGLTVHQLVKQGRYPYQNWlkqwSKEDEEA-VERALKATKL---EDMADRAVDSLSGGQRQRAWIAMTLAQET 160
Cdd:PRK10261 112 EPmtSLNPVFTVGEQIAESIRLHQGA----SREEAMVeAKRMLDQVRIpeaQTILSRYPHQLSGGMRQRVMIAMALSCRP 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499189069 161 DIILLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEV 229
Cdd:PRK10261 188 AVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
21-220 |
5.36e-13 |
|
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: 65.53 E-value: 5.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 21 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKE-VAKELAILPQGPSApEGLtvhql 99
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDaIRAGIAYVPEDRKR-EGL----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 100 vkqgrypyqnwlkqwskedeeaverALKATKLEDMAdrAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIE 179
Cdd:cd03215 90 -------------------------VLDLSVAENIA--LSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAE 142
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499189069 180 ILDLLFELNEkEDRTIVMVLHDLNLACRYAHHLVAIKDKRI 220
Cdd:cd03215 143 IYRLIRELAD-AGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
20-208 |
7.45e-13 |
|
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: 68.04 E-value: 7.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 20 IIDELNLT-IPKGEITVfIGSNGCGKSTLLRSLARLMKPrggsvlLEGRAIAKLPTKevakeLAILPQGPSAPEGLTVHQ 98
Cdd:TIGR03719 20 ILKDISLSfFPGAKIGV-LGLNGAGKSTLLRIMAGVDKD------FNGEARPQPGIK-----VGYLPQEPQLDPTKTVRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 99 LVKQGRYPYQNWLK-------QWSKEDEEAVERALKATKLED---------------MA---------DRAVDSLSGGQR 147
Cdd:TIGR03719 88 NVEEGVAEIKDALDrfneisaKYAEPDADFDKLAAEQAELQEiidaadawdldsqleIAmdalrcppwDADVTKLSGGER 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499189069 148 QRAWIAMTLAQETDIILLDEPTTYLDMthqiEILDLLFELNEKEDRTIVMVLHDlnlacRY 208
Cdd:TIGR03719 168 RRVALCRLLLSKPDMLLLDEPTNHLDA----ESVAWLERHLQEYPGTVVAVTHD-----RY 219
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
24-201 |
8.01e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 68.07 E-value: 8.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 24 LNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAkLPTKEVAKEL--AIL-----------PQGPSA 90
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT-AEQPEDYRKLfsAVFtdfhlfdqllgPEGKPA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 91 PEGLtvhqlvkqgrypYQNWLKQWSKEDeeaveralkatKLEDMADRAVD-SLSGGQRQRAWIAMTLAQETDIILLDEPT 169
Cdd:PRK10522 421 NPAL------------VEKWLERLKMAH-----------KLELEDGRISNlKLSKGQKKRLALLLALAEERDILLLDEWA 477
|
170 180 190
....*....|....*....|....*....|...
gi 499189069 170 TYLD-MTHQIEILDLLFELNEKeDRTIVMVLHD 201
Cdd:PRK10522 478 ADQDpHFRREFYQVLLPLLQEM-GKTIFAISHD 509
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-200 |
1.07e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 67.63 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 22 DELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKE-----VA---KELAILPQgpsapeg 93
Cdd:PRK11288 21 DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAalaagVAiiyQELHLVPE------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 94 LTVHQLVKQGRYPYQ-NWLKQwskedEEAVERALKatKLEDMA-----DRAVDSLSGGQRQRAWIAMTLAQETDIILLDE 167
Cdd:PRK11288 94 MTVAENLYLGQLPHKgGIVNR-----RLLNYEARE--QLEHLGvdidpDTPLKYLSIGQRQMVEIAKALARNARVIAFDE 166
|
170 180 190
....*....|....*....|....*....|...
gi 499189069 168 PTTYLDmTHQIEILDLLFELNEKEDRTIVMVLH 200
Cdd:PRK11288 167 PTSSLS-AREIEQLFRVIRELRAEGRVILYVSH 198
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
6-187 |
1.66e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 64.51 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDAVIIDeLNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVakelailp 85
Cdd:PRK13541 2 LSLHQLQFNIEQKNLFD-LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYC-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 86 qgpsapeGLTVHQL-VKQGRYPYQNwLKQWSK--EDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDI 162
Cdd:PRK13541 73 -------TYIGHNLgLKLEMTVFEN-LKFWSEiyNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDL 144
|
170 180
....*....|....*....|....*
gi 499189069 163 ILLDEPTTYLDMTHQieilDLLFEL 187
Cdd:PRK13541 145 WLLDEVETNLSKENR----DLLNNL 165
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
20-173 |
3.17e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 64.21 E-value: 3.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 20 IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSvllegrAIAKLPTKEVAKELAILpqgpsapEGLtvhql 99
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVA------GCVDVPDNQFGREASLI-------DAI----- 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499189069 100 vkqgrypyqnwlkqWSKEDEEAVERALKATKLEDMAD--RAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLD 173
Cdd:COG2401 107 --------------GRKGDFKDAVELLNAVGLSDAVLwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
6-226 |
4.64e-12 |
|
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: 62.97 E-value: 4.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDAVIIDELNlTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEvakelailp 85
Cdd:cd03222 1 QLYPDCVKRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQYI--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 86 qgpsapegltvhqlvkqgrypyqnwlkqwskedeeaveralkatkledmadravdSLSGGQRQRAWIAMTLAQETDIILL 165
Cdd:cd03222 71 -------------------------------------------------------DLSGGELQRVAIAAALLRNATFYLF 95
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499189069 166 DEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLacryahhLVAIKDKRIYAEGRP 226
Cdd:cd03222 96 DEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAV-------LDYLSDRIHVFEGEP 149
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
31-200 |
4.81e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 65.67 E-value: 4.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 31 GEITVFIGSNGCGKSTLLRSLARLMKPRG--GSVLLEGRAiaklPTKEVAKELAILPQGPSAPEGLTVHQ---LVKQGRY 105
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRK----PTKQILKRTGFVTQDDILYPHLTVREtlvFCSLLRL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 106 PyqnwlKQWSKEDE----EAVERALKATKLED--MADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIE 179
Cdd:PLN03211 170 P-----KSLTKQEKilvaESVISELGLTKCENtiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYR 244
|
170 180
....*....|....*....|.
gi 499189069 180 ILDLLFELNEKeDRTIVMVLH 200
Cdd:PLN03211 245 LVLTLGSLAQK-GKTIVTSMH 264
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
25-202 |
5.32e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 65.32 E-value: 5.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 25 NLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIA-KLPTKEVA----------KELAILPqGPSAPEG 93
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDiRSPRDAIRagimlcpedrKAEGIIP-VHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 94 LTV----HQLvkqgryPYQNWLKQwSKEDEEAvERALKATKLED-MADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEP 168
Cdd:PRK11288 352 INIsarrHHL------RAGCLINN-RWEAENA-DRFIRSLNIKTpSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEP 423
|
170 180 190
....*....|....*....|....*....|....
gi 499189069 169 TTYLDMTHQIEILDLLFELNEKeDRTIVMVLHDL 202
Cdd:PRK11288 424 TRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDL 456
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
16-173 |
8.78e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 64.75 E-value: 8.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 16 GDAVIIDELNLT-IPKGEITVfIGSNGCGKSTLLRSLARLMKPRGG-SVLLEGRAIaklptkevakelAILPQGPSAPEG 93
Cdd:PRK11819 18 PKKQILKDISLSfFPGAKIGV-LGLNGAGKSTLLRIMAGVDKEFEGeARPAPGIKV------------GYLPQEPQLDPE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 94 LTVHQLVKQGRYPYQNWLK-------QWSKEDEEAVERALKATKLED---------------MA---------DRAVDSL 142
Cdd:PRK11819 85 KTVRENVEEGVAEVKAALDrfneiyaAYAEPDADFDALAAEQGELQEiidaadawdldsqleIAmdalrcppwDAKVTKL 164
|
170 180 190
....*....|....*....|....*....|.
gi 499189069 143 SGGQRQRAWIAMTLAQETDIILLDEPTTYLD 173
Cdd:PRK11819 165 SGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
9-204 |
9.32e-12 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 64.81 E-value: 9.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 9 ETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVllegrAIAKlptkevAKELAILPQgp 88
Cdd:PRK10636 316 EKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI-----GLAK------GIKLGYFAQ-- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 89 sapegltvHQL--VKQGRYPYQNWLKQWSKEDEEAVERAL-----KATKLEDMADRavdsLSGGQRQRAWIAMTLAQETD 161
Cdd:PRK10636 383 --------HQLefLRADESPLQHLARLAPQELEQKLRDYLggfgfQGDKVTEETRR----FSGGEKARLVLALIVWQRPN 450
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499189069 162 IILLDEPTTYLDMTHQIEILDLLFELnekeDRTIVMVLHDLNL 204
Cdd:PRK10636 451 LLLLDEPTNHLDLDMRQALTEALIDF----EGALVVVSHDRHL 489
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-230 |
1.06e-11 |
|
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: 64.44 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLaRLMK---PRGGSVL------------------- 63
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVL-RGMDqyePTSGRIIyhvalcekcgyverpskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 64 ---------LEGRAI-----AKLPTKEVAKELAILPQGPSAPEG-LTVHQLVKQGrypyqnwLKQWSKEDEEAVERALKA 128
Cdd:TIGR03269 80 epcpvcggtLEPEEVdfwnlSDKLRRRIRKRIAIMLQRTFALYGdDTVLDNVLEA-------LEEIGYEGKEAVGRAVDL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 129 TKLEDMADR----AVDsLSGGQRQRAWIAMTLAQETDIILLDEPTTYLD-MTHQIeILDLLFELNEKEDRTIVMVLHDLN 203
Cdd:TIGR03269 153 IEMVQLSHRithiARD-LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDpQTAKL-VHNALEEAVKASGISMVLTSHWPE 230
|
250 260
....*....|....*....|....*..
gi 499189069 204 LACRYAHHLVAIKDKRIYAEGRPEEVI 230
Cdd:TIGR03269 231 VIEDLSDKAIWLENGEIKEEGTPDEVV 257
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
25-198 |
1.12e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 64.27 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 25 NLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIA-KLPTKEVAKELAILP---QGpsapEGLTVHQ-- 98
Cdd:COG1129 272 SFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRiRSPRDAIRAGIAYVPedrKG----EGLVLDLsi 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 99 -----LVKQGRYPYQNWLKQwsKEDEEAVERALKA--TKLEDMaDRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTY 171
Cdd:COG1129 348 renitLASLDRLSRGGLLDR--RRERALAEEYIKRlrIKTPSP-EQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRG 424
|
170 180 190
....*....|....*....|....*....|.
gi 499189069 172 LDmthqI----EILDLLFELNEkEDRTIVMV 198
Cdd:COG1129 425 ID----VgakaEIYRLIRELAA-EGKAVIVI 450
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
21-202 |
1.50e-11 |
|
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: 62.45 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 21 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLL--EGRAI--AKLPTKE-----------VAKELAILP 85
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVdlAQASPREilalrrrtigyVSQFLRVIP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 86 QGPSapEGLTVHQLVKQGRypyqnwlkqwskEDEEAVERALKA-TKL---EDMADRAVDSLSGGQRQRAWIAMTLAQETD 161
Cdd:COG4778 107 RVSA--LDVVAEPLLERGV------------DREEARARARELlARLnlpERLWDLPPATFSGGEQQRVNIARGFIADPP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499189069 162 IILLDEPTTYLDMTHQIEILDLLFELnEKEDRTIVMVLHDL 202
Cdd:COG4778 173 LLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDE 212
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
9-201 |
1.64e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 64.20 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 9 ETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVllegraiaKLPTK-EVA---KELAIL 84
Cdd:PRK11147 323 ENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI--------HCGTKlEVAyfdQHRAEL 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 85 PqgpsaPEGlTVHQLVKQGrypyqnwlkqwsKEDEE--AVER-ALkaTKLEDM---ADRA---VDSLSGGQRQRAWIAMT 155
Cdd:PRK11147 395 D-----PEK-TVMDNLAEG------------KQEVMvnGRPRhVL--GYLQDFlfhPKRAmtpVKALSGGERNRLLLARL 454
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499189069 156 LAQETDIILLDEPTTYLDmthqIEILDLLFELNEKEDRTIVMVLHD 201
Cdd:PRK11147 455 FLKPSNLLILDEPTNDLD----VETLELLEELLDSYQGTVLLVSHD 496
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
23-229 |
1.66e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 63.74 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 23 ELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAK------LPTKE-----VAKELAILPqgpsap 91
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDaekgicLPPEKrrigyVFQDARLFP------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 92 egltvHQLVKQgrypyqNWLKQWSKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTY 171
Cdd:PRK11144 90 -----HYKVRG------NLRYGMAKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLAS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 499189069 172 LDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEV 229
Cdd:PRK11144 159 LDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
21-202 |
1.80e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 63.83 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 21 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAILPQGPsapeGL---TVH 97
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDA----GLfnrSIE 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 98 QLVKQGRypyqnwlkqwskED--EEAVERALKATKLEDMADRAVD-----------SLSGGQRQRAWIAMTLAQETDIIL 164
Cdd:PRK13657 427 DNIRVGR------------PDatDEEMRAAAERAQAHDFIERKPDgydtvvgergrQLSGGERQRLAIARALLKDPPILI 494
|
170 180 190
....*....|....*....|....*....|....*...
gi 499189069 165 LDEPTTYLDMTHQIEILDLLFELneKEDRTIVMVLHDL 202
Cdd:PRK13657 495 LDEATSALDVETEAKVKAALDEL--MKGRTTFIIAHRL 530
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
23-184 |
2.33e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 63.53 E-value: 2.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 23 ELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKE-VAKELAILPQGPS-------APEGL 94
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPEDRQssglyldAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 95 TVHQLVkQGRYPYqnWLKqwSKEDEEAVERALKA--TKLEDmADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYL 172
Cdd:PRK15439 361 NVCALT-HNRRGF--WIK--PARENAVLERYRRAlnIKFNH-AEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
170
....*....|..
gi 499189069 173 DMTHQIEILDLL 184
Cdd:PRK15439 435 DVSARNDIYQLI 446
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
17-218 |
2.56e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 63.89 E-value: 2.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 17 DAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLL-EGRAIAKLPTKEVAKELAILPQGPSAPEGlT 95
Cdd:PTZ00265 397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSN-S 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 96 VHQLVKQGRYPYQN--WLKQWSKEDEEAVE---------RALKATKLEDMAdRAVDS----------------------- 141
Cdd:PTZ00265 476 IKNNIKYSLYSLKDleALSNYYNEDGNDSQenknkrnscRAKCAGDLNDMS-NTTDSneliemrknyqtikdsevvdvsk 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 142 -------------------------LSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEKEDRTIV 196
Cdd:PTZ00265 555 kvlihdfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITI 634
|
250 260
....*....|....*....|..
gi 499189069 197 MVLHDLNlACRYAHHLVAIKDK 218
Cdd:PTZ00265 635 IIAHRLS-TIRYANTIFVLSNR 655
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-220 |
2.96e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 63.64 E-value: 2.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 19 VIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEgRAIAKLPTkevakelailpqgpsapegltvhq 98
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-RSIAYVPQ------------------------ 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 99 lvkqgrypyQNWLKQ---------WSKEDEEAVERALKATKLE-DMA-----------DRAVDsLSGGQRQRAWIAMTLA 157
Cdd:PTZ00243 729 ---------QAWIMNatvrgnilfFDEEDAARLADAVRVSQLEaDLAqlgggleteigEKGVN-LSGGQKARVSLARAVY 798
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499189069 158 QETDIILLDEPTTYLDMTHQIEILDLLFeLNEKEDRTIVMVLHDLNLACRyAHHLVAIKDKRI 220
Cdd:PTZ00243 799 ANRDVYLLDDPLSALDAHVGERVVEECF-LGALAGKTRVLATHQVHVVPR-ADYVVALGDGRV 859
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-170 |
3.52e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 63.22 E-value: 3.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 5 AISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLrSL---ARlmKPRGGSVLLEGRAIA-KLPTKEVAKE 80
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLL-SLiagAR--KIQQGRVEVLGGDMAdARHRRAVCPR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 81 LAILPQG------PSapegLTVH-------QLVKQGRypyqnwlkqwsKEDEEAVERALKATKLEDMADRAVDSLSGGQR 147
Cdd:NF033858 78 IAYMPQGlgknlyPT----LSVFenldffgRLFGQDA-----------AERRRRIDELLRATGLAPFADRPAGKLSGGMK 142
|
170 180
....*....|....*....|...
gi 499189069 148 QRAWIAMTLAQETDIILLDEPTT 170
Cdd:NF033858 143 QKLGLCCALIHDPDLLILDEPTT 165
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
21-234 |
3.96e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 61.73 E-value: 3.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 21 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAILPQGPSApeGLTVHQLV 100
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPST--SLNPRQRI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 101 KQG-RYPYQNWLKQWSKEDEEAVERALKATKL-EDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQI 178
Cdd:PRK15112 107 SQIlDFPLRLNTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRS 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499189069 179 EILDLLFELNEKEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEVITCDL 234
Cdd:PRK15112 187 QLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPL 242
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
24-69 |
1.14e-10 |
|
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: 61.35 E-value: 1.14e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 499189069 24 LNLTIPKGEItVFI-GSNGCGKSTLLRSLARLMKPRGGSVLLEGRAI 69
Cdd:COG4615 351 IDLTIRRGEL-VFIvGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV 396
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1-202 |
1.44e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 61.27 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 1 MGMSAISTETLSLGY-GDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAK 79
Cdd:PRK10790 336 LQSGRIDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 80 ELAILPQGPSAPEGlTVHQLVKQGRypyqnwlkqwsKEDEEAVERALKATKLEDMADRAVD-----------SLSGGQRQ 148
Cdd:PRK10790 416 GVAMVQQDPVVLAD-TFLANVTLGR-----------DISEEQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQ 483
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499189069 149 RAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEKEdrTIVMVLHDL 202
Cdd:PRK10790 484 LLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHT--TLVVIAHRL 535
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
15-211 |
1.56e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.10 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 15 YGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMkPRG---GSVLLEGRAIAKLPTKEV-AKELAILPQGPSA 90
Cdd:PRK13549 15 FGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEGEELQASNIRDTeRAGIAIIHQELAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 91 PEGLTVHQLVKQGRYPYQNWLKQWSKEDEEAvERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTT 170
Cdd:PRK13549 94 VKELSVLENIFLGNEITPGGIMDYDAMYLRA-QKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTA 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499189069 171 yldmthqieildllfELNEKEDRTIVMVLHDL---NLACRYAHH 211
Cdd:PRK13549 173 ---------------SLTESETAVLLDIIRDLkahGIACIYISH 201
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
37-251 |
2.20e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.15 E-value: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 37 IGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAILPQGPSAPEGlTVhqlvkqgRYPyqnwLKQWSK 116
Cdd:PLN03232 1268 VGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSG-TV-------RFN----IDPFSE 1335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 117 EDEEAVERALKATKLEDMADRAV-----------DSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMThqieiLDLLF 185
Cdd:PLN03232 1336 HNDADLWEALERAHIKDVIDRNPfgldaevseggENFSVGQRQLLSLARALLRRSKILVLDEATASVDVR-----TDSLI 1410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499189069 186 ELNEKEDR---TIVMVLHDLN--LACryaHHLVAIKDKRIYAEGRPEEVITCD------LVQNVFSMNCQVTQDPLF 251
Cdd:PLN03232 1411 QRTIREEFkscTMLVIAHRLNtiIDC---DKILVLSSGQVLEYDSPQELLSRDtsaffrMVHSTGPANAQYLSNLVF 1484
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
60-200 |
2.45e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 60.81 E-value: 2.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 60 GSVLLEGRAIAKLPTKEVAKELAILPQGPSApEGLTVHQLVKQGRypyqnwlKQWSKEDeeaVERALKATKLEDMADRAV 139
Cdd:PTZ00265 1277 GKILLDGVDICDYNLKDLRNLFSIVSQEPML-FNMSIYENIKFGK-------EDATRED---VKRACKFAAIDEFIESLP 1345
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499189069 140 D-----------SLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLH 200
Cdd:PTZ00265 1346 NkydtnvgpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH 1417
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
21-172 |
3.15e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.13 E-value: 3.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 21 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVakelaiLPQGPSapeglTVHQ-- 98
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEA------LENGIS-----MVHQel 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 99 -LVKQ---------GRYPYQNWLKqwskeDEEAVERALKATKLE---DMADRA-VDSLSGGQRQRAWIAMTLAQETDIIL 164
Cdd:PRK10982 83 nLVLQrsvmdnmwlGRYPTKGMFV-----DQDKMYRDTKAIFDEldiDIDPRAkVATLSVSQMQMIEIAKAFSYNAKIVI 157
|
....*...
gi 499189069 165 LDEPTTYL 172
Cdd:PRK10982 158 MDEPTSSL 165
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-202 |
3.99e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 59.63 E-value: 3.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 21 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKE--------VAKELAILPQgpsape 92
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSsqeagigiIHQELNLIPQ------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 93 gLTVHQLVKQGRYPYQNWLK-QWSKEDEEAvERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTY 171
Cdd:PRK10762 94 -LTIAENIFLGREFVNRFGRiDWKKMYAEA-DKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDA 171
|
170 180 190
....*....|....*....|....*....|.
gi 499189069 172 LDMTHQIEILDLLFELNEkEDRTIVMVLHDL 202
Cdd:PRK10762 172 LTDTETESLFRVIRELKS-QGRGIVYISHRL 201
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
19-210 |
4.07e-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: 57.37 E-value: 4.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 19 VIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLArlmkprggsvLLEGRAIAKLPTKEVAKelailPQGPSAPEGLTVHQ 98
Cdd:cd03227 9 SYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIG----------LALGGAQSATRRRSGVK-----AGCIVAAVSAELIF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 99 LVKQgrypyqnwlkqwskedeeaveralkatkledmadravdsLSGGQRQRAWIAMTLA----QETDIILLDEPTTYLDM 174
Cdd:cd03227 74 TRLQ---------------------------------------LSGGEKELSALALILAlaslKPRPLYILDEIDRGLDP 114
|
170 180 190
....*....|....*....|....*....|....*.
gi 499189069 175 THQIEILDLLFELNEKEDRTIVmVLHDLNLACRYAH 210
Cdd:cd03227 115 RDGQALAEAILEHLVKGAQVIV-ITHLPELAELADK 149
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
21-231 |
4.31e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.80 E-value: 4.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 21 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIA-KLPTKEVAKELAILPQGP---------SA 90
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKGMAYITESRrdngffpnfSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 91 PEGLTVHQLVKQGRYPYQNWLKQWSKEDEEA-VERALKATKLEDMaDRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPT 169
Cdd:PRK09700 359 AQNMAISRSLKDGGYKGAMGLFHEVDEQRTAeNQRELLALKCHSV-NQNITELSGGNQQKVLISKWLCCCPEVIIFDEPT 437
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499189069 170 TYLDMTHQIEILDLLFELNEkEDRTIVMVLHDLNlacryahHLVAIKDK-RIYAEGRPEEVIT 231
Cdd:PRK09700 438 RGIDVGAKAEIYKVMRQLAD-DGKVILMVSSELP-------EIITVCDRiAVFCEGRLTQILT 492
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
15-211 |
6.27e-10 |
|
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: 59.07 E-value: 6.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 15 YGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMkPRG---GSVLLEGRAIAKLPTKEV-AKELAILPQGPSA 90
Cdd:TIGR02633 11 FGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHGtwdGEIYWSGSPLKASNIRDTeRAGIVIIHQELTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 91 PEGLTVHQLVKQGRypyQNWLKQWSKEDEEAVERA---LKATKLEDMAD-RAVDSLSGGQRQRAWIAMTLAQETDIILLD 166
Cdd:TIGR02633 90 VPELSVAENIFLGN---EITLPGGRMAYNAMYLRAknlLRELQLDADNVtRPVGDYGGGQQQLVEIAKALNKQARLLILD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 499189069 167 EPTTYLDMTHQIEILDLLFELNEKedrtivmvlhdlNLACRYAHH 211
Cdd:TIGR02633 167 EPSSSLTEKETEILLDIIRDLKAH------------GVACVYISH 199
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
15-236 |
6.33e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 59.29 E-value: 6.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 15 YGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKL-PTKevAKELAI--LPQGPSAP 91
Cdd:PRK15439 21 YSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLtPAK--AHQLGIylVPQEPLLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 92 EGLTVHQ--LVKQGRYPyqnwlkqwskEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPT 169
Cdd:PRK15439 99 PNLSVKEniLFGLPKRQ----------ASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499189069 170 TYLDmthQIEILDLLFELNE--KEDRTIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEVITCDLVQ 236
Cdd:PRK15439 169 ASLT---PAETERLFSRIREllAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDIIQ 234
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
11-174 |
7.24e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 57.55 E-value: 7.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 11 LSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAklpTKEVAKELAILPQGPSA 90
Cdd:PRK13543 17 LAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT---RGDRSRFMAYLGHLPGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 91 PEGLT----VHQLVK-QGRYPYQnwlkqwskedeeAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILL 165
Cdd:PRK13543 94 KADLStlenLHFLCGlHGRRAKQ------------MPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLL 161
|
....*....
gi 499189069 166 DEPTTYLDM 174
Cdd:PRK13543 162 DEPYANLDL 170
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
19-200 |
1.57e-09 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 58.22 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 19 VIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVllegraiaklpTKEVAKELAILPQGPSapegLTVHQ 98
Cdd:TIGR00954 466 VLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRL-----------TKPAKGKLFYVPQRPY----MTLGT 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 99 LVKQGRYPYqnwlkqwSKED-------EEAVERALKATKLEDMADRAV---------DSLSGGQRQRAWIAMTLAQETDI 162
Cdd:TIGR00954 531 LRDQIIYPD-------SSEDmkrrglsDKDLEQILDNVQLTHILEREGgwsavqdwmDVLSGGEKQRIAMARLFYHKPQF 603
|
170 180 190
....*....|....*....|....*....|....*...
gi 499189069 163 ILLDEPTTYLdmthQIEILDLLFELNEKEDRTIVMVLH 200
Cdd:TIGR00954 604 AILDECTSAV----SVDVEGYMYRLCREFGITLFSVSH 637
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-221 |
1.72e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 55.07 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 30 KGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLegraIaklptkevakelailpqgpsapegltvhqlvkqgrypyqn 109
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY----I---------------------------------------- 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 110 wlkqwskeDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDL-----L 184
Cdd:smart00382 37 --------DGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlL 108
|
170 180 190
....*....|....*....|....*....|....*..
gi 499189069 185 FELNEKEDRTIVMVLHDLNLACRyaHHLVAIKDKRIY 221
Cdd:smart00382 109 LLLKSEKNLTVILTTNDEKDLGP--ALLRRRFDRRIV 143
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
21-207 |
2.91e-09 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 55.02 E-value: 2.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 21 IDELNLTIPKGEITVFIGSNGCGKSTLLrslarlmkprggsvlLEGRAiaklptKEVAKELAILPQGPSAPEGLTVHQLv 100
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLV---------------NEGLY------ASGKARLISFLPKFSRNKLIFIDQL- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 101 kqgrypyqnwlkqwskedeeaveRALKATKLEDMA-DRAVDSLSGGQRQRAWIAMTLAQETD--IILLDEPTTYLdmtHQ 177
Cdd:cd03238 69 -----------------------QFLIDVGLGYLTlGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGL---HQ 122
|
170 180 190
....*....|....*....|....*....|..
gi 499189069 178 IEILDLLFELNEKEDR--TIVMVLHDLNLACR 207
Cdd:cd03238 123 QDINQLLEVIKGLIDLgnTVILIEHNLDVLSS 154
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
33-216 |
3.17e-09 |
|
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: 55.31 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 33 ITVFIGSNGCGKSTLLR----SLARLMKPRGGSVLL--------EGRAIAKLPTKEVAKELAILPQGPSAPEGLTvhqLV 100
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEalkyALTGELPPNSKGGAHdpkliregEVRAQVKLAFENANGKKYTITRSLAILENVI---FC 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 101 KQGRYpyqNWLkqwskedeeaveralkatkLEDMADRavdsLSGGQRQ------RAWIAMTLAQETDIILLDEPTTYLDM 174
Cdd:cd03240 101 HQGES---NWP-------------------LLDMRGR----CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499189069 175 TH-QIEILDLLFELNEKEDRTIVMVLHDLNLAcRYAHHLVAIK 216
Cdd:cd03240 155 ENiEESLAEIIEERKSQKNFQLIVITHDEELV-DAADHIYRVE 196
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
6-174 |
4.19e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 55.57 E-value: 4.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLA--RLMKPRGGSVLLEGRAIAKLPTKEVAKELAI 83
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPEDRAGEGIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 84 LP-QGPSAPEGLTVHQLVKQG-----RYPYQNWLKQWSKEDeeAVERALKATKL-EDMADRAVD-SLSGGQRQRAWIAMT 155
Cdd:PRK09580 82 MAfQYPVEIPGVSNQFFLQTAlnavrSYRGQEPLDRFDFQD--LMEEKIALLKMpEDLLTRSVNvGFSGGEKKRNDILQM 159
|
170
....*....|....*....
gi 499189069 156 LAQETDIILLDEPTTYLDM 174
Cdd:PRK09580 160 AVLEPELCILDESDSGLDI 178
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
21-202 |
4.19e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 57.33 E-value: 4.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 21 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKlPTKEVAKELAILPQGPSAPEGLTvhqlv 100
Cdd:TIGR01257 1955 VDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQFDAIDDLLT----- 2028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 101 kqGR---YPYQNWLKQWSKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQ 177
Cdd:TIGR01257 2029 --GRehlYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQAR 2106
|
170 180
....*....|....*....|....*
gi 499189069 178 IEILDLLFELnEKEDRTIVMVLHDL 202
Cdd:TIGR01257 2107 RMLWNTIVSI-IREGRAVVLTSHSM 2130
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
11-204 |
5.63e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.57 E-value: 5.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 11 LSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAK-LPTKEvaKELAILPQgps 89
Cdd:PRK13540 7 LDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKdLCTYQ--KQLCFVGH--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 90 apegltvhqlvKQGRYPYQNwLKQWSKEDEEAVERALKAT------KLEDMADRAVDSLSGGQRQRAWIAMTLAQETDII 163
Cdd:PRK13540 82 -----------RSGINPYLT-LRENCLYDIHFSPGAVGITelcrlfSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLW 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 499189069 164 LLDEPTTYLDmTHQIEILDLLFELNEKEDRTIVMVLH-DLNL 204
Cdd:PRK13540 150 LLDEPLVALD-ELSLLTIITKIQEHRAKGGAVLLTSHqDLPL 190
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
20-181 |
8.11e-09 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 54.19 E-value: 8.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 20 IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRG---GSVLLEGraiakLPTKEVAK----ELAILPQGPSAPE 92
Cdd:cd03233 22 ILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNG-----IPYKEFAEkypgEIIYVSEEDVHFP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 93 GLTVhqlvkqgrypyqnwlkqwskedEEAVERALKATkledmADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYL 172
Cdd:cd03233 97 TLTV----------------------RETLDFALRCK-----GNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGL 149
|
....*....
gi 499189069 173 DMTHQIEIL 181
Cdd:cd03233 150 DSSTALEIL 158
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
20-200 |
1.02e-08 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 53.79 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 20 IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLA--RLMKPRGGSVLLEGRAIaklpTKEVAKELAILPQGPSAPEGLTVh 97
Cdd:cd03232 22 LLNNISGYVKPGTLTALMGESGAGKTTLLDVLAgrKTAGVITGEILINGRPL----DKNFQRSTGYVEQQDVHSPNLTV- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 98 qlvkqgrypyqnwlkqwskedEEAVE--RALKAtkledmadravdsLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMT 175
Cdd:cd03232 97 ---------------------REALRfsALLRG-------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQ 142
|
170 180
....*....|....*....|....*
gi 499189069 176 HQIEILDLLFELNEkEDRTIVMVLH 200
Cdd:cd03232 143 AAYNIVRFLKKLAD-SGQAILCTIH 166
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
24-173 |
1.11e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 55.90 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 24 LNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAILPQGPSAPEGlTVhqlvkqg 103
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSG-TV------- 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 104 RY---PY--QNWLKQWskedeEAVERA-LKAT------KLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTY 171
Cdd:PLN03130 1330 RFnldPFneHNDADLW-----ESLERAhLKDVirrnslGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAA 1404
|
..
gi 499189069 172 LD 173
Cdd:PLN03130 1405 VD 1406
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-182 |
1.13e-08 |
|
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: 55.69 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 20 IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRaiaklptkevakeLAILPQGPSAPEGLTVHQL 99
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 100 VKQGRYpyqnwlkqwskeDEEAVERALKATKLE-DMA-----DRAV-----DSLSGGQRQRAWIAMTLAQETDIILLDEP 168
Cdd:TIGR01271 508 IFGLSY------------DEYRYTSVIKACQLEeDIAlfpekDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDSP 575
|
170
....*....|....
gi 499189069 169 TTYLDMTHQIEILD 182
Cdd:TIGR01271 576 FTHLDVVTEKEIFE 589
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
6-173 |
1.32e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 55.72 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGrAIAKLPTKEVAkelailp 85
Cdd:TIGR00957 639 VHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-SVAYVPQQAWI------- 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 86 QGPSAPEGLTVHQLVKQGRYpyqnwlkqwskedEEAVERALKATKLE--------DMADRAVDsLSGGQRQRAWIAMTLA 157
Cdd:TIGR00957 711 QNDSLRENILFGKALNEKYY-------------QQVLEACALLPDLEilpsgdrtEIGEKGVN-LSGGQKQRVSLARAVY 776
|
170
....*....|....*.
gi 499189069 158 QETDIILLDEPTTYLD 173
Cdd:TIGR00957 777 SNADIYLFDDPLSAVD 792
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-178 |
1.57e-08 |
|
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: 55.30 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 20 IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRgGSVLLEGRAIAKLPTKEVAKELAILPQGPSAPEGltvhqL 99
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSG-----T 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 100 VKQGRYPYQnwlkQWSkeDEE----AVERALKATkLEDMADR----AVDS---LSGGQRQRAWIAMTLAQETDIILLDEP 168
Cdd:TIGR01271 1308 FRKNLDPYE----QWS--DEEiwkvAEEVGLKSV-IEQFPDKldfvLVDGgyvLSNGHKQLMCLARSILSKAKILLLDEP 1380
|
170
....*....|.
gi 499189069 169 TTYLD-MTHQI 178
Cdd:TIGR01271 1381 SAHLDpVTLQI 1391
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
21-209 |
2.47e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 54.04 E-value: 2.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 21 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKP---------RGGSV-LLegRAIAKLPTKEVAKELAILPQGPSA 90
Cdd:PRK15093 23 VDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvtadrmRFDDIdLL--RLSPRERRKLVGHNVSMIFQEPQS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 91 ---PEGLTVHQLVK-------QGRYpYQ--NWLKQWSKEDEEAVerALKATKleDMADRAVDSLSGGQRQRAWIAMTLAQ 158
Cdd:PRK15093 101 cldPSERVGRQLMQnipgwtyKGRW-WQrfGWRKRRAIELLHRV--GIKDHK--DAMRSFPYELTEGECQKVMIAIALAN 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499189069 159 ETDIILLDEPTTYLDMTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYA 209
Cdd:PRK15093 176 QPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWA 226
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
6-253 |
4.64e-08 |
|
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: 52.60 E-value: 4.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDAV--IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAI 83
Cdd:cd03288 20 IKIHDLCVRYENNLkpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 84 LPQGPSAPEGLTVHQLVKQgrypyqnwlkqwSKEDEEAVERALKATKLEDMA-------DRAV----DSLSGGQRQRAWI 152
Cdd:cd03288 100 ILQDPILFSGSIRFNLDPE------------CKCTDDRLWEALEIAQLKNMVkslpgglDAVVteggENFSVGQRQLFCL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 153 AMTLAQETDIILLDEPTTYLDMTHQiEILDLLFeLNEKEDRTIVMVLHDLnlacryaHHLVAIKDKRIYAEGrpeEVITC 232
Cdd:cd03288 168 ARAFVRKSSILIMDEATASIDMATE-NILQKVV-MTAFADRTVVTIAHRV-------STILDADLVLVLSRG---ILVEC 235
|
250 260
....*....|....*....|.
gi 499189069 233 DLVQNVFSMncqvtQDPLFGT 253
Cdd:cd03288 236 DTPENLLAQ-----EDGVFAS 251
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
115-231 |
5.23e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 53.20 E-value: 5.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 115 SKEDEEA-VERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELnEKEDR 193
Cdd:NF000106 117 SRKDARArADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSM-VRDGA 195
|
90 100 110
....*....|....*....|....*....|....*...
gi 499189069 194 TIVMVLHDLNLACRYAHHLVAIKDKRIYAEGRPEEVIT 231
Cdd:NF000106 196 TVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKT 233
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
22-203 |
9.02e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.48 E-value: 9.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 22 DELNLTIPKGEITVFIGSNGCGKSTllrslarLMK------PRG---GSVLLEG--RAIAKLPTKE------VAKELAIL 84
Cdd:NF040905 18 DDVNLSVREGEIHALCGENGAGKST-------LMKvlsgvyPHGsyeGEILFDGevCRFKDIRDSEalgiviIHQELALI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 85 PQgpsapegLTVHQLVKQGRYPYQNWLKQWSKEDEEAVErALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIIL 164
Cdd:NF040905 91 PY-------LSIAENIFLGNERAKRGVIDWNETNRRARE-LLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLI 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 499189069 165 LDEPTTYLDMTHQIEILDLLFELnEKEDRTIVMVLHDLN 203
Cdd:NF040905 163 LDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLN 200
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
21-196 |
9.40e-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: 9.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 21 IDELNLTIPKGeITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLE----GRAIAKLPTKEVAKELA-----ILPQGPSAP 91
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSRKFDEedfyLGDDPDLPEIEIELTFGsllsrLLRLLLKEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 92 EGLTVHQLVKQGRYPYQNWLKQWSKEDEEAVERALKATKLE-DMADRAVDSLSG-----------------GQRQRAWIA 153
Cdd:COG3593 93 DKEELEEALEELNEELKEALKALNELLSEYLKELLDGLDLElELSLDELEDLLKslslriedgkelpldrlGSGFQRLIL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 499189069 154 MTLAQ---------ETDIILLDEPTTYLDMTHQIEILDLLFELNEKEDRTIV 196
Cdd:COG3593 173 LALLSalaelkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVII 224
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
9-173 |
1.15e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 51.57 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 9 ETLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLA--RLMKPRGGSVLLEGRAIAKLPTKEVAKE---LAI 83
Cdd:CHL00131 11 KNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAghPAYKILEGDILFKGESILDLEPEERAHLgifLAF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 84 lpQGPSAPEGLTVHQLVkqgRYPYQNWLKQWSKEDEEAVE-RALKATKLE--DMA----DRAV-DSLSGGQRQRAWIAMT 155
Cdd:CHL00131 91 --QYPIEIPGVSNADFL---RLAYNSKRKFQGLPELDPLEfLEIINEKLKlvGMDpsflSRNVnEGFSGGEKKRNEILQM 165
|
170
....*....|....*...
gi 499189069 156 LAQETDIILLDEPTTYLD 173
Cdd:CHL00131 166 ALLDSELAILDETDSGLD 183
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
18-182 |
1.20e-07 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 51.78 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 18 AVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRaiaklptkevakeLAILPQGPSAPEGLTVH 97
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIKE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 98 QLVKQGRYpyqnwlkqwskeDEEAVERALKATKLED------------MADRAVdSLSGGQRQRAWIAMTLAQETDIILL 165
Cdd:cd03291 117 NIIFGVSY------------DEYRYKSVVKACQLEEditkfpekdntvLGEGGI-TLSGGQRARISLARAVYKDADLYLL 183
|
170
....*....|....*..
gi 499189069 166 DEPTTYLDMTHQIEILD 182
Cdd:cd03291 184 DSPFGYLDVFTEKEIFE 200
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
21-202 |
1.29e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 52.13 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 21 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPR-GGSVLLEGRAIA-KLPTKEVAKELAILPqgpsapEGLTVHQ 98
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDiRNPAQAIRAGIAMVP------EDRKRHG 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 99 LVKQ---GRYPYQNWLKQWSK-------EDEEAVERALKATKLEDMA-DRAVDSLSGGQRQRAWIAMTLAQETDIILLDE 167
Cdd:TIGR02633 350 IVPIlgvGKNITLSVLKSFCFkmridaaAELQIIGSAIQRLKVKTASpFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDE 429
|
170 180 190
....*....|....*....|....*....|....*
gi 499189069 168 PTTYLDMTHQIEILDLLFELnEKEDRTIVMVLHDL 202
Cdd:TIGR02633 430 PTRGVDVGAKYEIYKLINQL-AQEGVAIIVVSSEL 463
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
6-178 |
1.95e-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: 51.01 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 6 ISTETLSLGYGDA--VIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGgSVLLEGRAIAKLPTKEVAKELAI 83
Cdd:cd03289 3 MTVKDLTAKYTEGgnAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEG-DIQIDGVSWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 84 LPQGPSAPEGLtvhqlVKQGRYPYQNWlkqwskEDEE----AVERALKaTKLEDMADRA----VDS---LSGGQRQRAWI 152
Cdd:cd03289 82 IPQKVFIFSGT-----FRKNLDPYGKW------SDEEiwkvAEEVGLK-SVIEQFPGQLdfvlVDGgcvLSHGHKQLMCL 149
|
170 180
....*....|....*....|....*..
gi 499189069 153 AMTLAQETDIILLDEPTTYLD-MTHQI 178
Cdd:cd03289 150 ARSVLSKAKILLLDEPSAHLDpITYQV 176
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-199 |
2.12e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.55 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 1 MGMSAISTETLSLGYGDAVIIDELnlTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKE 80
Cdd:PRK10938 1 MSSLQISQGTFRLSDTKTLQLPSL--TLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 81 LAILPQ-----GPSAPE---GLTVHQLVkqgrypyqnwlkQWSKEDEEAVERALKATKLEDMADRAVDSLSGGQRQRAWI 152
Cdd:PRK10938 79 VSDEWQrnntdMLSPGEddtGRTTAEII------------QDEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499189069 153 AMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELNeKEDRTIVMVL 199
Cdd:PRK10938 147 CQALMSEPDLLILDEPFDGLDVASRQQLAELLASLH-QSGITLVLVL 192
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
10-174 |
2.18e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 51.71 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 10 TLSLGYGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGR-AIAklptkEVAKELAILPQgp 88
Cdd:PRK10636 6 SLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwQLA-----WVNQETPALPQ-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 89 SAPEgltvhqLVKQGRYPYqnwlKQWSKEDEEAVER--------------ALKATKLEDMA--------------DRAVD 140
Cdd:PRK10636 79 PALE------YVIDGDREY----RQLEAQLHDANERndghaiatihgkldAIDAWTIRSRAasllhglgfsneqlERPVS 148
|
170 180 190
....*....|....*....|....*....|....
gi 499189069 141 SLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDM 174
Cdd:PRK10636 149 DFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDL 182
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
21-169 |
3.88e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 50.80 E-value: 3.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 21 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKE-LAILPQGPSApEGL----T 95
Cdd:COG3845 274 LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYIPEDRLG-RGLvpdmS 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 96 VHQ---LVKQGRYPYQNW-LKQWSKEDEEAVEralkatKLEDM------ADRAVDSLSGGQRQRAWIAMTLAQETDIILL 165
Cdd:COG3845 353 VAEnliLGRYRRPPFSRGgFLDRKAIRAFAEE------LIEEFdvrtpgPDTPARSLSGGNQQKVILARELSRDPKLLIA 426
|
....
gi 499189069 166 DEPT 169
Cdd:COG3845 427 AQPT 430
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-220 |
7.02e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.24 E-value: 7.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 2 GMSAISTETLSLGY-GDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAiaklptkevakE 80
Cdd:PLN03073 505 GPPIISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKV-----------R 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 81 LAILPQGPSAPEGLTVHQLVKQGR-YPyqnwlkqwskedeEAVERALKA-----TKLEDMADRAVDSLSGGQRQRAWIAM 154
Cdd:PLN03073 574 MAVFSQHHVDGLDLSSNPLLYMMRcFP-------------GVPEQKLRAhlgsfGVTGNLALQPMYTLSGGQKSRVAFAK 640
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499189069 155 TLAQETDIILLDEPTTYLDMThQIEILD---LLFElnekedRTIVMVLHDLNLACRYAHHLVAIKDKRI 220
Cdd:PLN03073 641 ITFKKPHILLLDEPSNHLDLD-AVEALIqglVLFQ------GGVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
37-206 |
8.26e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.89 E-value: 8.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 37 IGSNGCGKSTLLRSLARLMKPRGGSVLLEgraiaklPTKEVAKelaiLPQGPSAPEGLTVHQLVKQGRypyqnwLKQWS- 115
Cdd:PRK15064 33 IGANGCGKSTFMKILGGDLEPSAGNVSLD-------PNERLGK----LRQDQFAFEEFTVLDTVIMGH------TELWEv 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 116 KEDEEAV--------ERALKATKLE------D--MAD-RAVDSLSG-----------------GQRQRAWIAMTLAQETD 161
Cdd:PRK15064 96 KQERDRIyalpemseEDGMKVADLEvkfaemDgyTAEaRAGELLLGvgipeeqhyglmsevapGWKLRVLLAQALFSNPD 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499189069 162 IILLDEPTTYLDMtHQIEILDLlfELNEKeDRTIVMVLHD---LNLAC 206
Cdd:PRK15064 176 ILLLDEPTNNLDI-NTIRWLED--VLNER-NSTMIIISHDrhfLNSVC 219
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-200 |
8.89e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.11 E-value: 8.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 16 GDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLRSLA-RLMKP--RGGSVLLEGRAIaklpTKEVAKELAILPQGPSAPE 92
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAeRVTTGviTGGDRLVNGRPL----DSSFQRSIGYVQQQDLHLP 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 93 GLTVHQLVKqgrypYQNWLKQWS----KEDEEAVERALKATKLEDMADRAV----DSLSGGQRQRAWIAMTLAQETDIIL 164
Cdd:TIGR00956 850 TSTVRESLR-----FSAYLRQPKsvskSEKMEYVEEVIKLLEMESYADAVVgvpgEGLNVEQRKRLTIGVELVAKPKLLL 924
|
170 180 190
....*....|....*....|....*....|....*..
gi 499189069 165 -LDEPTTYLDMTHQIEILDLLFELnEKEDRTIVMVLH 200
Cdd:TIGR00956 925 fLDEPTSGLDSQTAWSICKLMRKL-ADHGQAILCTIH 960
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
20-202 |
9.30e-07 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 49.71 E-value: 9.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 20 IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAILPQGP---SApeglTV 96
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPflfSD----TV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 97 HQLVKQGRypyqnwlKQWSKEDEEAVERAlkATKLEDM-----------ADRAVdSLSGGQRQRAWIAMTLAQETDIILL 165
Cdd:PRK10789 406 ANNIALGR-------PDATQQEIEHVARL--ASVHDDIlrlpqgydtevGERGV-MLSGGQKQRISIARALLLNAEILIL 475
|
170 180 190
....*....|....*....|....*....|....*..
gi 499189069 166 DEPTTYLDMTHQIEILDLLFELNEKedRTIVMVLHDL 202
Cdd:PRK10789 476 DDALSAVDGRTEHQILHNLRQWGEG--RTVIISAHRL 510
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-198 |
1.64e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.85 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 21 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAI-AKLPTKEVAKELAILPQGPSApEGLTVHQL 99
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvTRSPQDGLANGIVYISEDRKR-DGLVLGMS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 100 VKQG------RYPYQNWLKQWSKEDEEAVERALKA--TKLEDMaDRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTY 171
Cdd:PRK10762 347 VKENmsltalRYFSRAGGSLKHADEQQAVSDFIRLfnIKTPSM-EQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRG 425
|
170 180
....*....|....*....|....*..
gi 499189069 172 LDMTHQIEILDLLFELnEKEDRTIVMV 198
Cdd:PRK10762 426 VDVGAKKEIYQLINQF-KAEGLSIILV 451
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
21-184 |
1.94e-06 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 48.07 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 21 IDELNLTIPKGE-ITVFIGSNGCGKSTLLRSLARLMKP---------------RGGSVLLEGRAIA------KLPTKEVA 78
Cdd:COG3950 14 FEDLEIDFDNPPrLTVLVGENGSGKTTLLEAIALALSGllsrlddvkfrklliRNGEFGDSAKLILyygtsrLLLDGPLK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 79 KELAILPQGPSAPEGLT--------VHQLVKQGRYPYQNWLKQWSKEDE---EAVERALKA------------------T 129
Cdd:COG3950 94 KLERLKEEYFSRLDGYDslldedsnLREFLEWLREYLEDLENKLSDELDeklEAVREALNKllpdfkdiridrdpgrlvI 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499189069 130 KLEDMADRAVDSLSGGQRQR----AWIAMTLAQ---------ETD-IILLDEPTTYLDMTHQIEILDLL 184
Cdd:COG3950 174 LDKNGEELPLNQLSDGERSLlalvGDLARRLAElnpalenplEGEgIVLIDEIDLHLHPKWQRRILPDL 242
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-245 |
2.84e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.43 E-value: 2.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 21 IDELNLTIPKGEITVFIGSNGCGKSTLLRS-LARLMKPRGGSVLLEGraiaklptkevakELAILPQGP-----SAPEGL 94
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAmLGELSHAETSSVVIRG-------------SVAYVPQVSwifnaTVRENI 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 95 TVHQLVKQGRYpyqnwlkqWSKEDEEAVERALK---ATKLEDMADRAVDsLSGGQRQRAWIAMTLAQETDIILLDEPTTY 171
Cdd:PLN03232 700 LFGSDFESERY--------WRAIDVTALQHDLDllpGRDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDIYIFDDPLSA 770
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499189069 172 LD--MTHQIEILDLLFELNEKEDRTIVMVLHDLNLACRYAhhLVA---IKDKRIYAEGRPEEVITCDLVQNVFSMNCQV 245
Cdd:PLN03232 771 LDahVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRII--LVSegmIKEEGTFAELSKSGSLFKKLMENAGKMDATQ 847
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
21-203 |
4.85e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.58 E-value: 4.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 21 IDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAklptkevakeLAIlpqgpsaPEGLTvHQLV 100
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAAL----------IAI-------SSGLN-GQLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 101 KQGRYPYQNWLKQWSKED-EEAVERALKATKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIE 179
Cdd:PRK13545 102 GIENIELKGLMMGLTKEKiKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKK 181
|
170 180
....*....|....*....|....
gi 499189069 180 ILDLLFELNEKeDRTIVMVLHDLN 203
Cdd:PRK13545 182 CLDKMNEFKEQ-GKTIFFISHSLS 204
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
37-179 |
5.04e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.85 E-value: 5.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 37 IGSNGCGKSTLLRSLARLMKPRGGSVLLEGRAIAKLPTKEVAKELAILPQGPSAPEGlTVHQLVKqgryPYqnwLKQWSK 116
Cdd:PTZ00243 1342 VGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDG-TVRQNVD----PF---LEASSA 1413
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499189069 117 EDEEAVE----RALKATKLEDMADRAVD---SLSGGQRQRAWIAMTLAQE-TDIILLDEPTTYLD--MTHQIE 179
Cdd:PTZ00243 1414 EVWAALElvglRERVASESEGIDSRVLEggsNYSVGQRQLMCMARALLKKgSGFILMDEATANIDpaLDRQIQ 1486
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
138-198 |
5.09e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.42 E-value: 5.09e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499189069 138 AVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIEILDLLFELnEKEDRTIVMV 198
Cdd:PRK10982 388 QIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAEL-AKKDKGIIII 447
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
21-61 |
1.39e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 45.14 E-value: 1.39e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 499189069 21 IDELNLTIPkgeITVFIGSNGCGKSTLLRSLARLM--KPRGGS 61
Cdd:COG3910 30 LEGLEFHPP---VTFFVGENGSGKSTLLEAIAVAAgfNPEGGS 69
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
25-54 |
3.99e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 44.54 E-value: 3.99e-05
10 20 30
....*....|....*....|....*....|
gi 499189069 25 NLTIPKGEITVFIGSNGCGKSTLLRSLARL 54
Cdd:COG4637 15 DLELPLGPLTVLIGANGSGKSNLLDALRFL 44
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
133-174 |
5.19e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.47 E-value: 5.19e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 499189069 133 DMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDM 174
Cdd:PLN03073 336 EMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
20-198 |
5.41e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 44.15 E-value: 5.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 20 IIDELNLTIPKGEITVFIGSNGCGKSTLLRSLARLMKPR-GGSVLLEGRAIA-KLPTKEVAKELAILPqgpsapEGLTVH 97
Cdd:PRK13549 277 RVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRwEGEIFIDGKPVKiRNPQQAIAQGIAMVP------EDRKRD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 98 QLVKQ---GRYPYQNWLKQWSKE---DEEA----VERALKATKLEDM-ADRAVDSLSGGQRQRAWIAMTLAQETDIILLD 166
Cdd:PRK13549 351 GIVPVmgvGKNITLAALDRFTGGsriDDAAelktILESIQRLKVKTAsPELAIARLSGGNQQKAVLAKCLLLNPKILILD 430
|
170 180 190
....*....|....*....|....*....|..
gi 499189069 167 EPTTYLDMTHQIEILDLLFELnEKEDRTIVMV 198
Cdd:PRK13549 431 EPTRGIDVGAKYEIYKLINQL-VQQGVAIIVI 461
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
28-130 |
9.59e-05 |
|
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: 42.37 E-value: 9.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 28 IPKGEITVFIGSNGCGKSTLLRSLA-----------RLMKPRGGSVLL---EGRAiaklptKEVAKELAILPQGPSAPEG 93
Cdd:pfam13481 30 LPAGGLGLLAGAPGTGKTTLALDLAaavatgkpwlgGPRVPEQGKVLYvsaEGPA------DELRRRLRAAGADLDLPAR 103
|
90 100 110
....*....|....*....|....*....|....*..
gi 499189069 94 LTVHQLVKQGRYPYQNWLKQWSKEDEEAVERALKATK 130
Cdd:pfam13481 104 LLFLSLVESLPLFFLDRGGPLLDADVDALEAALEEVE 140
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
31-173 |
1.44e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 43.30 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 31 GEITVFIGSNGCGKSTLLRSLARlmKPRGGSVLLEGRaIAKLPTKE--VAKELAILPQGPSAPEGLTVHQ-LVKQG--RY 105
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEGDIR-ISGFPKKQetFARISGYCEQNDIHSPQVTVREsLIYSAflRL 982
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499189069 106 PyqnwlKQWSKEDEEA-VERALKATKLEDMADR-----AVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLD 173
Cdd:PLN03140 983 P-----KEVSKEEKMMfVDEVMELVELDNLKDAivglpGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
24-215 |
3.27e-04 |
|
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: 41.09 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 24 LNLTIPKGEITVFIGSNGCGKSTL----------------LRSLARlmkprggsvllegRAIAKLPTKEVakelailpqg 87
Cdd:cd03270 14 VDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryvesLSAYAR-------------QFLGQMDKPDV---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 88 pSAPEGLTVHQLVKQGR---------------YPYQNWLkqWSKEDEEAVERALKATKLEDMA-DRAVDSLSGGQRQRAW 151
Cdd:cd03270 71 -DSIEGLSPAIAIDQKTtsrnprstvgtvteiYDYLRLL--FARVGIRERLGFLVDVGLGYLTlSRSAPTLSGGEAQRIR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499189069 152 IAMTL-AQETDII-LLDEPTTYLDMTHQIEILDLLFELNEKeDRTIVMVLHDLNLAcRYAHHLVAI 215
Cdd:cd03270 148 LATQIgSGLTGVLyVLDEPSIGLHPRDNDRLIETLKRLRDL-GNTVLVVEHDEDTI-RAADHVIDI 211
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
141-230 |
3.55e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.92 E-value: 3.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 141 SLSGGQRQRAWIAMTLAQETD---IILLDEPTTYLDMTHQIEILDLLFELNEKEDrTIVMVLHDLNLAcRYAHHLVAI-- 215
Cdd:TIGR00630 829 TLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLHFDDIKKLLEVLQRLVDKGN-TVVVIEHNLDVI-KTADYIIDLgp 906
|
90
....*....|....*....
gi 499189069 216 ----KDKRIYAEGRPEEVI 230
Cdd:TIGR00630 907 eggdGGGTVVASGTPEEVA 925
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
21-187 |
8.87e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 39.95 E-value: 8.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 21 IDELNLTIpkGEITVFIGSNGCGKSTLLRSLARLMKPRggSVLLE-GRAIAKLPTKEVAKELAIL-PQGPSAPEGLTVHQ 98
Cdd:COG4938 12 FKEAELEL--KPLTLLIGPNGSGKSTLIQALLLLLQSN--FIYLPaERSGPARLYPSLVRELSDLgSRGEYTADFLAELE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 99 LVKQGRYP-------YQNWLKQ---------WSKEDEEAVERALKATKLEDMADravdsLSGGQRQRAWIAMTL---AQE 159
Cdd:COG4938 88 NLEILDDKskelleqVEEWLEKifpgkvevdASSDLVRLVFRPSGNGKRIPLSN-----VGSGVSELLPILLALlsaAKP 162
|
170 180
....*....|....*....|....*...
gi 499189069 160 TDIILLDEPTTYLDMTHQIEILDLLFEL 187
Cdd:COG4938 163 GSLLIIEEPEAHLHPKAQSALAELLAEL 190
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
15-67 |
1.65e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 39.61 E-value: 1.65e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 499189069 15 YGDAVIIDELNLTIPKGEITVFIGSNGCGKSTLLrSLARLMKPRGGS--VLLEGR 67
Cdd:PRK10938 270 YNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLL-SLITGDHPQGYSndLTLFGR 323
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
33-259 |
2.42e-03 |
|
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: 38.91 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 33 ITVFIGSNGCGKSTLLRSLARLmkpRGGSVLLEGRAIAKLPTKEVAKELAILPQGPSAPEG-LTVHQLVKQG-RYPY--- 107
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFL---ADFDALVIGLTDERSRNGGIGGIPSLLNGIDPKEPIeFEISEFLEDGvRYRYgld 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 108 --QNWLKQWSKEDEEAVERALkaTKLEDMADRAVDSLSGGQRQRAWIAMTLAQETDIILLDEPTTYLDMTHQIE----IL 181
Cdd:pfam13304 78 leREDVEEKLSSKPTLLEKRL--LLREDSEEREPKFPPEAEELRLGLDVEERIELSLSELSDLISGLLLLSIISplsfLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 182 DLLFELNEKEDRTIVMV--LHDLNLACRYAHHLVAIKDKRIYAEGRPEEVI-TCDLVQNVFSMNCQVTQDPLFGTPLCIP 258
Cdd:pfam13304 156 LLDEGLLLEDWAVLDLAadLALFPDLKELLQRLVRGLKLADLNLSDLGEGIeKSLLVDDRLRERGLILLENGGGGELPAF 235
|
.
gi 499189069 259 H 259
Cdd:pfam13304 236 E 236
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
136-232 |
6.73e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 37.69 E-value: 6.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499189069 136 DRAVDSLSGGQRQRAWIAMTL-AQETDII-LLDEPTTYLdmtHQIEILDLLFELNEKED--RTIVMVLHDLNlACRYAHH 211
Cdd:TIGR00630 483 SRAAGTLSGGEAQRIRLATQIgSGLTGVLyVLDEPSIGL---HQRDNRRLINTLKRLRDlgNTLIVVEHDED-TIRAADY 558
|
90 100
....*....|....*....|....*..
gi 499189069 212 LVAIKDK------RIYAEGRPEEVITC 232
Cdd:TIGR00630 559 VIDIGPGagehggEVVASGTPEEILAN 585
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
30-52 |
6.76e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 36.75 E-value: 6.76e-03
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
32-51 |
7.70e-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: 7.70e-03
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
136-201 |
8.03e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 37.89 E-value: 8.03e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499189069 136 DRAVDSLSGGQRQRAWIAMTLAQETDII--LLDEPTTYLDMTHQIEILDLLFELNEKEDrTIVMVLHD 201
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRDQGN-TVLLVEHD 537
|
|
| |
