|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1-265 |
0e+00 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 559.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 1 MTESVARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA 80
Cdd:PRK10253 1 MTESVARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 81 RRIGLLAQNATTLGDITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQ 160
Cdd:PRK10253 81 RRIGLLAQNATTPGDITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 161 ETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERI 240
Cdd:PRK10253 161 ETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERI 240
|
250 260
....*....|....*....|....*
gi 15829881 241 YGLRCMIIDDPVAGTPLVVPLGRTA 265
Cdd:PRK10253 241 YGLRCMIIDDPVAGTPLVVPLGRTA 265
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
7-260 |
1.73e-140 |
|
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: 395.18 E-value: 1.73e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 7 RLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLL 86
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 87 AQNATTLGDITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIML 166
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGRYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 167 LDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYGLRCM 246
Cdd:COG1120 161 LDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVYGVEAR 240
|
250
....*....|....
gi 15829881 247 IIDDPVAGTPLVVP 260
Cdd:COG1120 241 VIEDPVTGRPLVLP 254
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
8-259 |
1.44e-119 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 341.99 E-value: 1.44e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLA 87
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 88 QNATTLGDITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
Cdd:PRK11231 83 QHHLTPEGITVRELVAYGRSPWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 168 DEPTTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYGLRCMI 247
Cdd:PRK11231 163 DEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVFDVEAEI 241
|
250
....*....|..
gi 15829881 248 IDDPVAGTPLVV 259
Cdd:PRK11231 242 HPEPVSGTPMCV 253
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
11-260 |
5.65e-90 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 266.95 E-value: 5.65e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQ-N 89
Cdd:COG4604 5 KNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQeN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 90 ATTLgDITVQELVARGRYPHqplfTRWR--KEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
Cdd:COG4604 85 HINS-RLTVRELVAFGRFPY----SKGRltAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 168 DEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYGLRCMI 247
Cdd:COG4604 160 DEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEVLSDIYDTDIEV 239
|
250
....*....|...
gi 15829881 248 IDdpVAGTPLVVP 260
Cdd:COG4604 240 EE--IDGKRICVY 250
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
8-260 |
1.60e-85 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 255.81 E-value: 1.60e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLA 87
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 88 QnATTLG-DITVQELVARGRYPHQplftRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQ------ 160
Cdd:COG4559 82 Q-HSSLAfPFTVEEVVALGRAPHG----SSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQlwepvd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 161 -ETAIMLLDEPTTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIER 239
Cdd:COG4559 157 gGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELLER 235
|
250 260
....*....|....*....|.
gi 15829881 240 IYGLRCMIIDDPVAGTPLVVP 260
Cdd:COG4559 236 VYGADLRVLAHPEGGCPQVLP 256
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
8-260 |
6.93e-85 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 254.31 E-value: 6.93e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLA 87
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 88 QNATTLGDITVQELVARGRYPHqplfTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQ------E 161
Cdd:PRK13548 83 QHSSLSFPFTVEEVVAMGRAPH----GLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepdgP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 162 TAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIY 241
Cdd:PRK13548 159 PRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPETLRRVY 238
|
250
....*....|....*....
gi 15829881 242 GLRCMIIDDPVAGTPLVVP 260
Cdd:PRK13548 239 GADVLVQPHPETGAPLVLP 257
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
11-226 |
1.41e-84 |
|
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: 250.43 E-value: 1.41e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQna 90
Cdd:cd03214 3 ENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 91 ttlgditvqelvargryphqplftrwrkedeeavtkAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
Cdd:cd03214 81 ------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15829881 171 TTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG 226
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-244 |
5.40e-76 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 231.13 E-value: 5.40e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 1 MTESVArLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIqhyasKEVA 80
Cdd:COG1121 1 MMMMPA-IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP-----RRAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 81 RRIGLLAQNATTLGD--ITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVL 158
Cdd:COG1121 75 RRIGYVPQRAEVDWDfpITVRDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 159 AQETAIMLLDEPTTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGkIVAQGAPKEIVTAELIE 238
Cdd:COG1121 155 AQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVLTPENLS 232
|
....*.
gi 15829881 239 RIYGLR 244
Cdd:COG1121 233 RAYGGP 238
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
21-257 |
9.48e-76 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 231.21 E-value: 9.48e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTLGDITVQE 100
Cdd:PRK10575 25 TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGMTVRE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 101 LVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQI 180
Cdd:PRK10575 105 LVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQV 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15829881 181 DLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYGLRCMIIDDPVAGTPL 257
Cdd:PRK10575 185 DVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIYGIPMGILPHPAGAAPV 261
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
13-271 |
1.35e-68 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 217.40 E-value: 1.35e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 13 LTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATT 92
Cdd:PRK09536 9 LSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 93 LGDITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
Cdd:PRK09536 89 SFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 173 WLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYGLRCMIIDDPV 252
Cdd:PRK09536 169 SLDINHQVRTLELVRRL-VDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFDARTAVGTDPA 247
|
250
....*....|....*....
gi 15829881 253 AGTPLVVPLGRTAPSTANS 271
Cdd:PRK09536 248 TGAPTVTPLPDPDRTEAAA 266
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
11-226 |
1.41e-67 |
|
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: 208.54 E-value: 1.41e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIqhyasKEVARRIGLLAQNA 90
Cdd:cd03235 3 EDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL-----EKERKRIGYVPQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 91 TTLGD--ITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168
Cdd:cd03235 78 SIDRDfpISVRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15829881 169 EPTTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALrEGKIVAQG 226
Cdd:cd03235 158 EPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
8-242 |
6.19e-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: 6.19e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 8 LRGEQLTLGYGKYTVA-ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA---RRI 83
Cdd:COG3638 3 LELRNLSKRYPGGTPAlDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRrlrRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 84 GLLAQNATTLGDITVQELVARGRYPHQP----LFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLA 159
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNVLAGRLGRTStwrsLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARALV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 160 QETAIMLLDEPTTWLD--ISHQIdlLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEiVTAELI 237
Cdd:COG3638 163 QEPKLILADEPVASLDpkTARQV--MDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAE-LTDAVL 239
|
....*
gi 15829881 238 ERIYG 242
Cdd:COG3638 240 REIYG 244
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
11-239 |
6.46e-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: 192.16 E-value: 6.46e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 11 EQLTLGY-GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQN 89
Cdd:COG1122 4 ENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLVFQN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 90 ATT-LGDITVQELVARGryphqPLFTRWRKED-EEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
Cdd:COG1122 84 PDDqLFAPTVEEDVAFG-----PENLGLPREEiRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15829881 168 DEPTTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVT-AELIER 239
Cdd:COG1122 159 DEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSdYELLEE 230
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
8-241 |
1.74e-57 |
|
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: 183.92 E-value: 1.74e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 8 LRGEQLTLGYGKYTVA-ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHI---QHYASKEVARRI 83
Cdd:cd03256 1 IEVENLSKTYPNGKKAlKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 84 GLLAQNATTLGDITVQELVARGRYPH----QPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLA 159
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRLGRrstwRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 160 QETAIMLLDEPTTWLD--ISHQIdlLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIvTAELI 237
Cdd:cd03256 161 QQPKLILADEPVASLDpaSSRQV--MDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL-TDEVL 237
|
....
gi 15829881 238 ERIY 241
Cdd:cd03256 238 DEIY 241
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
8-242 |
2.55e-56 |
|
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: 180.96 E-value: 2.55e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 8 LRGEQLTLGYGKYTVA-ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKE---VARRI 83
Cdd:TIGR02315 2 LEVENLSKVYPNGKQAlKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrkLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 84 GLLAQNATTLGDITVQELVARGRYPHQP----LFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLA 159
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVLHGRLGYKPtwrsLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 160 QETAIMLLDEPTTWLD--ISHQIdlLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIvTAELI 237
Cdd:TIGR02315 162 QQPDLILADEPIASLDpkTSKQV--MDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL-DDEVL 238
|
....*
gi 15829881 238 ERIYG 242
Cdd:TIGR02315 239 RHIYG 243
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
11-221 |
2.63e-51 |
|
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: 166.87 E-value: 2.63e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 11 EQLTLGYGKYTVA--ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQ 88
Cdd:cd03225 3 KNLSFSYPDGARPalDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 89 NATT--LGDiTVQELVARG-RYPHQPlftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIM 165
Cdd:cd03225 83 NPDDqfFGP-TVEEEVAFGlENLGLP-----EEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15829881 166 LLDEPTTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGK 221
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
11-241 |
8.05e-51 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 166.39 E-value: 8.05e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyASKEVARRIGLLAQNA 90
Cdd:COG1131 4 RGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGYVPQEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 91 TTLGDITVQELVargRYpHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
Cdd:COG1131 83 ALYPDLTVRENL---RF-FARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15829881 171 TTWLDISHQIDLLELLSELNREKgytlAAVL---HDLNQACRYASHLIALREGKIVAQGAPKEIvTAELIERIY 241
Cdd:COG1131 159 TSGLDPEARRELWELLRELAAEG----KTVLlstHYLEEAERLCDRVAIIDKGRIVADGTPDEL-KARLLEDVF 227
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
8-233 |
4.79e-49 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 161.84 E-value: 4.79e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARR-IGLL 86
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 87 AQNATTLGDITVQE---LVARGRYPHQPLFTRWRKEDEEAVTKAMQA---TGITHLADQSVDTLSGGQRQRAWIAMVLAQ 160
Cdd:cd03219 81 FQIPRLFPELTVLEnvmVAAQARTGSGLLLARARREEREARERAEELlerVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15829881 161 ETAIMLLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVT 233
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-235 |
4.08e-48 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 159.76 E-value: 4.08e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 1 MTESVARLRGeqLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKE-- 78
Cdd:COG1127 1 MSEPMIEVRN--LTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKEly 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 79 -VARRIGLLAQNATTLGDITVQELVArgryphQPL--FTRW-RKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWI 154
Cdd:COG1127 79 eLRRRIGMLFQGGALFDSLTVFENVA------FPLreHTDLsEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 155 AMVLAQETAIMLLDEPTTWLDI--SHQIDllELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV 232
Cdd:COG1127 153 ARALALDPEILLYDEPTAGLDPitSAVID--ELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELL 230
|
...
gi 15829881 233 TAE 235
Cdd:COG1127 231 ASD 233
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
8-226 |
6.14e-48 |
|
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: 158.45 E-value: 6.14e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLA 87
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER--RNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 88 QNATTLGDITVQELVARGRYPHqplftRWRKEDEEA-VTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIML 166
Cdd:cd03259 79 QDYALFPHLTVAENIAFGLKLR-----GVPKAEIRArVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 167 LDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG 226
Cdd:cd03259 154 LDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
7-233 |
6.32e-47 |
|
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: 156.51 E-value: 6.32e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 7 RLRGeqLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKE---VARRI 83
Cdd:cd03261 2 ELRG--LTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 84 GLLAQNATTLGDITVQELVArgrYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETA 163
Cdd:cd03261 80 GMLFQSGALFDSLTVFENVA---FPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15829881 164 IMLLDEPTTWLD--ISHQIDllELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVT 233
Cdd:cd03261 157 LLLYDEPTAGLDpiASGVID--DLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
8-244 |
3.99e-46 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 161.22 E-value: 3.99e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 8 LRGEQLTLGY-----GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHY---ASKEV 79
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLsrrSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 80 ARRIGLLAQNAT-------TLGDItVQE-LVARGRYPhqplftrwRKEDEEAVTKAMQATGI-THLADQSVDTLSGGQRQ 150
Cdd:COG1123 341 RRRVQMVFQDPYsslnprmTVGDI-IAEpLRLHGLLS--------RAERRERVAELLERVGLpPDLADRYPHELSGGQRQ 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 151 RAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG---- 226
Cdd:COG1123 412 RVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGptee 491
|
250 260
....*....|....*....|.
gi 15829881 227 ---APKEIVTAELIERIYGLR 244
Cdd:COG1123 492 vfaNPQHPYTRALLAAVPSLD 512
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-234 |
8.34e-46 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 160.45 E-value: 8.34e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 3 ESVARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPA---HGHVWLDGEHIQHYASKEV 79
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 80 ARRIGLLAQNATT-LGDITVQELVARGRYphqpLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVL 158
Cdd:COG1123 82 GRRIGMVFQDPMTqLNPVTVGDQIAEALE----NLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15829881 159 AQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTA 234
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
8-260 |
1.32e-45 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 154.21 E-value: 1.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPA--------HGHVWLDGEHIQHYASKEV 79
Cdd:PRK13547 2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 80 ARRIGLLAQNATTLGDITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLA 159
Cdd:PRK13547 82 ARLRAVLPQAAQPAFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 160 Q---------ETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKE 230
Cdd:PRK13547 162 QlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPAD 241
|
250 260 270
....*....|....*....|....*....|
gi 15829881 231 IVTAELIERIYGLRCMIIDDPVAGTPLVVP 260
Cdd:PRK13547 242 VLTPAHIARCYGFAVRLVDAGDGVPPVIVP 271
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
8-222 |
2.57e-45 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 151.51 E-value: 2.57e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLA 87
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 88 QNATTLGDiTVQELVARgryphqPLFTRWRKEDEEAVTKAMQATGITH-LADQSVDTLSGGQRQRAWIAMVLAQETAIML 166
Cdd:COG4619 81 QEPALWGG-TVRDNLPF------PFQLRERKFDRERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15829881 167 LDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKI 222
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
24-231 |
5.12e-45 |
|
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: 152.99 E-value: 5.12e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHY---ASKEVARRIGLLAQNA-TTLGDITVQ 99
Cdd:TIGR04521 22 DDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKkkkKLKDLRKKVGLVFQFPeHQLFEETVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 100 ELVARGryPHQplFTRWRKEDEEAVTKAMQATGITH-LADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISH 178
Cdd:TIGR04521 102 KDIAFG--PKN--LGLSEEEAEERVKEALELVGLDEeYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKG 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15829881 179 QIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
Cdd:TIGR04521 178 RKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREV 230
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
8-238 |
6.01e-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: 149.18 E-value: 6.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 8 LRGEQLTLGYGKY----TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRI 83
Cdd:COG1124 2 LEVRNLSVSYGQGgrrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 84 GLLAQNATtlGDI----TVQELVArgryphQPLFTRWRKEDEEAVTKAMQATGIT-HLADQSVDTLSGGQRQRAWIAMVL 158
Cdd:COG1124 82 QMVFQDPY--ASLhprhTVDRILA------EPLRIHGLPDREERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 159 AQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV------ 232
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLagpkhp 233
|
....*..
gi 15829881 233 -TAELIE 238
Cdd:COG1124 234 yTRELLA 240
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
11-231 |
1.01e-43 |
|
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: 148.47 E-value: 1.01e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYaSKEVARRIGLLAQNA 90
Cdd:COG4555 5 ENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKE-PREARRQIGVLPDER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 91 TTLGDITVQELVargRYpHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
Cdd:COG4555 84 GLYDRLTVRENI---RY-FAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15829881 171 TTWLDISHQIDLLELLSELNREKGytlaAVL---HDLNQACRYASHLIALREGKIVAQGAPKEI 231
Cdd:COG4555 160 TNGLDVMARRLLREILRALKKEGK----TVLfssHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
8-222 |
8.24e-43 |
|
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: 145.33 E-value: 8.24e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 8 LRGEQLTLGYG----KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA--- 80
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 81 -RRIGLLAQNATTLGDITVQELVArgrYPhQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLA 159
Cdd:cd03255 81 rRHIGFVFQSFNLLPDLTALENVE---LP-LLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15829881 160 QETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQAcRYASHLIALREGKI 222
Cdd:cd03255 157 NDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
8-231 |
8.24e-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: 146.34 E-value: 8.24e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRiGlLA 87
Cdd:COG0411 5 LEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARL-G-IA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 88 ---QNATTLGDITVQE--LVARGRYPHQPLFT------RWRKEDEEAVTKAMQA---TGITHLADQSVDTLSGGQRQRAW 153
Cdd:COG0411 83 rtfQNPRLFPELTVLEnvLVAAHARLGRGLLAallrlpRARREEREARERAEELlerVGLADRADEPAGNLSYGQQRRLE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15829881 154 IAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
Cdd:COG0411 163 IARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEV 240
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
16-217 |
1.76e-42 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 143.53 E-value: 1.76e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 16 GYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwldgehiqhyaSKEVARRIGLLAQNaTTLGD 95
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----------RRAGGARVAYVPQR-SEVPD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 96 ---ITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
Cdd:NF040873 69 slpLTVRDLVAMGRWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15829881 173 WLDISHQIDLLELLSELNREkGYTLAAVLHDLNQAcRYASHLIAL 217
Cdd:NF040873 149 GLDAESRERIIALLAEEHAR-GATVVVVTHDLELV-RRADPCVLL 191
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
16-225 |
2.15e-42 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 144.42 E-value: 2.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 16 GYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA----RRIGLLAQNAT 91
Cdd:COG1136 17 GEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELArlrrRHIGFVFQFFN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 92 TLGDITVQELVArgrYPHqpLFTRW-RKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
Cdd:COG1136 97 LLPELTALENVA---LPL--LLAGVsRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15829881 171 TTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQAcRYASHLIALREGKIVAQ 225
Cdd:COG1136 172 TGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELA-ARADRVIRLRDGRIVSD 225
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
26-260 |
2.81e-42 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 144.98 E-value: 2.81e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 26 LTVEIPDGHFTAIIGPNGCGKSTLlrtLSRL--MTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTLGDITVQELVA 103
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTL---LARMagLLPGQGEILLNGRPLSDWSAAELARHRAYLSQQQSPPFAMPVFQYLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 104 RgrypHQPlftrwRKEDEEAVTKAM----QATGITHLADQSVDTLSGGQRQRAWIAMVLAQ-------ETAIMLLDEPTT 172
Cdd:COG4138 92 L----HQP-----AGASSEAVEQLLaqlaEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 173 WLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYGLRCMIIDdpV 252
Cdd:COG4138 163 SLDVAQQAALDRLLREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVFGVKFRRLE--V 239
|
....*...
gi 15829881 253 AGTPLVVP 260
Cdd:COG4138 240 EGHRWLIP 247
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
7-231 |
6.87e-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: 143.09 E-value: 6.87e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 7 RLRGeqLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRL-----MTPAHGHVWLDGEHIQHYASK--EV 79
Cdd:cd03260 2 ELRD--LNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDvlEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 80 ARRIGLLAQNATTLgDITVQELVARGRYPHQplfTRWRKEDEEAVTKAMQATGITHLADQSVD--TLSGGQRQRAWIAMV 157
Cdd:cd03260 80 RRRVGMVFQKPNPF-PGSIYDNVAYGLRLHG---IKLKEELDERVEEALRKAALWDEVKDRLHalGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15829881 158 LAQETAIMLLDEPTTWLDISHQIDLLELLSELNREkgYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
8-233 |
3.55e-40 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 139.36 E-value: 3.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 8 LRGEQLTLGYGKYTVA-ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLL 86
Cdd:cd03295 1 IEFENVTKRYGGGKKAvNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 87 AQNATTLGDITVQELVARgryphQPLFTRWRKED-EEAVTKAMQATGI--THLADQSVDTLSGGQRQRAWIAMVLAQETA 163
Cdd:cd03295 81 IQQIGLFPHMTVEENIAL-----VPKLLKWPKEKiRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 164 IMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVT 233
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
19-251 |
4.91e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 139.74 E-value: 4.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 19 KYTVAE-----NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATT- 92
Cdd:PRK13632 16 SYPNSEnnalkNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIFQNPDNq 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 93 -LGdITVQELVARG----RYPhqplftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
Cdd:PRK13632 96 fIG-ATVEDDIAFGlenkKVP--------PKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 168 DEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRyASHLIALREGKIVAQGAPKEIVTAELIeriygLRCMI 247
Cdd:PRK13632 167 DESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILNNKEI-----LEKAK 240
|
....
gi 15829881 248 IDDP 251
Cdd:PRK13632 241 IDSP 244
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-243 |
1.12e-39 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 138.29 E-value: 1.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 3 ESVARLRGeqLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHG-HVWL-----DGEHIQhyas 76
Cdd:COG1119 1 DPLLELRN--VTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLfgerrGGEDVW---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 77 kEVARRIGLL--AQNATTLGDITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWI 154
Cdd:COG1119 75 -ELRKRIGLVspALQLRFPRDETVLDVVLSGFFDSIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 155 AMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTA 234
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLTS 233
|
....*....
gi 15829881 235 ELIERIYGL 243
Cdd:COG1119 234 ENLSEAFGL 242
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
11-221 |
6.80e-39 |
|
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: 133.14 E-value: 6.80e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQna 90
Cdd:cd00267 3 ENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 91 ttlgditvqelvargryphqplftrwrkedeeavtkamqatgithladqsvdtLSGGQRQRAWIAMVLAQETAIMLLDEP 170
Cdd:cd00267 81 -----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15829881 171 TTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGK 221
Cdd:cd00267 108 TSGLDPASRERLLELLREL-AEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
11-222 |
1.92e-38 |
|
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: 132.52 E-value: 1.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyASKEVARRIGLLAQNA 90
Cdd:cd03230 4 RNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLPEEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 91 TTLGDITVQELVargryphqplftrwrkedeeavtkamqatgithladqsvdTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
Cdd:cd03230 83 SLYENLTVRENL----------------------------------------KLSGGMKQRLALAQALLHDPELLILDEP 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15829881 171 TTWLDISHQIDLLELLSELNREKGytlaAVL---HDLNQACRYASHLIALREGKI 222
Cdd:cd03230 123 TSGLDPESRREFWELLRELKKEGK----TILlssHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
8-226 |
2.78e-38 |
|
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: 133.79 E-value: 2.78e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 8 LRGEQLTLGY----GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA--- 80
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 81 RRIGLLAQNATTLGD--ITVQELVARGRYPHQPLftrwRKEDEEAVTKAMQATGI---THLADQSVDTLSGGQRQRAWIA 155
Cdd:cd03257 82 KEIQMVFQDPMSSLNprMTIGEQIAEPLRIHGKL----SKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15829881 156 MVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG 226
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
8-240 |
4.53e-38 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 133.34 E-value: 4.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 8 LRGEQLTLGYGKYTVAENLTveIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLA 87
Cdd:COG3840 2 LRLDDLTYRYGDFPLRFDLT--IAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--RPVSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 88 QNATTLGDITVQELVARGRYPHqplfTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
Cdd:COG3840 78 QENNLFPHLTVAQNIGLGLRPG----LKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15829881 168 DEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERI 240
Cdd:COG3840 154 DEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPAL 226
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
24-172 |
6.98e-38 |
|
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: 130.46 E-value: 6.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTLGDITVQELVA 103
Cdd:pfam00005 2 KNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENLR 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15829881 104 RGRYphqpLFTRWRKEDEEAVTKAMQATGITHLADQSVD----TLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
Cdd:pfam00005 82 LGLL----LKGLSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
8-221 |
8.21e-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: 131.16 E-value: 8.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYA--SKEVARRIGL 85
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 86 LAQNATTLGDITVQELVARGryphqplftrwrkedeeavtkamqatgithladqsvdtLSGGQRQRAWIAMVLAQETAIM 165
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG--------------------------------------LSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15829881 166 LLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGK 221
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-231 |
8.35e-38 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 136.00 E-value: 8.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 1 MTESVARLRGeqLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyaskeVA 80
Cdd:COG3842 1 MAMPALELEN--VSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTG-----LP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 81 ---RRIGLLAQNATTLGDITVQELVA---RGRyphqplftRWRKED-EEAVTKAMQATGITHLADQSVDTLSGGQRQRAW 153
Cdd:COG3842 74 pekRNVGMVFQDYALFPHLTVAENVAfglRMR--------GVPKAEiRARVAELLELVGLEGLADRYPHQLSGGQQQRVA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15829881 154 IAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
Cdd:COG3842 146 LARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
6-231 |
1.38e-37 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 135.20 E-value: 1.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 6 ARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGL 85
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD--RNIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 86 LAQN-AttLgditvqelvargrYPHQ--------PLftRWRKED----EEAVTKAMQATGITHLADQSVDTLSGGQRQRA 152
Cdd:COG3839 80 VFQSyA--L-------------YPHMtvyeniafPL--KLRKVPkaeiDRRVREAAELLGLEDLLDRKPKQLSGGQRQRV 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15829881 153 WIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
Cdd:COG3839 143 ALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
8-226 |
1.49e-37 |
|
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: 131.46 E-value: 1.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 8 LRGEQLTLGYGkyTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGehiQHYASKEVARR-IGLL 86
Cdd:cd03298 1 VRLDKIRFSYG--EQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING---VDVTAAPPADRpVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 87 AQNATTLGDITVQELVARGRYPHqplfTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIML 166
Cdd:cd03298 76 FQENNLFAHLTVEQNVGLGLSPG----LKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 167 LDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG 226
Cdd:cd03298 152 LDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
33-244 |
2.60e-37 |
|
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: 131.51 E-value: 2.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 33 GHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEhiqhyASKEVARRIGLLAQNATTLGD--ITVQELVARGRYPHQ 110
Cdd:TIGR03771 6 GELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGA-----SPGKGWRHIGYVPQRHEFAWDfpISVAHTVMSGRTGHI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 111 PLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELN 190
Cdd:TIGR03771 81 GWLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFIELA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15829881 191 REkGYTLAAVLHDLNQACrYASHLIALREGKIVAQGAPKEIVTAELIERIYGLR 244
Cdd:TIGR03771 161 GA-GTAILMTTHDLAQAM-ATCDRVVLLNGRVIADGTPQQLQDPAPWMTTFGVS 212
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
11-231 |
3.86e-37 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 131.27 E-value: 3.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIqHYASKEVA---RRIGLLA 87
Cdd:COG1126 5 ENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDINklrRKVGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 88 QN------AT-----TLGDITVQelvargryphqplftRWRKedEEAVTKAMQA---TGITHLADQSVDTLSGGQRQRAW 153
Cdd:COG1126 84 QQfnlfphLTvlenvTLAPIKVK---------------KMSK--AEAEERAMELlerVGLADKADAYPAQLSGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 154 IAMVLAQETAIMLLDEPTTWLD---IShqiDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKE 230
Cdd:COG1126 147 IARALAMEPKVMLFDEPTSALDpelVG---EVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEE 222
|
.
gi 15829881 231 I 231
Cdd:COG1126 223 F 223
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
6-199 |
1.24e-36 |
|
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: 129.14 E-value: 1.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 6 ARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyASKEVARRIGL 85
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 86 LAQNATTLGDITVQELVArgryphqpLFTRWRKE--DEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETA 163
Cdd:COG4133 80 LGHADGLKPELTVRENLR--------FWAALYGLraDREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAP 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 15829881 164 IMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAA 199
Cdd:COG4133 152 LWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLT 187
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
11-225 |
4.60e-36 |
|
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: 127.97 E-value: 4.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 11 EQLTLGYG----KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQhyaskEVARRIGLL 86
Cdd:cd03293 4 RNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT-----GPGPDRGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 87 AQNATTLGDITVQELVARGryphqPLFTRW-RKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIM 165
Cdd:cd03293 79 FQQDALLPWLTVLDNVALG-----LELQGVpKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15829881 166 LLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIAL--REGKIVAQ 225
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAE 215
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
24-231 |
6.10e-36 |
|
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: 128.22 E-value: 6.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNATTLGDITVQELVA 103
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK--RDISYVPQNYALFPHMTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 104 RGryphQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLL 183
Cdd:cd03299 94 YG----LKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15829881 184 ELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
Cdd:cd03299 170 EELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEV 217
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
17-248 |
2.24e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 127.89 E-value: 2.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 17 YGKYTVA-ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQhYASK---EVARRIGLLAQNA-T 91
Cdd:PRK13639 11 YPDGTEAlKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKsllEVRKTVGIVFQNPdD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 92 TLGDITVQELVARGryphqPLFTRWRKED-EEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
Cdd:PRK13639 90 QLFAPTVEEDVAFG-----PLNLGLSKEEvEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15829881 171 TTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYGLRCMII 248
Cdd:PRK13639 165 TSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIRKANLRLPRV 241
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
32-226 |
7.02e-35 |
|
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: 124.71 E-value: 7.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 32 DGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGH------VWLDGEHIQHYASKEvaRRIGLLAQNATTLGDITVQELVARG 105
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTivlngtVLFDSRKKINLPPQQ--RKIGLVFQQYALFPHLNVRENLAFG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 106 ryphqpLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLEL 185
Cdd:cd03297 100 ------LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15829881 186 LSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG 226
Cdd:cd03297 174 LKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
25-233 |
7.72e-35 |
|
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: 126.22 E-value: 7.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEV----ARRIGLLAQNATTLGDITVQE 100
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLPHRTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 101 LVARG-RYPHQPlftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQ 179
Cdd:cd03294 122 NVAFGlEVQGVP-----RAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIR 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15829881 180 IDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVT 233
Cdd:cd03294 197 REMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-233 |
7.87e-35 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 125.92 E-value: 7.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 1 MTESVARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRL--MTP---AHGHVWLDGEHIqhYA 75
Cdd:COG1117 5 ASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPgarVEGEILLDGEDI--YD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 76 SK----EVARRIGLLAQNATTLgDITVQELVARG-RYpHQplfTRWRKEDEEAVTKAMQATGI-----THLaDQSVDTLS 145
Cdd:COG1117 83 PDvdvvELRRRVGMVFQKPNPF-PKSIYDNVAYGlRL-HG---IKSKSELDEIVEESLRKAALwdevkDRL-KKSALGLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 146 GGQRQRAWIAMVLAQETAIMLLDEPTTWLD-IS-HQIDllELLSELnREKgYTLAAVLHDLNQACRYASHLIALREGKIV 223
Cdd:COG1117 157 GGQQQRLCIARALAVEPEVLLMDEPTSALDpIStAKIE--ELILEL-KKD-YTIVIVTHNMQQAARVSDYTAFFYLGELV 232
|
250
....*....|
gi 15829881 224 AQGAPKEIVT 233
Cdd:COG1117 233 EFGPTEQIFT 242
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-231 |
1.95e-34 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 125.51 E-value: 1.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 1 MTESVARLrgEQLTLGY---GKYTVaENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASK 77
Cdd:PRK13635 1 MKEEIIRV--EHISFRYpdaATYAL-KDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 78 EVARRIGLLAQNATT--LGdITVQELVARGRYPHQ-PlftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWI 154
Cdd:PRK13635 78 DVRRQVGMVFQNPDNqfVG-ATVQDDVAFGLENIGvP-----REEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15829881 155 AMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRyASHLIALREGKIVAQGAPKEI 231
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEI 227
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
11-231 |
2.10e-34 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 126.80 E-value: 2.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGE------HIQHyaskevaRRIG 84
Cdd:COG1118 6 RNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRdlftnlPPRE-------RRVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 85 LLAQNATTLGDITVQELVARGrYPHQPLFtrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAI 164
Cdd:COG1118 79 FVFQHYALFPHMTVAENIAFG-LRVRPPS---KAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15829881 165 MLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
Cdd:COG1118 155 LLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
17-222 |
2.37e-34 |
|
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: 123.41 E-value: 2.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHI--QHYASKEVARRIGLLAQ------ 88
Cdd:cd03262 10 FGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGMVFQqfnlfp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 89 NATTLGDITVqelvargryphqPLFTRWRKEDEEAVTKAMQA---TGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIM 165
Cdd:cd03262 90 HLTVLENITL------------APIKVKGMSKAEAEERALELlekVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15829881 166 LLDEPTTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKI 222
Cdd:cd03262 158 LFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
16-231 |
2.88e-34 |
|
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: 123.46 E-value: 2.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 16 GYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEV---ARRIGLLAQNATT 92
Cdd:cd03258 14 TGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaRRRIGMIFQHFNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 93 LGDITVQELVArgrYPHQPLFTRwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
Cdd:cd03258 94 LSSRTVFENVA---LPLEIAGVP-KAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15829881 173 WLD--ISHQIdlLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
Cdd:cd03258 170 ALDpeTTQSI--LALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
8-231 |
3.04e-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: 123.50 E-value: 3.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLA 87
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK--RPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 88 QNATTLGDITVQELVARGryphqpLFTRWRKEDE--EAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIM 165
Cdd:cd03300 79 QNYALFPHLTVFENIAFG------LRLKKLPKAEikERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15829881 166 LLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
Cdd:cd03300 153 LLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
11-244 |
3.50e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 124.46 E-value: 3.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 11 EQLTLGYGKYTVA-ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQN 89
Cdd:PRK13647 8 EDLHFRYKDGTKAlKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 90 AT-TLGDITVQELVARGryphqPLFTRWRKED-EEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
Cdd:PRK13647 88 PDdQVFSSTVWDDVAFG-----PVNMGLDKDEvERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15829881 168 DEPTTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPkEIVTAELIERIYGLR 244
Cdd:PRK13647 163 DEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK-SLLTDEDIVEQAGLR 237
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
8-244 |
6.81e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 124.19 E-value: 6.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 8 LRGEQLTLGYGKYTVAEN-LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQhYASK---EVARRI 83
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKgININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID-YSRKglmKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 84 GLLAQNA-TTLGDITVQELVARGRYPHQ-PlftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQE 161
Cdd:PRK13636 85 GMVFQDPdNQLFSASVYQDVSFGAVNLKlP-----EDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVME 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 162 TAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIY 241
Cdd:PRK13636 160 PKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEMLRKV 239
|
...
gi 15829881 242 GLR 244
Cdd:PRK13636 240 NLR 242
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
28-231 |
7.54e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 123.98 E-value: 7.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 28 VEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYAS----KEVARRIGLLAQNA-TTLGDITVQELV 102
Cdd:PRK13634 28 VSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKnkklKPLRKKVGIVFQFPeHQLFEETVEKDI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 103 ARGryphqPL-FTRWRKEDEEAVTKAMQATGITH-LADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQI 180
Cdd:PRK13634 108 CFG-----PMnFGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRK 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15829881 181 DLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
Cdd:PRK13634 183 EMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-224 |
9.10e-34 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 122.89 E-value: 9.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 1 MTESVARLRGEQLTLGY----GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIqhyas 76
Cdd:COG1116 1 MSAAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 77 KEVARRIGLLAQNATTLGDITVQE-----LVARGRYphqplftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQR 151
Cdd:COG1116 76 TGPGPDRGVVFQEPALLPWLTVLDnvalgLELRGVP---------KAERRERARELLELVGLAGFEDAYPHQLSGGMRQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15829881 152 AWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIAL--REGKIVA 224
Cdd:COG1116 147 VAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLsaRPGRIVE 221
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
11-243 |
1.12e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 123.62 E-value: 1.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 11 EQLTLGYGKYTVAE-----NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHI--QHYASKEVARRI 83
Cdd:PRK13637 6 ENLTHIYMEGTPFEkkaldNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 84 GLLAQnattlgditvqelvargrYPHQPLF------------TRWRKEDEEA---VTKAMQATGITH--LADQSVDTLSG 146
Cdd:PRK13637 86 GLVFQ------------------YPEYQLFeetiekdiafgpINLGLSEEEIenrVKRAMNIVGLDYedYKDKSPFELSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 147 GQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG 226
Cdd:PRK13637 148 GQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQG 227
|
250
....*....|....*...
gi 15829881 227 APKEIVT-AELIERIyGL 243
Cdd:PRK13637 228 TPREVFKeVETLESI-GL 244
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
11-223 |
1.65e-33 |
|
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: 121.21 E-value: 1.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNA 90
Cdd:cd03301 4 ENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMVFQNY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 91 TTLGDITVQELVARG-RYPHQPlftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
Cdd:cd03301 82 ALYPHMTVYDNIAFGlKLRKVP-----KDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15829881 170 PTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIV 223
Cdd:cd03301 157 PLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
6-232 |
1.76e-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: 127.57 E-value: 1.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 6 ARLRGEQLTLGY--GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRI 83
Cdd:COG4987 332 PSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 84 GLLAQNA----TTLGD-ItvqeLVARGRyphqplftrwrkEDEEAVTKAMQATGITHLADQSVD-----------TLSGG 147
Cdd:COG4987 412 AVVPQRPhlfdTTLREnL----RLARPD------------ATDEELWAALERVGLGDWLAALPDgldtwlgeggrRLSGG 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 148 QRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKgyTLAAVLHDLnQACRYASHLIALREGKIVAQGA 227
Cdd:COG4987 476 ERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRL-AGLERMDRILVLEDGRIVEQGT 552
|
....*
gi 15829881 228 PKEIV 232
Cdd:COG4987 553 HEELL 557
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
17-231 |
2.48e-33 |
|
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: 121.29 E-value: 2.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNATTLGDI 96
Cdd:cd03296 12 FGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFVFQHYALFRHM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 97 TVQELVARGrYPHQPLFTRWRK-EDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
Cdd:cd03296 90 TVFDNVAFG-LRVKPRSERPPEaEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15829881 176 ISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
Cdd:cd03296 169 AKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
8-231 |
4.12e-33 |
|
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: 120.23 E-value: 4.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARR-IGLL 86
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 87 AQNATTLGDITVQELVARGRYPHQPLFTRWRKEDEEA---VTKAMQatgithlaDQSVDTLSGGQRQRAWIAMVLAQETA 163
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYElfpRLKERR--------KQLAGTLSGGEQQMLAIARALMSRPK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 164 IMLLDEPTTWL--DISHQIdlLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
Cdd:cd03224 153 LLLLDEPSEGLapKIVEEI--FEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
8-230 |
2.85e-32 |
|
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: 124.10 E-value: 2.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 8 LRGEQLTLGY-GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLL 86
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 87 AQNATTLGDiTVQELVARGRyphqplftrwRKEDEEAVTKAMQATGITHLADQS---VDT--------LSGGQRQRAWIA 155
Cdd:COG4988 417 PQNPYLFAG-TIRENLRLGR----------PDASDEELEAALEAAGLDEFVAALpdgLDTplgeggrgLSGGQAQRLALA 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15829881 156 MVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKgyTLAAVLHDLNQAcRYASHLIALREGKIVAQGAPKE 230
Cdd:COG4988 486 RALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALL-AQADRILVLDDGRIVEQGTHEE 557
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
11-230 |
3.49e-32 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 117.85 E-value: 3.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 11 EQLTLGYGKYTVA-ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA---RRIGLL 86
Cdd:COG2884 5 ENVSKRYPGGREAlSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPylrRRIGVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 87 AQNATTLGDITVQE-----LVARGRYphqplftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQE 161
Cdd:COG2884 85 FQDFRLLPDRTVYEnvalpLRVTGKS---------RKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15829881 162 TAIMLLDEPTTWLDISHQIDLLELLSELNREKgytlAAVL---HDLNQACRYASHLIALREGKIVAQGAPKE 230
Cdd:COG2884 156 PELLLADEPTGNLDPETSWEIMELLEEINRRG----TTVLiatHDLELVDRMPKRVLELEDGRLVRDEARGV 223
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
25-231 |
3.61e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 119.09 E-value: 3.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATT--LGDItVQELV 102
Cdd:PRK13648 27 DVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQNPDNqfVGSI-VKYDV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 103 ARG----RYPHqplftrwrKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISH 178
Cdd:PRK13648 106 AFGlenhAVPY--------DEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15829881 179 QIDLLELLSELNREKGYTLAAVLHDLNQACRyASHLIALREGKIVAQGAPKEI 231
Cdd:PRK13648 178 RQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEI 229
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-239 |
5.61e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 118.09 E-value: 5.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 6 ARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLM-----TPAHGHVWLDGEHIQHYASKEVA 80
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIFKMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 81 RRIGLLAQNATTLGDITVQELVARGryPHQPLFTRWRKEDEEAVTKAMQATG----ITHLADQSVDTLSGGQRQRAWIAM 156
Cdd:PRK14247 82 RRVQMVFQIPNPIPNLSIFENVALG--LKLNRLVKSKKELQERVRWALEKAQlwdeVKDRLDAPAGKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 157 VLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREkgYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTA-- 234
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNpr 237
|
....*.
gi 15829881 235 -ELIER 239
Cdd:PRK14247 238 hELTEK 243
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
25-226 |
1.41e-31 |
|
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: 116.11 E-value: 1.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 25 NLTVEipDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEhiQHYASKEVARRIGLLAQNATTLGDITVQELVAR 104
Cdd:TIGR01277 18 DLNVA--DGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQ--SHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 105 GRYPHQPLftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLE 184
Cdd:TIGR01277 94 GLHPGLKL----NAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15829881 185 LLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG 226
Cdd:TIGR01277 170 LVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
8-230 |
1.86e-31 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 117.04 E-value: 1.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMT---PAHGHVWLDGEHIQHyaSKEVARRI- 83
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdkSAGSHIELLGRTVQR--EGRLARDIr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 84 ------GLLAQNATTLGDITVQELVARGRYPHQPLFT---RW--RKEDEEAVtKAMQATGITHLADQSVDTLSGGQRQRA 152
Cdd:PRK09984 83 ksrantGYIFQQFNLVNRLSVLENVLIGALGSTPFWRtcfSWftREQKQRAL-QALTRVGMVHFAHQRVSTLSGGQQQRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15829881 153 WIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKE 230
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
11-231 |
2.31e-31 |
|
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: 115.54 E-value: 2.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyASKEVARRIGLLAQNA 90
Cdd:cd03265 4 ENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 91 TTLGDITVQELVargrYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
Cdd:cd03265 83 SVDDELTGWENL----YIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15829881 171 TTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
Cdd:cd03265 159 TIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
11-235 |
2.36e-31 |
|
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: 122.25 E-value: 2.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 11 EQLTLGYGKYTVA--ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQ 88
Cdd:COG2274 477 ENVSFRYPGDSPPvlDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQ 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 89 NATTLGDiTVQELVARGRyPHQplftrwrkeDEEAVTKAMQATGI------------THLADQSVdTLSGGQRQRAWIAM 156
Cdd:COG2274 557 DVFLFSG-TIRENITLGD-PDA---------TDEEIIEAARLAGLhdfiealpmgydTVVGEGGS-NLSGGQRQRLAIAR 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15829881 157 VLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKgyTLAAVLHDLNQAcRYASHLIALREGKIVAQGAPKEIVTAE 235
Cdd:COG2274 625 ALLRNPRILILDEATSALDAETEAIILENLRRLLKGR--TVIIIAHRLSTI-RLADRIIVLDKGRIVEDGTHEELLARK 700
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
11-241 |
3.55e-31 |
|
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: 115.46 E-value: 3.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARR-IGLLAQN 89
Cdd:COG0410 7 ENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgIGYVPEG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 90 ATTLGDITVQE---LVARGRYPHQPLftRWRKEDeeavtkamqatgITHL-------ADQSVDTLSGGQRQRAWIAMVLA 159
Cdd:COG0410 87 RRIFPSLTVEEnllLGAYARRDRAEV--RADLER------------VYELfprlkerRRQRAGTLSGGEQQMLAIGRALM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 160 QETAIMLLDEPTtwLDISHQI--DLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELI 237
Cdd:COG0410 153 SRPKLLLLDEPS--LGLAPLIveEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEV 229
|
....
gi 15829881 238 ERIY 241
Cdd:COG0410 230 REAY 233
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
11-226 |
1.06e-30 |
|
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: 113.83 E-value: 1.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 11 EQLTLGYGKYTVAENLTVEIPDGhFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKeVARRIGLLAQNA 90
Cdd:cd03264 4 ENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-LRRRIGYLPQEF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 91 TTLGDITVQELVArgrypHQPLFTRWR-KEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
Cdd:cd03264 82 GVYPNFTVREFLD-----YIAWLKGIPsKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15829881 170 PTTWLDISHQIDLLELLSELNREKGYTLAAvlHDLNQACRYASHLIALREGKIVAQG 226
Cdd:cd03264 157 PTAGLDPEERIRFRNLLSELGEDRIVILST--HIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
8-241 |
1.07e-30 |
|
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: 114.18 E-value: 1.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARR-IGLL 86
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 87 AQNATTLGDITVQE---LVARGRYphqplFTRWRKEDE-EAVTKAMQatgITHLADQSVDTLSGGQRQRAWIAMVLAQET 162
Cdd:cd03218 81 PQEASIFRKLTVEEnilAVLEIRG-----LSKKEREEKlEELLEEFH---ITHLRKSKASSLSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 163 AIMLLDEPTTWLD-ISHQiDLLELLSELnREKGYtlaAVL---HDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIE 238
Cdd:cd03218 153 KFLLLDEPFAGVDpIAVQ-DIQKIIKIL-KDRGI---GVLitdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVR 227
|
...
gi 15829881 239 RIY 241
Cdd:cd03218 228 KVY 230
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-250 |
1.07e-30 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 114.64 E-value: 1.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLmTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTLGDITVQELVARg 105
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFAMPVFQYLTL- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 106 rypHQPLFTRWRkEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQ-------ETAIMLLDEPTTWLDISH 178
Cdd:PRK03695 93 ---HQPDKTRTE-AVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDVAQ 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15829881 179 QIDLLELLSELNREKGytlaAVL---HDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYGL--RCMIIDD 250
Cdd:PRK03695 169 QAALDRLLSELCQQGI----AVVmssHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVFGVnfRRLDVEG 241
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
9-223 |
3.43e-30 |
|
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: 112.35 E-value: 3.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 9 RGEQLTLGYGK-YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIqhyASKEVARRIGLLA 87
Cdd:cd03226 1 RIENISFSYKKgTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 88 QNATT-LGDITVQELVARG--RYPhqplftrwrkEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAI 164
Cdd:cd03226 78 QDVDYqLFTDSVREELLLGlkELD----------AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15829881 165 MLLDEPTTWLDISHqidlLELLSELNRE---KGYTLAAVLHDLNQACRYASHLIALREGKIV 223
Cdd:cd03226 148 LIFDEPTSGLDYKN----MERVGELIRElaaQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
24-254 |
3.77e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 114.16 E-value: 3.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYAS----KEVARRIGLLAQ-NATTLGDITV 98
Cdd:PRK13641 24 DNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGnknlKKLRKKVSLVFQfPEAQLFENTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 99 QELVARGryphqPL-FTRWRKEDEEAVTKAMQATGI-THLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
Cdd:PRK13641 104 LKDVEFG-----PKnFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15829881 177 SHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVT-AELIERIYglrcmiIDDPVAG 254
Cdd:PRK13641 179 EGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSdKEWLKKHY------LDEPATS 250
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
19-240 |
7.93e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 113.36 E-value: 7.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTP---AHGHVWLDGEHIQHYASKEVARRIGLLAQN------ 89
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIREKVGIVFQNpdnqfv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 90 ATTLGDITVQELVARGrYPhqplftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
Cdd:PRK13640 99 GATVGDDVAFGLENRA-VP--------RPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDE 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15829881 170 PTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQAcRYASHLIALREGKIVAQGAPKEIVT-AELIERI 240
Cdd:PRK13640 170 STSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSkVEMLKEI 240
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
8-211 |
2.26e-29 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 111.80 E-value: 2.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRL--MTP---AHGHVWLDGEHIqhYASK----E 78
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPgfrVEGKVTFHGKNL--YAPDvdpvE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 79 VARRIGLLAQNATTLGDiTVQELVARGryphqPLFTRWRKEDEEAVTKAM-QATGITHLAD---QSVDTLSGGQRQRAWI 154
Cdd:PRK14243 89 VRRRIGMVFQKPNPFPK-SIYDNIAYG-----ARINGYKGDMDELVERSLrQAALWDEVKDklkQSGLSLSGGQQQRLCI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15829881 155 AMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREkgYTLAAVLHDLNQACRYA 211
Cdd:PRK14243 163 ARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVS 217
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
19-224 |
2.98e-29 |
|
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: 110.13 E-value: 2.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA----RRIGLLAQNATTLG 94
Cdd:TIGR02211 17 DTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAklrnKKLGFIYQFHHLLP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 95 DITVQELVArgryphQPLFTRW--RKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
Cdd:TIGR02211 97 DFTALENVA------MPLLIGKksVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTG 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15829881 173 WLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRyASHLIALREGKIVA 224
Cdd:TIGR02211 171 NLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKK-LDRVLEMKDGQLFN 221
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
17-240 |
4.75e-29 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 110.18 E-value: 4.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKE--VARRIGLLAQNATTLG 94
Cdd:PRK09493 11 FGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlIRQEAGMVFQQFYLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 95 DITVQELVARGryphqPLFTR-WRKEDEEAVTKAMQA-TGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
Cdd:PRK09493 91 HLTALENVMFG-----PLRVRgASKEEAEKQARELLAkVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15829881 173 WLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERI 240
Cdd:PRK09493 166 ALDPELRHEVLKVMQDL-AEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRL 232
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
27-235 |
5.43e-29 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 109.67 E-value: 5.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 27 TVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEhiQHYASKEVARRIGLLAQNATTLGDITVQELVARGR 106
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ--DHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 107 YPHQPLfTRWRKEDEEAVTKAMqatGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELL 186
Cdd:PRK10771 97 NPGLKL-NAAQREKLHAIARQM---GIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15829881 187 SELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAE 235
Cdd:PRK10771 173 SQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGK 221
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
25-231 |
5.64e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 110.99 E-value: 5.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYAS----KEVARRIGLLAQNA-TTLGDITVQ 99
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdiKQIRKKVGLVFQFPeSQLFEETVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 100 ELVARGryPHQplFTRWRKEDEEAVTKAMQATGITH-LADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISH 178
Cdd:PRK13649 105 KDVAFG--PQN--FGVSQEEAEALAREKLALVGISEsLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15829881 179 QIDLLELLSELNrEKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
Cdd:PRK13649 181 RKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
17-231 |
8.82e-29 |
|
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: 112.13 E-value: 8.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 17 YGKYTVAENLTveIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyASKEV-----ARRIGLLAQNAT 91
Cdd:TIGR02142 9 LGDFSLDADFT--LPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFD-SRKGIflppeKRRIGYVFQEAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 92 TLGDITVQELVARGRYPHQPLFTRWRkedEEAVTKAMqatGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
Cdd:TIGR02142 86 LFPHLSVRGNLRYGMKRARPSERRIS---FERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 172 TWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
Cdd:TIGR02142 160 AALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
12-231 |
1.04e-28 |
|
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: 111.73 E-value: 1.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 12 QLTLGYGKYTVAENLTveIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyASKEV-----ARRIGLL 86
Cdd:COG4148 6 DFRLRRGGFTLDVDFT--LPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQD-SARGIflpphRRRIGYV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 87 AQNATTLGDITVQELVargRYPHQPLFTRWRKEDEEAVTKAMqatGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIML 166
Cdd:COG4148 83 FQEARLFPHLSVRGNL---LYGRKRAPRAERRISFDEVVELL---GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15829881 167 LDEPTTWLDISHQIDLLELLSELNREKG----YtlaaVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
Cdd:COG4148 157 MDEPLAALDLARKAEILPYLERLRDELDipilY----VSHSLDEVARLADHVVLLEQGRVVASGPLAEV 221
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-231 |
2.40e-28 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 111.19 E-value: 2.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 1 MTESVARLRGeqLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKevA 80
Cdd:PRK09452 10 SLSPLVELRG--ISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--N 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 81 RRIGLLAQNATTLGDITVQELVARG----RYPHQplftrwrkEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAM 156
Cdd:PRK09452 86 RHVNTVFQSYALFPHMTVFENVAFGlrmqKTPAA--------EITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15829881 157 VLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
Cdd:PRK09452 158 AVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 232
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
22-221 |
7.05e-28 |
|
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: 105.16 E-value: 7.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTLGDiTVQEL 101
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAYVPQDPFLFSG-TIREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 102 VargryphqplftrwrkedeeavtkamqatgithladqsvdtLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQID 181
Cdd:cd03228 96 I-----------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEAL 134
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15829881 182 LLELLSELNREKgyTLAAVLHDLNQAcRYASHLIALREGK 221
Cdd:cd03228 135 ILEALRALAKGK--TVIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-239 |
7.49e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 107.24 E-value: 7.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLM-----TPAHGHVWLDGEHIqhYASK----EVAR 81
Cdd:PRK14267 8 VNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRNI--YSPDvdpiEVRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 82 RIGLLAQNATTLGDITVQELVARGRYPHQplFTRWRKEDEEAVTKAMQATGI-THLADQSVD---TLSGGQRQRAWIAMV 157
Cdd:PRK14267 86 EVGMVFQYPNPFPHLTIYDNVAIGVKLNG--LVKSKKELDERVEWALKKAALwDEVKDRLNDypsNLSGGQRQRLVIARA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 158 LAQETAIMLLDEPTTWLDISHQIDLLELLSELNREkgYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV---TA 234
Cdd:PRK14267 164 LAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFenpEH 241
|
....*
gi 15829881 235 ELIER 239
Cdd:PRK14267 242 ELTEK 246
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
37-235 |
8.62e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 107.97 E-value: 8.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 37 AIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNAT-TLGDITVQELVARGryphqPLFTR 115
Cdd:PRK13652 34 AVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPDdQIFSPTVEQDIAFG-----PINLG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 116 WrkeDEEA----VTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNR 191
Cdd:PRK13652 109 L---DEETvahrVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPE 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15829881 192 EKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAE 235
Cdd:PRK13652 186 TYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
25-226 |
9.48e-28 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 106.65 E-value: 9.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEhIQHYASKEVARRIGL-LAQNATTLGDITVQELVA 103
Cdd:cd03267 39 GISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL-VPWKRRKKFLRRIGVvFGQKTQLWWDLPVIDSFY 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 104 RGRYPHQPLFTRWRKEDEEaVTKAMQatgITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLL 183
Cdd:cd03267 118 LLAAIYDLPPARFKKRLDE-LSELLD---LEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIR 193
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15829881 184 ELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG 226
Cdd:cd03267 194 NFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
17-231 |
1.40e-27 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 108.63 E-value: 1.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNATTLGDI 96
Cdd:PRK10851 12 FGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVFQHYALFRHM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 97 TVQELVARGryphQPLFTRWRKEDEEA----VTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
Cdd:PRK10851 90 TVFDNIAFG----LTVLPRRERPNAAAikakVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15829881 173 WLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
Cdd:PRK10851 166 ALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
16-231 |
1.47e-27 |
|
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: 105.66 E-value: 1.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 16 GYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGeHIQHYASKEVARRIGLLAQNATTLGD 95
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYING-YSIRTDRKAARQSLGYCPQFDALFDE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 96 ITVQELVArgryphqpLFTRWR----KEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
Cdd:cd03263 90 LTVREHLR--------FYARLKglpkSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPT 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15829881 172 TWLDISHQIDLLELLSELNREKgytlAAVL--HDLNQACRYASHLIALREGKIVAQGAPKEI 231
Cdd:cd03263 162 SGLDPASRRAIWDLILEVRKGR----SIILttHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-222 |
1.70e-27 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 106.69 E-value: 1.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 2 TESVARL-RGEQLTLG-----YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwLDGEHIQHYA 75
Cdd:PRK11247 1 MMNTARLnQGTPLLLNavskrYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPLAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 76 SKEvarrIGLLAQNATTLGDITVQELVARGryphqpLFTRWRKEDEEAvtkaMQATGITHLADQSVDTLSGGQRQRAWIA 155
Cdd:PRK11247 80 RED----TRLMFQDARLLPWKKVIDNVGLG------LKGQWRDAALQA----LAAVGLADRANEWPAALSGGQKQRVALA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15829881 156 MVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKI 222
Cdd:PRK11247 146 RALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
13-231 |
1.73e-27 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 108.65 E-value: 1.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 13 LTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNATT 92
Cdd:PRK11432 12 ITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ--RDICMVFQSYAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 93 LGDITVQELVARGryphQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
Cdd:PRK11432 90 FPHMSLGENVGYG----LKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15829881 173 WLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
Cdd:PRK11432 166 NLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-231 |
1.90e-27 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 106.23 E-value: 1.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 1 MTESVARLRGeqLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA 80
Cdd:PRK11300 1 MSQPLLSVSG--LMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 81 RRiGLLA--QNATTLGDITVQE--LVARGRYPHQPLFT------RWRKEDEEAVTKA---MQATGITHLADQSVDTLSGG 147
Cdd:PRK11300 79 RM-GVVRtfQHVRLFREMTVIEnlLVAQHQQLKTGLFSgllktpAFRRAESEALDRAatwLERVGLLEHANRQAGNLAYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 148 QRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGA 227
Cdd:PRK11300 158 QQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGT 237
|
....
gi 15829881 228 PKEI 231
Cdd:PRK11300 238 PEEI 241
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
18-243 |
1.93e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 107.10 E-value: 1.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 18 GKYTVA-ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDG------EHIQhyaskEVARRIGLLAQN- 89
Cdd:PRK13633 20 STEKLAlDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtsdeENLW-----DIRNKAGMVFQNp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 90 -----ATTlgditVQELVARGryPH----QPlftrwrKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQ 160
Cdd:PRK13633 95 dnqivATI-----VEEDVAFG--PEnlgiPP------EEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 161 ETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRyASHLIALREGKIVAQGAPKEIVT-AELIER 239
Cdd:PRK13633 162 RPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKeVEMMKK 240
|
....
gi 15829881 240 IyGL 243
Cdd:PRK13633 241 I-GL 243
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
22-207 |
1.94e-27 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 104.43 E-value: 1.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYAS--KEVARRIGLLAQNA-TTLGDITV 98
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKglLERRQRVGLVFQDPdDQLFAADV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 99 QELVARGryphqPLfTRWRKEDE--EAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
Cdd:TIGR01166 87 DQDVAFG-----PL-NLGLSEAEveRRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDP 160
|
170 180 190
....*....|....*....|....*....|.
gi 15829881 177 SHQIDLLELLSELnREKGYTLAAVLHDLNQA 207
Cdd:TIGR01166 161 AGREQMLAILRRL-RAEGMTVVISTHDVDLA 190
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
11-222 |
2.15e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 110.15 E-value: 2.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHiqhyaskevarRIGLLAQNA 90
Cdd:COG0488 2 ENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL-----------RIGYLPQEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 91 TTLGDITVQELVARGrypHQPLFtRWRKEDEEAVTK--------------------------------AMQATGITH-LA 137
Cdd:COG0488 71 PLDDDLTVLDTVLDG---DAELR-ALEAELEELEAKlaepdedlerlaelqeefealggweaearaeeILSGLGFPEeDL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 138 DQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIsHQIDLLEllSELNREKGyTLAAVLHD---LNQACryaSHL 214
Cdd:COG0488 147 DRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL-ESIEWLE--EFLKNYPG-TVLVVSHDryfLDRVA---TRI 219
|
....*...
gi 15829881 215 IALREGKI 222
Cdd:COG0488 220 LELDRGKL 227
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-261 |
2.41e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 107.20 E-value: 2.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 4 SVARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYAsKEVARRI 83
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA-RHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 84 GLLAQNATTLGDITVQE-LVARGRYphqplFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQET 162
Cdd:PRK13537 83 GVVPQFDNLDPDFTVREnLLVFGRY-----FGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 163 AIMLLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAEL---IER 239
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLRSL-LARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEIgcdVIE 236
|
250 260
....*....|....*....|..
gi 15829881 240 IYGlrcmiiDDPVAGTPLVVPL 261
Cdd:PRK13537 237 IYG------PDPVALRDELAPL 252
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
7-236 |
3.59e-27 |
|
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: 110.34 E-value: 3.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 7 RLRG----EQLTLGY-GKYTVA-ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA 80
Cdd:TIGR03375 459 RLQGeiefRNVSFAYpGQETPAlDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLR 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 81 RRIGLLAQNATTL-GdiTVQELVARGRyphqPLFtrwrkeDEEAVTKAMQATGITHLADQSVD-----------TLSGGQ 148
Cdd:TIGR03375 539 RNIGYVPQDPRLFyG--TLRDNIALGA----PYA------DDEEILRAAELAGVTEFVRRHPDgldmqigergrSLSGGQ 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 149 RQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKgyTLAAVLHDLnQACRYASHLIALREGKIVAQGaP 228
Cdd:TIGR03375 607 RQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGK--TLVLVTHRT-SLLDLVDRIIVMDNGRIVADG-P 682
|
....*...
gi 15829881 229 KEIVTAEL 236
Cdd:TIGR03375 683 KDQVLEAL 690
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
38-231 |
4.80e-27 |
|
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: 106.81 E-value: 4.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 38 IIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNATTLGDITVQELVARGryphqplfTRWR 117
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHL--RHINMVFQSYALFPHMTVEENVAFG--------LKMR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 118 KEDEEAVT-KAMQATGITHL---ADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQiDLLEL-LSELNRE 192
Cdd:TIGR01187 71 KVPRAEIKpRVLEALRLVQLeefADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLR-DQMQLeLKTIQEQ 149
|
170 180 190
....*....|....*....|....*....|....*....
gi 15829881 193 KGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
Cdd:TIGR01187 150 LGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
6-241 |
5.39e-27 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 104.73 E-value: 5.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 6 ARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARR-IG 84
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLgIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 85 LLAQNATTLGDITVQE---LVARGRYPHqplftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQE 161
Cdd:COG1137 82 YLPQEASIFRKLTVEDnilAVLELRKLS-------KKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 162 TAIMLLDEPTTWLD-IShQIDLLELLSELnREKGY-----------TL-----AAVLHdlnqacryashlialrEGKIVA 224
Cdd:COG1137 155 PKFILLDEPFAGVDpIA-VADIQKIIRHL-KERGIgvlitdhnvreTLgicdrAYIIS----------------EGKVLA 216
|
250
....*....|....*..
gi 15829881 225 QGAPKEIVTAELIERIY 241
Cdd:COG1137 217 EGTPEEILNNPLVRKVY 233
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-228 |
8.70e-27 |
|
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: 104.05 E-value: 8.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 1 MTESVARLRGEQLTL--GYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKE 78
Cdd:COG4181 4 SSAPIIELRGLTKTVgtGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 79 VAR----RIGLLAQNATTLGDITVQELVArgryphQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWI 154
Cdd:COG4181 84 RARlrarHVGFVFQSFQLLPTLTALENVM------LPLELAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15829881 155 AMVLAQETAIMLLDEPTTWLD--ISHQIdlLELLSELNREKGYTLAAVLHDLNQACRyASHLIALREGKIVAQGAP 228
Cdd:COG4181 158 ARAFATEPAILFADEPTGNLDaaTGEQI--IDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTAA 230
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
22-225 |
9.72e-27 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 104.13 E-value: 9.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA----RRIGLLAQNATTLGDIT 97
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAelrnQKLGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 98 VQELVArgryphQPLFT--RWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
Cdd:PRK11629 104 ALENVA------MPLLIgkKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15829881 176 ISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLiALREGKIVAQ 225
Cdd:PRK11629 178 ARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL-EMRDGRLTAE 226
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-239 |
2.00e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 103.59 E-value: 2.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIqhYASKEVAR--------RIGLLAQNATTL 93
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVL--YFGKDIFQidaiklrkEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 94 GDITVQELVArgrYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDT----LSGGQRQRAWIAMVLAQETAIMLLDE 169
Cdd:PRK14246 103 PHLSIYDNIA---YPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSpasqLSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15829881 170 PTTWLDISHQIDLLELLSELNREkgYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTA---ELIER 239
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSpknELTEK 250
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
11-222 |
2.87e-26 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 102.10 E-value: 2.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 11 EQLTLGYGKYTVA-ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA---RRIGLL 86
Cdd:cd03292 4 INVTKTYPNGTAAlDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPylrRKIGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 87 AQNATTLGDITVQELVARG-RYPHQPlftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIM 165
Cdd:cd03292 84 FQDFRLLPDRNVYENVAFAlEVTGVP-----PREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15829881 166 LLDEPTTWLDISHQIDLLELLSELNReKGYTLAAVLHDLNQACRYASHLIALREGKI 222
Cdd:cd03292 159 IADEPTGNLDPDTTWEIMNLLKKINK-AGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
5-204 |
3.15e-26 |
|
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: 107.06 E-value: 3.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 5 VARLRGEQLTLGY-GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRI 83
Cdd:TIGR02868 332 KPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRV 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 84 GLLAQNAtTLGDITVQE--LVARGryphqplftrwrKEDEEAVTKAMQATGITHLADQSVD-----------TLSGGQRQ 150
Cdd:TIGR02868 412 SVCAQDA-HLFDTTVREnlRLARP------------DATDEELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQ 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15829881 151 RAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLseLNREKGYTLAAVLHDL 204
Cdd:TIGR02868 479 RLALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
24-226 |
3.87e-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: 101.90 E-value: 3.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNaTTLGDITVQELVA 103
Cdd:cd03245 21 DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQD-VTLFYGTLRDNIT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 104 RGRYPHqplftrwrkeDEEAVTKAMQATGITHLADQSVD-----------TLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
Cdd:cd03245 100 LGAPLA----------DDERILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARALLNDPPILLLDEPTS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15829881 173 WLDISHQIDLLELLSELNREKgyTLAAVLHDLNqACRYASHLIALREGKIVAQG 226
Cdd:cd03245 170 AMDMNSEERLKERLRQLLGDK--TLIIITHRPS-LLDLVDRIIVMDSGRIVADG 220
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
2-231 |
7.98e-26 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 102.54 E-value: 7.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 2 TESVARLRGeqLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASK---E 78
Cdd:PRK11831 4 VANLVDMRG--VSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSrlyT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 79 VARRIGLLAQNATTLGDITVQELVA-----RGRYPHQPLFTrwrkedeeAVTKAMQATGITHLADQSVDTLSGGQRQRAW 153
Cdd:PRK11831 82 VRKRMSMLFQSGALFTDMNVFDNVAyplreHTQLPAPLLHS--------TVMMKLEAVGLRGAAKLMPSELSGGMARRAA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15829881 154 IAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
Cdd:PRK11831 154 LARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
24-226 |
8.49e-26 |
|
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: 100.91 E-value: 8.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyASKEVARRIGLLAQNATTLGDITVQELVA 103
Cdd:cd03266 22 DGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYDRLTARENLE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 104 R-GRyphqpLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDL 182
Cdd:cd03266 101 YfAG-----LYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRAL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15829881 183 LELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG 226
Cdd:cd03266 176 REFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
11-226 |
9.63e-26 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 100.82 E-value: 9.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyaskEVARRIGLLAQNA 90
Cdd:cd03269 4 ENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI----AARNRIGYLPEER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 91 TTLGDITVQE-LVARGRyphqpLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
Cdd:cd03269 80 GLYPKMKVIDqLVYLAQ-----LKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15829881 170 PTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG 226
Cdd:cd03269 155 PFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
8-231 |
1.03e-25 |
|
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: 103.21 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 8 LRGEQLTLGY----GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTP---AHGHVWLDGEHIQHYASKEV- 79
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 80 ---ARRIGLLAQNAT-------TLGDITVQELVARGRYPhqplftrwRKEDEEAVTKAMQATGITHlADQSVD----TLS 145
Cdd:COG0444 82 kirGREIQMIFQDPMtslnpvmTVGDQIAEPLRIHGGLS--------KAEARERAIELLERVGLPD-PERRLDryphELS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 146 GGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGytLAAVL--HDLNQAcRYASHLIA---LreG 220
Cdd:COG0444 153 GGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELG--LAILFitHDLGVV-AEIADRVAvmyA--G 227
|
250
....*....|.
gi 15829881 221 KIVAQGAPKEI 231
Cdd:COG0444 228 RIVEEGPVEEL 238
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
25-230 |
1.36e-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: 101.08 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNAtTLGDITVQELVAR 104
Cdd:cd03249 21 GLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEP-VLFDGTIAENIRY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 105 GRYPhqplftRWRKEDEEAVTKAMQATGITHLADQsVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
Cdd:cd03249 100 GKPD------ATDEEVEEAAKKANIHDFIMSLPDG-YDTlvgergsqLSGGQKQRIAIARALLRNPKILLLDEATSALDA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15829881 177 SHQIDLLELLSELnrEKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKE 230
Cdd:cd03249 173 ESEKLVQEALDRA--MKGRTTIVIAHRLS-TIRNADLIAVLQNGQVVEQGTHDE 223
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
11-241 |
1.53e-25 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 101.88 E-value: 1.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 11 EQLTLGY-GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVarrIGLLAQN 89
Cdd:PRK15056 10 NDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 90 ATTLGD--ITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
Cdd:PRK15056 87 EEVDWSfpVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15829881 168 DEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALReGKIVAQGAPKEIVTAELIERIY 241
Cdd:PRK15056 167 DEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDYTVMVK-GTVLASGPTETTFTAENLELAF 238
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
8-226 |
1.61e-25 |
|
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: 99.98 E-value: 1.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyaSKEVARRIGLLA 87
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK--NIEALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 88 QNATTLGDITVQE-LVARGRYPHQPlftrwrkedEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIML 166
Cdd:cd03268 79 EAPGFYPNLTAREnLRLLARLLGIR---------KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 167 LDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG 226
Cdd:cd03268 150 LDEPTNGLDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
11-235 |
2.14e-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: 100.38 E-value: 2.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 11 EQLTLGYGKYT--VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQ 88
Cdd:cd03251 4 KNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVSQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 89 NaTTLGDITVQELVARGRyphqplftrwRKEDEEAVTKAMQATG----ITHLADQsVDT--------LSGGQRQRAWIAM 156
Cdd:cd03251 84 D-VFLFNDTVAENIAYGR----------PGATREEVEEAARAANahefIMELPEG-YDTvigergvkLSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15829881 157 VLAQETAIMLLDEPTTWLDISHQIDLLELLSELnrEKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIVTAE 235
Cdd:cd03251 152 ALLKDPPILILDEATSALDTESERLVQAALERL--MKNRTTFVIAHRLS-TIENADRIVVLEDGKIVERGTHEELLAQG 227
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
11-232 |
3.53e-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: 3.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 11 EQLTLGYG-KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQN 89
Cdd:cd03253 4 ENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 90 aTTLGDITVQELVARGRyphqPLFTrwRKEDEEAVTKAMQATGITHLADQsVDT--------LSGGQRQRAWIAMVLAQE 161
Cdd:cd03253 84 -TVLFNDTIGYNIRYGR----PDAT--DEEVIEAAKAAQIHDKIMRFPDG-YDTivgerglkLSGGEKQRVAIARAILKN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15829881 162 TAIMLLDEPTTWLDISHQIDLLELLSELNreKGYTLAAVLHDLNQACRyASHLIALREGKIVAQGAPKEIV 232
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAALRDVS--KGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELL 223
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
8-226 |
4.90e-25 |
|
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: 97.77 E-value: 4.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 8 LRGEQLTLGYG--KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYaSKEVARRIGL 85
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL-EKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 86 LAQNattlgditvqelvargryPHqpLFTrwrkedeeavTKAMQATGIThladqsvdtLSGGQRQRAWIAMVLAQETAIM 165
Cdd:cd03247 80 LNQR------------------PY--LFD----------TTLRNNLGRR---------FSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15829881 166 LLDEPTTWLDISHQIDLLELLSELNREKgyTLAAVLHDLnQACRYASHLIALREGKIVAQG 226
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDK--TLIWITHHL-TGIEHMDKILFLENGKIIMQG 178
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
21-238 |
5.30e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 100.93 E-value: 5.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHV-WL-DGEHIQHYAS---------------------- 76
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIeWIfKDEKNKKKTKekekvleklviqktrfkkikki 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 77 KEVARRIGLLAQNAT-TLGDITVQELVARGryphqPLFTRWRKEdeEAVTKAMQATGITHLA----DQSVDTLSGGQRQR 151
Cdd:PRK13651 101 KEIRRRVGVVFQFAEyQLFEQTIEKDIIFG-----PVSMGVSKE--EAKKRAAKYIELVGLDesylQRSPFELSGGQKRR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 152 AWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNrEKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
Cdd:PRK13651 174 VALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLN-KQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDI 252
|
....*....
gi 15829881 232 VTAE--LIE 238
Cdd:PRK13651 253 LSDNkfLIE 261
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-231 |
6.15e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 99.46 E-value: 6.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 1 MTESVarLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRL--MTP---AHGHVWLDGEHIqhYA 75
Cdd:PRK14239 1 MTEPI--LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPevtITGSIVYNGHNI--YS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 76 SK----EVARRIGLLAQNATTLgDITVQELVARGryphqpLFTRWRKEDE---EAVTKAMQATGI-----THLADQSVdT 143
Cdd:PRK14239 77 PRtdtvDLRKEIGMVFQQPNPF-PMSIYENVVYG------LRLKGIKDKQvldEAVEKSLKGASIwdevkDRLHDSAL-G 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 144 LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD-ISH-QIDllELLSELnrEKGYTLAAVLHDLNQACRYASHLIALREGK 221
Cdd:PRK14239 149 LSGGQQQRVCIARVLATSPKIILLDEPTSALDpISAgKIE--ETLLGL--KDDYTMLLVTRSMQQASRISDRTGFFLDGD 224
|
250
....*....|
gi 15829881 222 IVAQGAPKEI 231
Cdd:PRK14239 225 LIEYNDTKQM 234
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
18-237 |
7.98e-25 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 100.92 E-value: 7.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEV--ARR-IGLLAQNATTLG 94
Cdd:COG1135 16 GPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELraARRkIGMIFQHFNLLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 95 DITVQELVARgryphqPL-FTRWRKEDEEA-VTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
Cdd:COG1135 96 SRTVAENVAL------PLeIAGVPKAEIRKrVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 173 WLD--ISHQIdlLELLSELNREKGYTLaaVL--HDLN---QACryasHLIA-LREGKIVAQG-------APKEIVTAELI 237
Cdd:COG1135 170 ALDpeTTRSI--LDLLKDINRELGLTI--VLitHEMDvvrRIC----DRVAvLENGRIVEQGpvldvfaNPQSELTRRFL 241
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
25-238 |
8.70e-25 |
|
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: 102.84 E-value: 8.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMtPAHGHVWLDGEHIQHYASKE---VARRIGLLAQnattlgD------ 95
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRAlrpLRRRMQVVFQ------Dpfgsls 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 96 --ITVQELVARGRYPHQPLFTrwRKEDEEAVTKAMQATGithLADQSVD----TLSGGQRQRAWIAMVLAQETAIMLLDE 169
Cdd:COG4172 377 prMTVGQIIAEGLRVHGPGLS--AAERRARVAEALEEVG---LDPAARHryphEFSGGQRQRIAIARALILEPKLLVLDE 451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15829881 170 PTTWLDISHQIDLLELLSELNREKGytLAAVL--HDLnQACRYASH-LIALREGKIVAQG-------APKEIVTAELIE 238
Cdd:COG4172 452 PTSALDVSVQAQILDLLRDLQREHG--LAYLFisHDL-AVVRALAHrVMVMKDGKVVEQGpteqvfdAPQHPYTRALLA 527
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
17-231 |
1.02e-24 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 99.27 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKE-------------VARRI 83
Cdd:PRK10619 15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDgqlkvadknqlrlLRTRL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 84 GLLAQNATTLGDITVQELVARGryPHQPLFTRwRKEDEEAVTKAMQATGITHLADQSVDT-LSGGQRQRAWIAMVLAQET 162
Cdd:PRK10619 95 TMVFQHFNLWSHMTVLENVMEA--PIQVLGLS-KQEARERAVKYLAKVGIDERAQGKYPVhLSGGQQQRVSIARALAMEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15829881 163 AIMLLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
Cdd:PRK10619 172 EVLLFDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
24-220 |
1.25e-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: 98.31 E-value: 1.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVarrigLLAQNATTLGDITVQELVA 103
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPWLTVRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 104 RGryPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLL 183
Cdd:TIGR01184 77 LA--VDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQ 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 15829881 184 ELLSELNREKGYTLAAVLHDLNQACRYASHLIALREG 220
Cdd:TIGR01184 155 EELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
25-231 |
2.12e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 99.04 E-value: 2.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLdGEHIQHYASKE-----VARRIGLLAQ-NATTLGDITV 98
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVSSTSKQkeikpVRKKVGVVFQfPESQLFEETV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 99 QELVARGryPHQplFTRWRKEDEEAVTKAMQATGIT-HLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS 177
Cdd:PRK13643 103 LKDVAFG--PQN--FGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15829881 178 HQIDLLELLSELNrEKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
Cdd:PRK13643 179 ARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDV 231
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-241 |
3.36e-24 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 97.27 E-value: 3.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 5 VARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARR-I 83
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 84 GLLAQNATTLGDITVQELVARGRYPHQPLFTRWRKEDEEAVtkaMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETA 163
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANEL---MEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPK 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15829881 164 IMLLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIY 241
Cdd:PRK10895 158 FILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVY 234
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-239 |
3.42e-24 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 97.56 E-value: 3.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 1 MTE-SVARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYAS--- 76
Cdd:COG4598 1 MTDtAPPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDrdg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 77 -------KEVAR---RIGLLAQNATTLGDITVQELVARGryPHQPLftrwRKEDEEAVTKAM---QATGITHLADQSVDT 143
Cdd:COG4598 81 elvpadrRQLQRirtRLGMVFQSFNLWSHMTVLENVIEA--PVHVL----GRPKAEAIERAEallAKVGLADKRDAYPAH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 144 LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIshqidllELLSELNR------EKGYTLAAVLHDLNQACRYASHLIAL 217
Cdd:COG4598 155 LSGGQQQRAAIARALAMEPEVMLFDEPTSALDP-------ELVGEVLKvmrdlaEEGRTMLVVTHEMGFARDVSSHVVFL 227
|
250 260
....*....|....*....|..
gi 15829881 218 REGKIVAQGAPKEIVTAELIER 239
Cdd:COG4598 228 HQGRIEEQGPPAEVFGNPKSER 249
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
8-236 |
3.52e-24 |
|
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: 96.83 E-value: 3.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARR-IGLL 86
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAgIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 87 AQNATTLGDITVQE-----LVARGRyphqplftRWRKEDEEA-----VTKAMqatgithLADQSVDtLSGGQRQRAWIAM 156
Cdd:TIGR03410 81 PQGREIFPRLTVEEnlltgLAALPR--------RSRKIPDEIyelfpVLKEM-------LGRRGGD-LSGGQQQQLAIAR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 157 VLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAEL 236
Cdd:TIGR03410 145 ALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDKV 224
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
25-223 |
3.68e-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: 3.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQN--ATTLGDITVQE-- 100
Cdd:COG1101 24 GLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVFQDpmMGTAPSMTIEEnl 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 101 LVARGRypHQPLFTRWrkedeeAVTKAMQATGITHLA----------DQSVDTLSGGQRQrAwIAMVLA--QETAIMLLD 168
Cdd:COG1101 104 ALAYRR--GKRRGLRR------GLTKKRRELFRELLAtlglglenrlDTKVGLLSGGQRQ-A-LSLLMAtlTKPKLLLLD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15829881 169 EPTTWLD--ISHQIdlLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIV 223
Cdd:COG1101 174 EHTAALDpkTAALV--LELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
6-231 |
3.95e-24 |
|
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: 100.98 E-value: 3.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 6 ARLRGEQLTLGY--GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRI 83
Cdd:COG4618 329 GRLSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHI 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 84 GLLAQNaTTLGDITVQELVARgryphqplFTrwrKEDEEAVTKAMQATGI------------THLADQSVdTLSGGQRQR 151
Cdd:COG4618 409 GYLPQD-VELFDGTIAENIAR--------FG---DADPEKVVAAAKLAGVhemilrlpdgydTRIGEGGA-RLSGGQRQR 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 152 AWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEI 231
Cdd:COG4618 476 IGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDEV 553
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
11-239 |
4.99e-24 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 101.01 E-value: 4.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 11 EQLTLGYGKYTVA-ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQN 89
Cdd:COG1132 343 ENVSFSYPGDRPVlKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 90 aTTLGDITVQELVARGRyphqplftrwRKEDEEAVTKAMQATGI------------THLADQSVdTLSGGQRQRAWIAMV 157
Cdd:COG1132 423 -TFLFSGTIRENIRYGR----------PDATDEEVEEAAKAAQAhefiealpdgydTVVGERGV-NLSGGQRQRIAIARA 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 158 LAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKgyTLAAVLHDLNQAcRYASHLIALREGKIVAQGAPkeivtAELI 237
Cdd:COG1132 491 LLKDPPILILDEATSALDTETEALIQEALERLMKGR--TTIVIAHRLSTI-RNADRILVLDDGRIVEQGTH-----EELL 562
|
..
gi 15829881 238 ER 239
Cdd:COG1132 563 AR 564
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
13-259 |
5.05e-24 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 99.52 E-value: 5.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 13 LTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNATT 92
Cdd:PRK11607 25 LTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ--RPINMMFQSYAL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 93 LGDITVQELVARG----RYPhqplftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168
Cdd:PRK11607 103 FPHMTVEQNIAFGlkqdKLP--------KAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 169 EPTTWLDIS----HQIDLLELLSELnrekGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI-------VTAELI 237
Cdd:PRK11607 175 EPMGALDKKlrdrMQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIyehpttrYSAEFI 250
|
250 260 270
....*....|....*....|....*....|.
gi 15829881 238 ERIYGLRC---------MIIDDPVAGTPLVV 259
Cdd:PRK11607 251 GSVNVFEGvlkerqedgLVIDSPGLVHPLKV 281
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-225 |
5.20e-24 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 97.24 E-value: 5.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 6 ARLRGEQLTLGYGKY----TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYAskevAR 81
Cdd:COG4525 2 SMLTVRHVSVRYPGGgqpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG----AD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 82 RiGLLAQNATTLGDITVQELVARG-RYPHQPlftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQ 160
Cdd:COG4525 78 R-GVVFQKDALLPWLNVLDNVAFGlRLRGVP-----KAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15829881 161 ETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIAL--REGKIVAQ 225
Cdd:COG4525 152 DPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRIVER 218
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-238 |
5.75e-24 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 100.55 E-value: 5.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMtPAHGHVWLDGEHIQHYASKE---VARRIGLLAQ--NATT 92
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQllpVRHRIQVVFQdpNSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 93 LGDITVQELVARGRYPHQPLFTRwrKEDEEAVTKAMQATGITHLADQSVDT-LSGGQRQRAWIAMVLAQETAIMLLDEPT 171
Cdd:PRK15134 376 NPRLNVLQIIEEGLRVHQPTLSA--AQREQQVIAVMEEVGLDPETRHRYPAeFSGGQRQRIAIARALILKPSLIILDEPT 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15829881 172 TWLDISHQIDLLELLSELNREKGYTLAAVLHDLnQACRYASH-LIALREGKIVAQG-------APKEIVTAELIE 238
Cdd:PRK15134 454 SSLDKTVQAQILALLKSLQQKHQLAYLFISHDL-HVVRALCHqVIVLRQGEVVEQGdcervfaAPQQEYTRQLLA 527
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
11-230 |
5.82e-24 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 96.53 E-value: 5.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 11 EQLTLGY-GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQN 89
Cdd:cd03254 6 ENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 90 ATTLGDiTVQELVARGRyphqplfTRWRKEDEEAVTKAMQATGI---------THLADQSvDTLSGGQRQRAWIAMVLAQ 160
Cdd:cd03254 86 TFLFSG-TIMENIRLGR-------PNATDEEVIEAAKEAGAHDFimklpngydTVLGENG-GNLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 161 ETAIMLLDEPTTWLDISHQIDLLELLSELNreKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKE 230
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLM--KGRTSIIIAHRLS-TIKNADKILVLDDGKIIEEGTHDE 223
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
25-226 |
6.18e-24 |
|
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: 96.19 E-value: 6.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRL-----MTpaHGHVWLDGEHIQHYaskEVARRIGLLAQNATTLGDITVQ 99
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRvegggTT--SGQILFNGQPRKPD---QFQKCVAYVRQDDILLPGLTVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 100 ELV---ARGRYP-HQPLFTRwrkeDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
Cdd:cd03234 100 ETLtytAILRLPrKSSDAIR----KKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15829881 176 ISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG 226
Cdd:cd03234 176 SFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-231 |
1.30e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 96.77 E-value: 1.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYAS----KEVARRIGLLAQ-NATTL 93
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkyiRPVRKRIGMVFQfPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 94 GDITVQELVARGryPHQplftrWRKEDEEAVTKA----MQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
Cdd:PRK13646 99 FEDTVEREIIFG--PKN-----FKMNLDEVKNYAhrllMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15829881 170 PTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
Cdd:PRK13646 172 PTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
8-233 |
1.49e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 96.59 E-value: 1.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 8 LRGEQLTLGYGKYTVA-ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYAS-KEVARRIGL 85
Cdd:PRK13644 2 IRLENVSYSYPDGTPAlENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 86 LAQNATT--LGDiTVQELVARGryPHQ----PLFTRWRkedeeaVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLA 159
Cdd:PRK13644 82 VFQNPETqfVGR-TVEEDLAFG--PENlclpPIEIRKR------VDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15829881 160 QETAIMLLDEPTTWLDISHQIDLLELLSELNrEKGYTLAAVLHDLNQaCRYASHLIALREGKIVAQGAPKEIVT 233
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLH-EKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-223 |
1.65e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 98.98 E-value: 1.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLdGEHIqhyaskevarRIGLLA 87
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------KIGYFD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 88 QNATTL-GDITVQELVARGRyphqplftrwRKEDEEAVTKAMQATGIT-HLADQSVDTLSGGQRQRAWIAMVLAQETAIM 165
Cdd:COG0488 385 QHQEELdPDKTVLDELRDGA----------PGGTEQEVRGYLGRFLFSgDDAFKPVGVLSGGEKARLALAKLLLSPPNVL 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15829881 166 LLDEPTTWLDishqIDLLELLSE-LNREKGyTLAAVLHDlnqacRY-----ASHLIALREGKIV 223
Cdd:COG0488 455 LLDEPTNHLD----IETLEALEEaLDDFPG-TVLLVSHD-----RYfldrvATRILEFEDGGVR 508
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
19-231 |
2.03e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 95.95 E-value: 2.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 19 KYTVaENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATT--LGdI 96
Cdd:PRK13650 20 KYTL-NDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQNPDNqfVG-A 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 97 TVQELVARGR----YPHQplftrwrkEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
Cdd:PRK13650 98 TVEDDVAFGLenkgIPHE--------EMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15829881 173 WLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACrYASHLIALREGKIVAQGAPKEI 231
Cdd:PRK13650 170 MLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPREL 227
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
8-231 |
3.10e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 95.54 E-value: 3.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 8 LRGEQLTLGYGKYTVAENL---TVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIG 84
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLngvSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 85 LLAQNA-TTLGDITVQELVARGR----YPHQPLFTRwrkedeeaVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLA 159
Cdd:PRK13642 85 MVFQNPdNQFVGATVEDDVAFGMenqgIPREEMIKR--------VDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15829881 160 QETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRyASHLIALREGKIVAQGAPKEI 231
Cdd:PRK13642 157 LRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSEL 227
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
22-233 |
3.25e-23 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 98.64 E-value: 3.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTLGDiTVQEL 101
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSG-SVREN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 102 VARGryphqplFTRWRKEDEEAVTKAMQA----TGITHLADQSVDT----LSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
Cdd:TIGR00958 575 IAYG-------LTDTPDEEIMAAAKAANAhdfiMEFPNGYDTEVGEkgsqLSGGQKQRIAIARALVRKPRVLILDEATSA 647
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 174 LDISHQidllELLSELNREKGYTLAAVLHDLnQACRYASHLIALREGKIVAQGAPKEIVT 233
Cdd:TIGR00958 648 LDAECE----QLLQESRSRASRTVLLIAHRL-STVERADQILVLKKGSVVEMGTHKQLME 702
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
11-231 |
4.06e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 95.56 E-value: 4.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyaskEVARRIGLLAQna 90
Cdd:COG4152 5 KGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP----EDRRRIGYLPE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 91 ttlgditvqelvARGRYPHQPL------FTRWR----KEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQ 160
Cdd:COG4152 79 ------------ERGLYPKMKVgeqlvyLARLKglskAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLH 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15829881 161 ETAIMLLDEPTTWLD-ISHQIdLLELLSELnREKGytlAAVL---HDLNQACRYASHLIALREGKIVAQGAPKEI 231
Cdd:COG4152 147 DPELLILDEPFSGLDpVNVEL-LKDVIREL-AAKG---TTVIfssHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
8-222 |
8.37e-23 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 91.89 E-value: 8.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 8 LRGEQLTLGYG--KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGL 85
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 86 LAQNATTLGDiTVQELVargryphqplftrwrkedeeavtkamqatgithladqsvdtLSGGQRQRAWIAMVLAQETAIM 165
Cdd:cd03246 81 LPQDDELFSG-SIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15829881 166 LLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNqACRYASHLIALREGKI 222
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPE-TLASADRILVLEDGRV 173
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
17-226 |
9.14e-23 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 93.54 E-value: 9.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEH------IQHYASKEVARRIGLLAQNA 90
Cdd:COG4161 12 YGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdfsqkPSEKAIRLLRQKVGMVFQQY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 91 TTLGDITV-QELVARgryPHQPLftrwRKEDEEAVTKAMQ---ATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIML 166
Cdd:COG4161 92 NLWPHLTVmENLIEA---PCKVL----GLSKEQAREKAMKllaRLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15829881 167 LDEPTTWLD--ISHQIdlLELLSELNrEKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG 226
Cdd:COG4161 165 FDEPTAALDpeITAQV--VEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG 223
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
17-226 |
1.00e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 93.54 E-value: 1.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHI---QHYASKEVA---RRIGLLAQNA 90
Cdd:PRK11124 12 YGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIRelrRNVGMVFQQY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 91 TTLGDITVQE-LVargRYPHQPLFTrwrkEDEEAVTKAMQATGITHLADQSvDT----LSGGQRQRAWIAMVLAQETAIM 165
Cdd:PRK11124 92 NLWPHLTVQQnLI---EAPCRVLGL----SKDQALARAEKLLERLRLKPYA-DRfplhLSGGQQQRVAIARALMMEPQVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15829881 166 LLDEPTTWLD--ISHQIdlLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG 226
Cdd:PRK11124 164 LFDEPTAALDpeITAQI--VSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
11-239 |
1.24e-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: 1.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHI--------QHYASKEVARR 82
Cdd:PRK11264 7 KNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslsqQKGLIRQLRQH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 83 IGLLAQNATTLGDITVQELVARGryphqPLFTRWR-KEDEEAVTKAMQA-TGITHLADQSVDTLSGGQRQRAWIAMVLAQ 160
Cdd:PRK11264 87 VGFVFQNFNLFPHRTVLENIIEG-----PVIVKGEpKEEATARARELLAkVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15829881 161 ETAIMLLDEPTTWLDISHQIDLLELLSELNREKgYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIER 239
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPR 239
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-206 |
1.30e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 92.85 E-value: 1.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 1 MTESVARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA 80
Cdd:PRK10247 1 MQENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 81 RRIGLLAQNATTLGDITVQELVargrYPHQplfTRWRKEDEEAVTKAMQATGI-THLADQSVDTLSGGQRQRAWIAMVLA 159
Cdd:PRK10247 81 QQVSYCAQTPTLFGDTVYDNLI----FPWQ---IRNQQPDPAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQ 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15829881 160 QETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQ 206
Cdd:PRK10247 154 FMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE 200
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
7-235 |
2.01e-22 |
|
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: 96.35 E-value: 2.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 7 RLRGEQLTLGYGKYT--VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIG 84
Cdd:TIGR01846 455 AITFENIRFRYAPDSpeVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMG 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 85 LLAQNaTTLGDITVQELVARGRyPHQPlftrwrkeDEEAVTKAMQA------TGITHLADQSVD----TLSGGQRQRAWI 154
Cdd:TIGR01846 535 VVLQE-NVLFSRSIRDNIALCN-PGAP--------FEHVIHAAKLAgahdfiSELPQGYNTEVGekgaNLSGGQRQRIAI 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 155 AMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNRekGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIVTA 234
Cdd:TIGR01846 605 ARALVGNPRILIFDEATSALDYESEALIMRNMREICR--GRTVIIIAHRLS-TVRACDRIIVLEKGQIAESGRHEELLAL 681
|
.
gi 15829881 235 E 235
Cdd:TIGR01846 682 Q 682
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
25-237 |
2.05e-22 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 94.48 E-value: 2.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEV--ARR-IGLLAQNATTLGDITVQEL 101
Cdd:PRK11153 23 NVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELrkARRqIGMIFQHFNLLSSRTVFDN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 102 VArgryphQPL-FTRWRKEDEEA-VTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD--IS 177
Cdd:PRK11153 103 VA------LPLeLAGTPKAEIKArVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDpaTT 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15829881 178 HQIdlLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGA-------PKEIVTAELI 237
Cdd:PRK11153 177 RSI--LELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTvsevfshPKHPLTREFI 241
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
17-231 |
3.02e-22 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 94.33 E-value: 3.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQNATTLGDI 96
Cdd:PRK11000 13 YGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE--RGVGMVFQSYALYPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 97 TVQELVARGryphQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
Cdd:PRK11000 91 SVAENMSFG----LKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15829881 177 SHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
Cdd:PRK11000 167 ALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-240 |
4.91e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 92.76 E-value: 4.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHI-----QHYASKEVARRIGLLAQ-NATT 92
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkKIKEVKRLRKEIGLVFQfPEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 93 LGDITVQELVARGryphqPLftRWRKEDEEAVTKAMQATGITHL----ADQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168
Cdd:PRK13645 103 LFQETIEKDIAFG-----PV--NLGENKQEAYKKVPELLKLVQLpedyVKRSPFELSGGQKRRVALAGIIAMDGNTLVLD 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15829881 169 EPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVT-AELIERI 240
Cdd:PRK13645 176 EPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSnQELLTKI 248
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
7-208 |
6.02e-22 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 90.32 E-value: 6.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 7 RLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGll 86
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 87 AQNATTlGDITVQELVArgryphqplFtrWRK---EDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETA 163
Cdd:PRK13539 80 HRNAMK-PALTVAENLE---------F--WAAflgGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRP 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15829881 164 IMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQAC 208
Cdd:PRK13539 148 IWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATHIPLGLPG 192
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
22-239 |
7.23e-22 |
|
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: 94.64 E-value: 7.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTLGDITVQEL 101
Cdd:TIGR03797 468 ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENI 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 102 VARGRYPHQPLFTRWRKEDEEAVTKAMqATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQID 181
Cdd:TIGR03797 548 AGGAPLTLDEAWEAARMAGLAEDIRAM-PMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAI 626
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15829881 182 LLELLSELNrekgYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEI-----VTAELIER 239
Cdd:TIGR03797 627 VSESLERLK----VTRIVIAHRLS-TIRNADRIYVLDAGRVVQQGTYDELmaregLFAQLARR 684
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
7-236 |
2.12e-21 |
|
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: 93.18 E-value: 2.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 7 RLRGEQLTLGY--GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIG 84
Cdd:TIGR01842 316 HLSVENVTIVPpgGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIG 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 85 LLAQNaTTLGDITVQELVARgryphqplFTRwrKEDEEAVTKAMQATGITHLA---DQSVDT--------LSGGQRQRAW 153
Cdd:TIGR01842 396 YLPQD-VELFPGTVAENIAR--------FGE--NADPEKIIEAAKLAGVHELIlrlPDGYDTvigpggatLSGGQRQRIA 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 154 IAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGaPKEIVT 233
Cdd:TIGR01842 465 LARALYGDPKLVVLDEPNSNLDEEGEQALANAIKAL-KARGITVVVITHRPS-LLGCVDKILVLQDGRIARFG-ERDEVL 541
|
...
gi 15829881 234 AEL 236
Cdd:TIGR01842 542 AKL 544
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-239 |
2.15e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 90.48 E-value: 2.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 1 MTESVARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRlMTPAHGHVWLDGEhIQHYASKEVA 80
Cdd:PRK14258 1 MSKLIPAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNR-MNELESEVRVEGR-VEFFNQNIYE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 81 RRIGL--------LAQNATTLGDITVQELVARGRYphqplFTRWRK--EDEEAVTKAMQATG----ITHLADQSVDTLSG 146
Cdd:PRK14258 79 RRVNLnrlrrqvsMVHPKPNLFPMSVYDNVAYGVK-----IVGWRPklEIDDIVESALKDADlwdeIKHKIHKSALDLSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 147 GQRQRAWIAMVLAQETAIMLLDEPTTWLD------ISHQIDLLELLSELnrekgyTLAAVLHDLNQACRYAS-----HLI 215
Cdd:PRK14258 154 GQQQRLCIARALAVKPKVLLMDEPCFGLDpiasmkVESLIQSLRLRSEL------TMVIVSHNLHQVSRLSDftaffKGN 227
|
250 260
....*....|....*....|....
gi 15829881 216 ALREGKIVAQGAPKEIVTAELIER 239
Cdd:PRK14258 228 ENRIGQLVEFGLTKKIFNSPHDSR 251
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
8-232 |
2.17e-21 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 92.40 E-value: 2.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA----RRI 83
Cdd:PRK10070 29 LSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 84 GLLAQNATTLGDITVQELVARGryphQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETA 163
Cdd:PRK10070 109 AMVFQSFALMPHMTVLDNTAFG----MELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPD 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15829881 164 IMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV 232
Cdd:PRK10070 185 ILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
25-242 |
2.18e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 92.77 E-value: 2.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 25 NLTVEipDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvARR--IGLLAQNATTLGDITVQELV 102
Cdd:COG1129 24 SLELR--PGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRD-AQAagIAIIHQELNLVPNLSVAENI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 103 ARGRYPHQPLFTRWRKEDEEAvTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDiSHQID- 181
Cdd:COG1129 101 FLGREPRRGGLIDWRAMRRRA-RELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLT-EREVEr 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15829881 182 LLELLSELnREKGytlAAVL---HDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYG 242
Cdd:COG1129 179 LFRIIRRL-KAQG---VAIIyisHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLMVG 238
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
22-234 |
2.39e-21 |
|
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: 93.24 E-value: 2.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNaTTLGDITVQEL 101
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQD-VVLFNDTIANN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 102 VARGRYphqplftrwRKEDEEAVTKAMQATGITHLADQS---VDT--------LSGGQRQRAWIAMVLAQETAIMLLDEP 170
Cdd:TIGR02203 426 IAYGRT---------EQADRAEIERALAAAYAQDFVDKLplgLDTpigengvlLSGGQRQRLAIARALLKDAPILILDEA 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15829881 171 TTWLDISHQIDLLELLSELNREKgyTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIVTA 234
Cdd:TIGR02203 497 TSALDNESERLVQAALERLMQGR--TTLVIAHRLS-TIEKADRIVVMDDGRIVERGTHNELLAR 557
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
7-217 |
2.97e-21 |
|
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: 92.73 E-value: 2.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 7 RLRGEQLTLGY-GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGL 85
Cdd:TIGR02857 321 SLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 86 LAQNATTLGDiTVQELVARGRyphqplftrwRKEDEEAVTKAMQATGITHLAD---QSVDT--------LSGGQRQRAWI 154
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENIRLAR----------PDASDAEIREALERAGLDEFVAalpQGLDTpigeggagLSGGQAQRLAL 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15829881 155 AMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNRekGYTLAAVLHDLNQACRyASHLIAL 217
Cdd:TIGR02857 470 ARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
18-236 |
3.12e-21 |
|
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: 89.86 E-value: 3.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGE---HIQHYASKEVARRIGLLAQNATTLG 94
Cdd:TIGR02769 22 QRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQdlyQLDRKQRRAFRRDVQLVFQDSPSAV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 95 D--ITVQELVArgryphQPL--FTRWRKEDEEAVTKAM-QATGI-THLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168
Cdd:TIGR02769 102 NprMTVRQIIG------EPLrhLTSLDESEQKARIAELlDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15829881 169 EPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVaqgapKEIVTAEL 236
Cdd:TIGR02769 176 EAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIV-----EECDVAQL 238
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
7-223 |
3.79e-21 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 89.75 E-value: 3.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 7 RLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHY---ASKEVARRI 83
Cdd:PRK10419 12 HYAHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAFRRDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 84 GLLAQNAttLGDITVQELVarGRYPHQPL--FTRWRKEDEEAVTKAM-QATGIT-HLADQSVDTLSGGQRQRAWIAMVLA 159
Cdd:PRK10419 92 QMVFQDS--ISAVNPRKTV--REIIREPLrhLLSLDKAERLARASEMlRAVDLDdSVLDKRPPQLSGGQLQRVCLARALA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15829881 160 QETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIV 223
Cdd:PRK10419 168 VEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
21-234 |
4.85e-21 |
|
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: 92.05 E-value: 4.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 21 TVAENLTVEIPDGHFTAIIGPNGCGKS----TLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVAR----RIGLLAQNA-T 91
Cdd:COG4172 24 EAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgnRIAMIFQEPmT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 92 TLGDI-TVQELVARGRYPHQPLFtrwRKEDEEAVTKAMQATGITHlADQSVDT----LSGGQRQRAWIAMVLAQETAIML 166
Cdd:COG4172 104 SLNPLhTIGKQIAEVLRLHRGLS---GAAARARALELLERVGIPD-PERRLDAyphqLSGGQRQRVMIAMALANEPDLLI 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15829881 167 LDEPTTWLDISHQIDLLELLSELNREKGytlAAVL---HDLNQACRYASHLIALREGKIVAQGAPKEIVTA 234
Cdd:COG4172 180 ADEPTTALDVTVQAQILDLLKDLQRELG---MALLlitHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAA 247
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
22-222 |
5.75e-21 |
|
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: 88.30 E-value: 5.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTLGDiTVQEL 101
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVLFAR-SLQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 102 VARGryphqpLFTRWRKEDEEAVTKAMQATGITHL-------ADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
Cdd:cd03248 108 IAYG------LQSCSFECVKEAAQKAHAHSFISELasgydteVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSAL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15829881 175 DISHQIDLLELLSELNREKGYTLAAvlHDLNQACRyASHLIALREGKI 222
Cdd:cd03248 182 DAESEQQVQQALYDWPERRTVLVIA--HRLSTVER-ADQILVLDGGRI 226
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
8-223 |
6.29e-21 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 88.39 E-value: 6.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 8 LRGEQLTLGY-GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA---RRI 83
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPflrRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 84 GLLAQNATTLGDITVQELVArgryphQPLFTRWRKEDE--EAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQE 161
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVA------IPLIIAGASGDDirRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15829881 162 TAIMLLDEPTTWLDISHQIDLLELLSELNReKGYTLAAVLHDLNQACRYASHLIALREGKIV 223
Cdd:PRK10908 156 PAVLLADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
29-231 |
9.75e-21 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 89.79 E-value: 9.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 29 EIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA---RRIGLLAQNAT-------TLGDI-- 96
Cdd:COG4608 40 DIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRplrRRMQMVFQDPYaslnprmTVGDIia 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 97 ----------------TVQELVAR--------GRYPHQplftrwrkedeeavtkamqatgithladqsvdtLSGGQRQRA 152
Cdd:COG4608 120 eplrihglaskaerreRVAELLELvglrpehaDRYPHE---------------------------------FSGGQRQRI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 153 WIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNqACRYASHLIA---LreGKIVAQGAPK 229
Cdd:COG4608 167 GIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLS-VVRHISDRVAvmyL--GKIVEIAPRD 243
|
..
gi 15829881 230 EI 231
Cdd:COG4608 244 EL 245
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-239 |
1.69e-20 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 90.46 E-value: 1.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 2 TESVARLRGE----QLTLGY-GKYTVA-ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYA 75
Cdd:PRK11176 332 KRVIERAKGDiefrNVTFTYpGKEVPAlRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYT 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 76 SKEVARRIGLLAQNATTLGDiTVQELVArgrYPHQPLFTRwrkEDEEAVTKAMQATGITHLADQSVDT--------LSGG 147
Cdd:PRK11176 412 LASLRNQVALVSQNVHLFND-TIANNIA---YARTEQYSR---EQIEEAARMAYAMDFINKMDNGLDTvigengvlLSGG 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 148 QRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKgyTLAAVLHDLNqACRYASHLIALREGKIVAQGa 227
Cdd:PRK11176 485 QRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLS-TIEKADEILVVEDGEIVERG- 560
|
250
....*....|..
gi 15829881 228 pkeiVTAELIER 239
Cdd:PRK11176 561 ----THAELLAQ 568
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
17-239 |
1.69e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 88.14 E-value: 1.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyaSKEvarriGLLA---QNATTL 93
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDY--SKR-----GLLAlrqQVATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 94 GDitvqelvargryPHQPLFT---------RWRK----EDEEA--VTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVL 158
Cdd:PRK13638 84 QD------------PEQQIFYtdidsdiafSLRNlgvpEAEITrrVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 159 AQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVlHDLNQACRYASHLIALREGKIVAQGAPKEIVT-AELI 237
Cdd:PRK13638 152 VLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISS-HDIDLIYEISDAVYVLRQGQILTHGAPGEVFAcTEAM 230
|
..
gi 15829881 238 ER 239
Cdd:PRK13638 231 EQ 232
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
17-263 |
2.33e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 88.73 E-value: 2.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYAskEVAR-RIGLLAQNATTLGD 95
Cdd:PRK13536 51 YGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARA--RLARaRIGVVPQFDNLDLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 96 ITVQE-LVARGRYphqplFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
Cdd:PRK13536 129 FTVREnLLVFGRY-----FGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 175 DISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAP----KEIVTAELIErIYGlrcmiiDD 250
Cdd:PRK13536 204 DPHARHLIWERLRSL-LARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPhaliDEHIGCQVIE-IYG------GD 275
|
250
....*....|...
gi 15829881 251 PVAGTPLVVPLGR 263
Cdd:PRK13536 276 PHELSSLVKPYAR 288
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-242 |
2.36e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 87.84 E-value: 2.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 13 LTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGH-----VWLDGEHIQHYASK-EVARRIGLL 86
Cdd:PRK14271 27 LTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRSIFNYRDVlEFRRRVGML 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 87 AQNATTLgDITVQELVARGRYPHQPLFtrwRKEDEEAVTKAMQATGI-THLADQSVDT---LSGGQRQRAWIAMVLAQET 162
Cdd:PRK14271 107 FQRPNPF-PMSIMDNVLAGVRAHKLVP---RKEFRGVAQARLTEVGLwDAVKDRLSDSpfrLSGGQQQLLCLARTLAVNP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 163 AIMLLDEPTTWLDISHQIDLLELLSELNREkgYTLAAVLHDLNQACRYASHLIALREGKIVAQG-------APKEIVTAE 235
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGpteqlfsSPKHAETAR 260
|
....*..
gi 15829881 236 LIERIYG 242
Cdd:PRK14271 261 YVAGLSG 267
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
8-207 |
5.20e-20 |
|
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: 85.10 E-value: 5.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIqHYASKEVARRIGLLA 87
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL-AEQRDEPHENILYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 88 QNATTLGDITVQELVARGRYPHQPlftrwrkeDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
Cdd:TIGR01189 80 HLPGLKPELSALENLHFWAAIHGG--------AQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWIL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15829881 168 DEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQA 207
Cdd:TIGR01189 152 DEPTTALDKAGVALLAGLLRAHLARGGIVLLTTHQDLGLV 191
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
8-207 |
5.65e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 85.23 E-value: 5.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTP---AHGHVWLDGEHIQHYASKevARRIG 84
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAE--QRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 85 LLAQNATTLGDITVQELVARGRYPHQPlftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAI 164
Cdd:COG4136 80 ILFQDDLLFPHLSVGENLAFALPPTIG-----RAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15829881 165 MLLDEPTTWLDISHQIDLLELLSELNREKGytLAAVL--HDLNQA 207
Cdd:COG4136 155 LLLDEPFSKLDAALRAQFREFVFEQIRQRG--IPALLvtHDEEDA 197
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-235 |
1.13e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 88.34 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQN----ATTLGDit 97
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRvhlfSATLRD-- 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 98 vQELVArgryphQPlftrwrKEDEEAVTKAMQATGITHLA--DQSVDT--------LSGGQRQRAWIAMVLAQETAIMLL 167
Cdd:PRK11160 433 -NLLLA------AP------NASDEALIEVLQQVGLEKLLedDKGLNAwlgeggrqLSGGEQRRLGIARALLHDAPLLLL 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15829881 168 DEPTTWLDISHQIDLLELLSELNREKgyTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIVTAE 235
Cdd:PRK11160 500 DEPTEGLDAETERQILELLAEHAQNK--TVLMITHRLT-GLEQFDRICVMDNGQIIEQGTHQELLAQQ 564
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
8-225 |
1.14e-19 |
|
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: 83.25 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvARRIGLla 87
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD-ARRAGI-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 88 qnattlgditvqELVargrypHQplftrwrkedeeavtkamqatgithladqsvdtLSGGQRQRAWIAMVLAQETAIMLL 167
Cdd:cd03216 78 ------------AMV------YQ---------------------------------LSVGERQMVEIARALARNARLLIL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15829881 168 DEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQ 225
Cdd:cd03216 107 DEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
16-234 |
1.20e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 85.13 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 16 GYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGehiqhyaskevarRIG-LLAQNATTLG 94
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-------------RVSaLLELGAGFHP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 95 DITVQE---LVAR--GRyphqplftrwRKEDEEAVTKAMQA-TGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168
Cdd:COG1134 102 ELTGREniyLNGRllGL----------SRKEIDEKFDEIVEfAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15829881 169 EpttWL---DISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTA 234
Cdd:COG1134 172 E---VLavgDAAFQKKCLARIREL-RESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-204 |
1.32e-19 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 85.50 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 32 DGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHV-----WLD------GEHIQHYASK------EVARRIGLLAQNATTLg 94
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdWDEildefrGSELQNYFTKllegdvKVIVKPQYVDLIPKAV- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 95 DITVQELVARgryphqplftrwrKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
Cdd:cd03236 104 KGKVGELLKK-------------KDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYL 170
|
170 180 190
....*....|....*....|....*....|
gi 15829881 175 DISHQIDLLELLSELNREKGYTLaAVLHDL 204
Cdd:cd03236 171 DIKQRLNAARLIRELAEDDNYVL-VVEHDL 199
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
25-202 |
5.12e-19 |
|
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: 82.21 E-value: 5.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLS-RLMTPA-HGHVWLDGEHIQhyaSKEVARRIGLLAQNATTLGDITVQElv 102
Cdd:cd03213 27 NVSGKAKPGELTAIMGPSGAGKSTLLNALAgRRTGLGvSGEVLINGRPLD---KRSFRKIIGYVPQDDILHPTLTVRE-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 103 argryphqplftrwrkedeeavTKAMQAtgitHLadQSvdtLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDL 182
Cdd:cd03213 102 ----------------------TLMFAA----KL--RG---LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQV 150
|
170 180
....*....|....*....|
gi 15829881 183 LELLSELnREKGYTLAAVLH 202
Cdd:cd03213 151 MSLLRRL-ADTGRTIICSIH 169
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
22-235 |
7.49e-19 |
|
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: 82.92 E-value: 7.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNaTTLGDITVQEL 101
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQE-NVLFNRSIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 102 VARGRyPHQPlftrwRKEDEEAVTKAMQATGI--------THLADQSVdTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
Cdd:cd03252 96 IALAD-PGMS-----MERVIEAAKLAGAHDFIselpegydTIVGEQGA-GLSGGQRQRIAIARALIHNPRILIFDEATSA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15829881 174 LDISHQIDLLELLSELNreKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIVTAE 235
Cdd:cd03252 169 LDYESEHAIMRNMHDIC--AGRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDELLAEN 227
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
8-221 |
2.08e-18 |
|
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: 79.41 E-value: 2.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGehiqhyaskevARRIGLLA 87
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-----------TVKIGYFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 88 QnattlgditvqelvargryphqplftrwrkedeeavtkamqatgithladqsvdtLSGGQRQRAWIAMVLAQETAIMLL 167
Cdd:cd03221 70 Q-------------------------------------------------------LSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15829881 168 DEPTTWLDISHqIDLLEllSELNREKGyTLAAVLHD---LNQACryaSHLIALREGK 221
Cdd:cd03221 95 DEPTNHLDLES-IEALE--EALKEYPG-TVILVSHDryfLDQVA---TKIIELEDGK 144
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
8-207 |
3.29e-18 |
|
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: 80.23 E-value: 3.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIqHYASKEVARRIGLLA 87
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL-DFQRDSIARGLLYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 88 QNATTLGDITVQELVargRYPHqplftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
Cdd:cd03231 80 HAPGIKTTLSVLENL---RFWH-------ADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWIL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15829881 168 DEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQA 207
Cdd:cd03231 150 DEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLS 189
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
27-204 |
3.56e-18 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 82.45 E-value: 3.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 27 TVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHV-WLdGEHIQHYASK---EVARRIGLLAQNA-------TTLGD 95
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVaWL-GKDLLGMKDDewrAVRSDIQMIFQDPlaslnprMTIGE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 96 ITVQELvaRGRYPHQPlftrwRKEDEEAVTKAMQATGI-THLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
Cdd:PRK15079 120 IIAEPL--RTYHPKLS-----RQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 192
|
170 180 190
....*....|....*....|....*....|
gi 15829881 175 DISHQIDLLELLSELNREKGYTLAAVLHDL 204
Cdd:PRK15079 193 DVSIQAQVVNLLQQLQREMGLSLIFIAHDL 222
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
24-249 |
3.85e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 82.44 E-value: 3.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGeHIQHYASKEVARRIGLLAQNATTL-GDITVQE-- 100
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG-YVPFKRRKEFARRIGVVFGQRSQLwWDLPAIDsf 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 101 -L------VARGRYphqplftrwrKEDEEAVTKAMqatGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
Cdd:COG4586 118 rLlkaiyrIPDAEY----------KKRLDELVELL---DLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIG 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15829881 174 LDISHQIDLLELLSELNREKGYTLaaVL--HDLNQACRYASHLIALREGKIVAQGApkeivTAELIERIYGLRCMIID 249
Cdd:COG4586 185 LDVVSKEAIREFLKEYNRERGTTI--LLtsHDMDDIEALCDRVIVIDHGRIIYDGS-----LEELKERFGPYKTIVLE 255
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
38-237 |
4.91e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 82.21 E-value: 4.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 38 IIGPNGCGKSTLLRTLSRLMTPAHGHVWLD----GEHIQHYAS------------KEVARRIGLLAQ-NATTLGDITVQE 100
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKNNHELitnpyskkiknfKELRRRVSMVFQfPEYQLFKDTIEK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 101 LVARGryphqPLFTRWRKEDEEAVTK---AMQATGITHLaDQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS 177
Cdd:PRK13631 137 DIMFG-----PVALGVKKSEAKKLAKfylNKMGLDDSYL-ERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPK 210
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 178 HQIDLLELLSElNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELI 237
Cdd:PRK13631 211 GEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQHI 269
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
8-220 |
7.54e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 80.51 E-value: 7.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYAskevARRiGLLA 87
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG----AER-GVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 88 QNATTLGDITVQELVARGryphQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
Cdd:PRK11248 77 QNEGLLPWRNVQDNVAFG----LQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15829881 168 DEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREG 220
Cdd:PRK11248 153 DEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
11-204 |
9.50e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 80.16 E-value: 9.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwldgehiqhyaSKEVARRIGLLAQNA 90
Cdd:PRK09544 8 ENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKLRIGYVPQKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 91 TTlgDITVQELVARgryphqplFTRWR----KEDEEAVTKAMQATgitHLADQSVDTLSGGQRQRAWIAMVLAQETAIML 166
Cdd:PRK09544 77 YL--DTTLPLTVNR--------FLRLRpgtkKEDILPALKRVQAG---HLIDAPMQKLSGGETQRVLLARALLNRPQLLV 143
|
170 180 190
....*....|....*....|....*....|....*...
gi 15829881 167 LDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDL 204
Cdd:PRK09544 144 LDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDL 181
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
8-226 |
1.49e-17 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 79.58 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWL---DGEHIQHYASKEVARRI- 83
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDLYALSEAERRRl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 84 -----GLLAQNA-------TTLGDITVQELVARGryphqplftrWRKEDEeavtkaMQATGITHLADQSVD--------- 142
Cdd:PRK11701 87 lrtewGFVHQHPrdglrmqVSAGGNIGERLMAVG----------ARHYGD------IRATAGDWLERVEIDaariddlpt 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 143 TLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGytLAAVL--HDLNQACRYASHLIALREG 220
Cdd:PRK11701 151 TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELG--LAVVIvtHDLAVARLLAHRLLVMKQG 228
|
....*.
gi 15829881 221 KIVAQG 226
Cdd:PRK11701 229 RVVESG 234
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
7-237 |
1.70e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 79.36 E-value: 1.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 7 RLRGEQLTLGYGKYTVaENLTVEIPDGHFTAIIGPNGCGKS----TLLRTLSRLMTPAHGHVWLDGEHIQhyASKEVARR 82
Cdd:PRK10418 4 QIELRNIALQAAQPLV-HGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVA--PCALRGRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 83 IGLLAQNAT-------TLGDITVQELVARGRYPhqplftrwrkeDEEAVTKAMQATGITH---LADQSVDTLSGGQRQRA 152
Cdd:PRK10418 81 IATIMQNPRsafnplhTMHTHARETCLALGKPA-----------DDATLTAALEAVGLENaarVLKLYPFEMSGGMLQRM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 153 WIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG------ 226
Cdd:PRK10418 150 MIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGdvetlf 229
|
250
....*....|..
gi 15829881 227 -APKEIVTAELI 237
Cdd:PRK10418 230 nAPKHAVTRSLV 241
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-204 |
1.78e-17 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 81.78 E-value: 1.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 32 DGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDG---EHIQHYASKEVARRIGLLAQnattlGDITV----Q--ELV 102
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPswdEVLKRFRGTELQNYFKKLYN-----GEIKVvhkpQyvDLI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 103 AR---GRyphqplfTR--WRKEDEEAVTKAM-QATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
Cdd:PRK13409 173 PKvfkGK-------VRelLKKVDERGKLDEVvERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDI 245
|
170 180
....*....|....*....|....*...
gi 15829881 177 SHQIDLLELLSELNREKgYTLaAVLHDL 204
Cdd:PRK13409 246 RQRLNVARLIRELAEGK-YVL-VVEHDL 271
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
8-226 |
2.09e-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: 2.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWL---DGEHIQHYASKEVARRI- 83
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYimrSGAELELYQLSEAERRRl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 84 -----GLLAQNATtlgDITVQELVARGRYPHQPLFT--RWRKEDEEAVTKAMQATGI--THLADQSVdTLSGGQRQRAWI 154
Cdd:TIGR02323 84 mrtewGFVHQNPR---DGLRMRVSAGANIGERLMAIgaRHYGNIRATAQDWLEEVEIdpTRIDDLPR-AFSGGMQQRLQI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15829881 155 AMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG 226
Cdd:TIGR02323 160 ARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
24-232 |
4.82e-17 |
|
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: 80.23 E-value: 4.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHV-------WLDGEHIQHYASKEVARRIGLLAQNATTlgdi 96
Cdd:TIGR03269 301 DNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdeWVDMTKPGPDGRGRAKRYIGILHQEYDL---- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 97 tvqelvargrYPHQPLFTRWRKE------DEEAVTKA---MQATGITHLADQSV-----DTLSGGQRQRAWIAMVLAQET 162
Cdd:TIGR03269 377 ----------YPHRTVLDNLTEAiglelpDELARMKAvitLKMVGFDEEKAEEIldkypDELSEGERHRVALAQVLIKEP 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15829881 163 AIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDL---NQACRYAShliALREGKIVAQGAPKEIV 232
Cdd:TIGR03269 447 RIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMdfvLDVCDRAA---LMRDGKIVKIGDPEEIV 516
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
33-204 |
5.53e-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: 80.21 E-value: 5.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 33 GHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDG---EHIQHYASKEVARRIGLLAQnattlGDITV----Q--ELVA 103
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPswdEVLKRFRGTELQDYFKKLAN-----GEIKVahkpQyvDLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 104 R---GRyphqplfTR--WRKEDEEAVTK-AMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS 177
Cdd:COG1245 174 KvfkGT-------VRelLEKVDERGKLDeLAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIY 246
|
170 180
....*....|....*....|....*..
gi 15829881 178 HQIDLLELLSELNREKGYTLaAVLHDL 204
Cdd:COG1245 247 QRLNVARLIRELAEEGKYVL-VVEHDL 272
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-242 |
7.63e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 79.83 E-value: 7.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 1 MTESVARLRGeqLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDG---EHIQHYASK 77
Cdd:PRK09700 1 MATPYISMAG--IGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinyNKLDHKLAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 78 EVArrIGLLAQNATTLGDITVQELVARGRYPHQPLF----TRWRKEDEEAvTKAMQATGITHLADQSVDTLSGGQRQRAW 153
Cdd:PRK09700 79 QLG--IGIIYQELSVIDELTVLENLYIGRHLTKKVCgvniIDWREMRVRA-AMMLLRVGLKVDLDEKVANLSISHKQMLE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 154 IAMVLAQETAIMLLDEPTTWLdISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVT 233
Cdd:PRK09700 156 IAKTLMLDAKVIIMDEPTSSL-TNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSN 234
|
....*....
gi 15829881 234 AELIERIYG 242
Cdd:PRK09700 235 DDIVRLMVG 243
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
12-220 |
1.13e-16 |
|
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: 76.60 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 12 QLTLGYGKYT----VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHV-WLDGEHIQHYASKEVARRIGLL 86
Cdd:cd03290 2 QVTNGYFSWGsglaTLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhWSNKNESEPSFEATRSRNRYSV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 87 AQNATT--LGDITVQELVARGryphqplfTRWRKEDEEAVTKA---------MQATGITHLADQSVDtLSGGQRQRAWIA 155
Cdd:cd03290 82 AYAAQKpwLLNATVEENITFG--------SPFNKQRYKAVTDAcslqpdidlLPFGDQTEIGERGIN-LSGGQRQRICVA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15829881 156 MVLAQETAIMLLDEPTTWLDIsHQIDLL--ELLSELNREKGYTLAAVLHDLnQACRYASHLIALREG 220
Cdd:cd03290 153 RALYQNTNIVFLDDPFSALDI-HLSDHLmqEGILKFLQDDKRTLVLVTHKL-QYLPHADWIIAMKDG 217
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
25-231 |
1.15e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 78.38 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLdGEHIQHYASKEVA-----RRIGLLAQNATTLGDITVq 99
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVL-NGRVLFDAEKGIClppekRRIGYVFQDARLFPHYKV- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 100 elvaRG--RYPhqplftrWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS 177
Cdd:PRK11144 94 ----RGnlRYG-------MAKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15829881 178 HQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
Cdd:PRK11144 163 RKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
25-238 |
1.15e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 79.30 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 25 NLTVEipDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIqHYASKEVARR--IGLLAQNATTLGDITVQELV 102
Cdd:COG3845 25 SLTVR--PGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV-RIRSPRDAIAlgIGMVHQHFMLVPNLTVAENI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 103 ARGRYPHQPLFTRWRKEDEEaVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDL 182
Cdd:COG3845 102 VLGLEPTKGGRLDRKAARAR-IRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADEL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15829881 183 LELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIE 238
Cdd:COG3845 181 FEILRRL-AAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELAE 235
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
18-231 |
1.30e-16 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 78.35 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvaRRIGLLAQN-ATtlgdi 96
Cdd:PRK11650 15 GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD--RDIAMVFQNyAL----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 97 tvqelvargrYPHQPLFT------RWRK----EDEEAVTKAMQATGITHLADQSVDTLSGGQRQRawIAM--VLAQETAI 164
Cdd:PRK11650 88 ----------YPHMSVREnmayglKIRGmpkaEIEERVAEAARILELEPLLDRKPRELSGGQRQR--VAMgrAIVREPAV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15829881 165 MLLDEPTTWLDISHQIDL-LELLsELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
Cdd:PRK11650 156 FLFDEPLSNLDAKLRVQMrLEIQ-RLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEV 222
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
4-234 |
1.36e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 78.98 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 4 SVARLRGEQLtlgygkYTVAENLTVEIPDGHFTAIIGPNGCGKS-TLLRTLSRLMTPA----HGHVWLDGEHIQHyASKE 78
Cdd:PRK15134 12 SVAFRQQQTV------RTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLH-ASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 79 VAR-----RIGLLAQNATT----LGDITVQ--ELVA--RGRyphqplftrwRKEDEEA-VTKAMQATGITHLADQSVD-- 142
Cdd:PRK15134 85 TLRgvrgnKIAMIFQEPMVslnpLHTLEKQlyEVLSlhRGM----------RREAARGeILNCLDRVGIRQAAKRLTDyp 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 143 -TLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGK 221
Cdd:PRK15134 155 hQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
250
....*....|...
gi 15829881 222 IVAQGAPKEIVTA 234
Cdd:PRK15134 235 CVEQNRAATLFSA 247
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
37-231 |
1.85e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 77.70 E-value: 1.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 37 AIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA---RRIGLLAQNA-------TTLGDITVQELVARGR 106
Cdd:PRK11308 45 AVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKllrQKIQIVFQNPygslnprKKVGQILEEPLLINTS 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 107 YPhqplftrwRKEDEEAVTKAMQATGI-THLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLEL 185
Cdd:PRK11308 125 LS--------AAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNL 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15829881 186 LSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
Cdd:PRK11308 197 MMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQI 242
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
6-241 |
2.85e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 75.69 E-value: 2.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 6 ARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARR-IG 84
Cdd:PRK11614 4 VMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREaVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 85 LLAQNATTLGDITVQELVARGRyphqplFTRWRKEDEEAVTKAMQA-TGITHLADQSVDTLSGGQRQRAWIAMVLAQETA 163
Cdd:PRK11614 84 IVPEGRRVFSRMTVEENLAMGG------FFAERDQFQERIKWVYELfPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 164 IMLLDEPTTWLD--ISHQI-DLLELLselnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERI 240
Cdd:PRK11614 158 LLLLDEPSLGLApiIIQQIfDTIEQL----REQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSA 233
|
.
gi 15829881 241 Y 241
Cdd:PRK11614 234 Y 234
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
16-232 |
3.01e-16 |
|
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: 78.24 E-value: 3.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 16 GYGKyTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTLGD 95
Cdd:TIGR01193 484 GYGS-NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSG 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 96 ITVQELVARGRyphqplftrwRKEDEEAVTKAMQATGI------------THLADQSvDTLSGGQRQRAWIAMVLAQETA 163
Cdd:TIGR01193 563 SILENLLLGAK----------ENVSQDEIWAACEIAEIkddienmplgyqTELSEEG-SSISGGQKQRIALARALLTDSK 631
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15829881 164 IMLLDEPTTWLDISHQIDLLELLSELNREkgyTLAAVLHDLNQACRyASHLIALREGKIVAQGAPKEIV 232
Cdd:TIGR01193 632 VLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDELL 696
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
15-226 |
3.45e-16 |
|
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: 75.26 E-value: 3.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 15 LGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGehiqhyaskevaRRIGLLAQNATTLG 94
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------------RVSSLLGLGGGFNP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 95 DITVQE---LVARgryphqpLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEpt 171
Cdd:cd03220 98 ELTGREniyLNGR-------LLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDE-- 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15829881 172 tWL---DISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG 226
Cdd:cd03220 169 -VLavgDAAFQEKCQRRLREL-LKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
2-235 |
4.65e-16 |
|
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: 77.68 E-value: 4.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 2 TESVARLRGE----QLTLGYGKYT--VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYA 75
Cdd:TIGR03796 468 SEPPRRLSGYvelrNITFGYSPLEppLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIP 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 76 SKEVARRIGLLAQNATTLGDiTVQELVargryphqplfTRW-RKEDEEAVTKAMQATGI------------THLAdQSVD 142
Cdd:TIGR03796 548 REVLANSVAMVDQDIFLFEG-TVRDNL-----------TLWdPTIPDADLVRACKDAAIhdvitsrpggydAELA-EGGA 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 143 TLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLselnREKGYTLAAVLHDLNqACRYASHLIALREGKI 222
Cdd:TIGR03796 615 NLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNL----RRRGCTCIIVAHRLS-TIRDCDEIIVLERGKV 689
|
250
....*....|...
gi 15829881 223 VAQGAPKEIVTAE 235
Cdd:TIGR03796 690 VQRGTHEELWAVG 702
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
12-221 |
9.86e-16 |
|
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: 74.37 E-value: 9.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 12 QLTLGYGKYTvaenLTVE---IPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIqhyASKevarrigllAQ 88
Cdd:cd03237 5 TMKKTLGEFT----LEVEggsISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV---SYK---------PQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 89 NATTLGDITVQELVA---RGRYPHqplfTRWRKEdeeaVTKAMQatgITHLADQSVDTLSGGQRQRAWIAMVLAQETAIM 165
Cdd:cd03237 69 YIKADYEGTVRDLLSsitKDFYTH----PYFKTE----IAKPLQ---IEQILDREVPELSGGELQRVAIAACLSKDADIY 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15829881 166 LLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALrEGK 221
Cdd:cd03237 138 LLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVF-EGE 192
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-204 |
1.19e-15 |
|
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: 76.36 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 26 LTVE---IPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwldgehiqhyaSKEVarRIGLLAQNATTLGDITVQELV 102
Cdd:COG1245 356 LEVEggeIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-----------DEDL--KISYKPQYISPDYDGTVEEFL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 103 aRGRYPhQPLFTRWRKEDeeaVTKAMqatGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDL 182
Cdd:COG1245 423 -RSANT-DDFGSSYYKTE---IIKPL---GLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAV 494
|
170 180
....*....|....*....|..
gi 15829881 183 LELLSELNREKGYTLAAVLHDL 204
Cdd:COG1245 495 AKAIRRFAENRGKTAMVVDHDI 516
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
6-188 |
1.78e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 75.61 E-value: 1.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 6 ARLRGEQLTLGYGKYTV-AENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLmtpahghvWLDGE-HIQHYASKEVArri 83
Cdd:COG4178 361 GALALEDLTLRTPDGRPlLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGL--------WPYGSgRIARPAGARVL--- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 84 gLLAQNA-TTLGdiTVQELVArgrYPHQPlftrwRKEDEEAVTKAMQATGITHLA---DQSVD---TLSGGQRQRAWIAM 156
Cdd:COG4178 430 -FLPQRPyLPLG--TLREALL---YPATA-----EAFSDAELREALEAVGLGHLAerlDEEADwdqVLSLGEQQRLAFAR 498
|
170 180 190
....*....|....*....|....*....|..
gi 15829881 157 VLAQETAIMLLDEPTTWLDISHQIDLLELLSE 188
Cdd:COG4178 499 LLLHKPDWLFLDEATSALDEENEAALYQLLRE 530
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
17-228 |
2.22e-15 |
|
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: 75.82 E-value: 2.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 17 YGKYTVaENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQhyASKEVARR-IGLLAQNATTLGD 95
Cdd:TIGR01257 941 SGRPAV-DRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE--TNLDAVRQsLGMCPQHNILFHH 1017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 96 ITVQElvargrypHQPLFTRWRKEDEEAVTKAMQA----TGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
Cdd:TIGR01257 1018 LTVAE--------HILFYAQLKGRSWEEAQLEMEAmledTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPT 1089
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15829881 172 TWLDISHQIDLLELLseLNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAP 228
Cdd:TIGR01257 1090 SGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
4-232 |
5.90e-15 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 74.23 E-value: 5.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 4 SVARLRG----EQLTLGY-GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKE 78
Cdd:PRK13657 327 DLGRVKGavefDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAS 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 79 VARRIGLLAQNAtTLGDITVQELVARGRyphqPLFTrwrkeDEE--AVTKAMQATGITHLADQSVDT--------LSGGQ 148
Cdd:PRK13657 407 LRRNIAVVFQDA-GLFNRSIEDNIRVGR----PDAT-----DEEmrAAAERAQAHDFIERKPDGYDTvvgergrqLSGGE 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 149 RQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNreKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAP 228
Cdd:PRK13657 477 RQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELM--KGRTTFIIAHRLS-TVRNADRILVFDNGRVVESGSF 553
|
....
gi 15829881 229 KEIV 232
Cdd:PRK13657 554 DELV 557
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
22-204 |
7.38e-15 |
|
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: 71.70 E-value: 7.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEH----IQHYASKEVA--RR--IGLLAQNATTL 93
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdLAQASPREILalRRrtIGYVSQFLRVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 94 GDITVQELVArgryphQPLFtRWRKEDEEAVTKAMQAT---GI-THLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
Cdd:COG4778 106 PRVSALDVVA------EPLL-ERGVDREEARARARELLarlNLpERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDE 178
|
170 180 190
....*....|....*....|....*....|....*
gi 15829881 170 PTTWLDISHQIDLLELLSELnREKGYTLAAVLHDL 204
Cdd:COG4778 179 PTASLDAANRAVVVELIEEA-KARGTAIIGIFHDE 212
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
11-223 |
9.37e-15 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 73.77 E-value: 9.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHV-WLDGEHIQHYA---SKEVArrigll 86
Cdd:PRK15064 323 ENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkWSENANIGYYAqdhAYDFE------ 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 87 aqnattlGDITVQELVARgryphqplftrWRKE-DEEAVTKAMqatgithL---------ADQSVDTLSGGQRQRAWIAM 156
Cdd:PRK15064 397 -------NDLTLFDWMSQ-----------WRQEgDDEQAVRGT-------LgrllfsqddIKKSVKVLSGGEKGRMLFGK 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15829881 157 VLAQETAIMLLDEPTTWLDIsHQIDLLELlsELNREKGyTLAAVLHDLNQACRYASHLIALREGKIV 223
Cdd:PRK15064 452 LMMQKPNVLVMDEPTNHMDM-ESIESLNM--ALEKYEG-TLIFVSHDREFVSSLATRIIEITPDGVV 514
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
22-234 |
2.10e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 72.85 E-value: 2.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 22 VAENLTVEIpdGHFTAI---------------IGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIqhyASKEVA--RRIG 84
Cdd:NF033858 268 EARGLTMRF--GDFTAVdhvsfrirrgeifgfLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---DAGDIAtrRRVG 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 85 LLAQNATTLGDITVQ---ELVARgryphqpLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQR---AwIAMVL 158
Cdd:NF033858 343 YMSQAFSLYGELTVRqnlELHAR-------LFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRlslA-VAVIH 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 159 AQEtaIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQA--C-RyashlIAL-REGKIVAQGAPKEIVTA 234
Cdd:NF033858 415 KPE--LLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAerCdR-----ISLmHAGRVLASDTPAALVAA 487
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
144-234 |
3.33e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 71.31 E-value: 3.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 144 LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIV 223
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVV 233
|
90
....*....|.
gi 15829881 224 AQGAPKEIVTA 234
Cdd:PRK11022 234 ETGKAHDIFRA 244
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
33-244 |
5.08e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.57 E-value: 5.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 33 GHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHY---ASKEVArrIGLLAQNATTLGDITVQELVARGRYPH 109
Cdd:PRK10762 30 GRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNgpkSSQEAG--IGIIHQELNLIPQLTIAENIFLGREFV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 110 QPlFTR--WRKEDEEAvTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLS 187
Cdd:PRK10762 108 NR-FGRidWKKMYAEA-DKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIR 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15829881 188 ELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYGLR 244
Cdd:PRK10762 186 EL-KSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTEDSLIEMMVGRK 241
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
16-230 |
5.65e-14 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 71.29 E-value: 5.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 16 GYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA--RR--IGLLAQNAT 91
Cdd:PRK10535 17 GEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAqlRRehFGFIFQRYH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 92 TLGDITV-QELVARGRYPHQPlftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
Cdd:PRK10535 97 LLSHLTAaQNVEVPAVYAGLE-----RKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 171 TTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRyASHLIALREGKIVAQGAPKE 230
Cdd:PRK10535 172 TGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPPAQE 229
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
24-239 |
8.59e-14 |
|
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: 68.32 E-value: 8.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLM--TPAHGHVWLDGEHIQHYASKEVARR-IGLLAQNATTLGDITVQE 100
Cdd:cd03217 17 KGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERARLgIFLAFQYPPEIPGVKNAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 101 LVargRYphqplftrwrkedeeavtkamqatgithladqsVD-TLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDishq 179
Cdd:cd03217 97 FL---RY---------------------------------VNeGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLD---- 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15829881 180 IDLLELLSE-LN--REKGYTLAAVLHdlNQacRYASHLIA-----LREGKIVAQGaPKEIvtAELIER 239
Cdd:cd03217 137 IDALRLVAEvINklREEGKSVLIITH--YQ--RLLDYIKPdrvhvLYDGRIVKSG-DKEL--ALEIEK 197
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
25-226 |
9.56e-14 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 70.62 E-value: 9.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNaTTLGDITVQELVAR 104
Cdd:COG5265 376 GVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQD-TVLFNDTIAYNIAY 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 105 GRyphqPLFTRwrkEDEEAVTKAMQATG-ITHLADQsVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
Cdd:COG5265 455 GR----PDASE---EEVEAAARAAQIHDfIESLPDG-YDTrvgerglkLSGGEKQRVAIARTLLKNPPILIFDEATSALD 526
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15829881 176 iSH--QidllELLSELNR-EKGYTLAAVLHDLNQAcRYASHLIALREGKIVAQG 226
Cdd:COG5265 527 -SRteR----AIQAALREvARGRTTLVIAHRLSTI-VDADEILVLEAGRIVERG 574
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-204 |
1.18e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 70.22 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 26 LTVE---IPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwldgehiqhyaSKEVarRIGLLAQNATTLGDITVQELV 102
Cdd:PRK13409 355 LEVEggeIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV-----------DPEL--KISYKPQYIKPDYDGTVEDLL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 103 ARGRyphQPLFTRWRKEDeeaVTKAMQatgITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDL 182
Cdd:PRK13409 422 RSIT---DDLGSSYYKSE---IIKPLQ---LERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAV 492
|
170 180
....*....|....*....|..
gi 15829881 183 LELLSELNREKGYTLAAVLHDL 204
Cdd:PRK13409 493 AKAIRRIAEEREATALVVDHDI 514
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
25-240 |
1.19e-13 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 68.56 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 25 NLTVEipDGHFTAIIGPNGCGKSTLLRTlsrLM-----TPAHGHVWLDGEHIQHYASKEVARR-IGLLAQNATTLGDITV 98
Cdd:COG0396 20 NLTIK--PGEVHAIMGPNGSGKSTLAKV---LMghpkyEVTSGSILLDGEDILELSPDERARAgIFLAFQYPVEIPGVSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 99 QEL----VARGRYPHQPLFTrWRKEdeeaVTKAMQATGITH-LADQSVD-TLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
Cdd:COG0396 95 SNFlrtaLNARRGEELSARE-FLKL----LKEKMKELGLDEdFLDRYVNeGFSGGEKKRNEILQMLLLEPKLAILDETDS 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15829881 173 WLDishqIDLLELLSE-LNREKGYTLAAVL--HdlNQacR-----YASHLIALREGKIVAQGapkeivTAELIERI 240
Cdd:COG0396 170 GLD----IDALRIVAEgVNKLRSPDRGILIitH--YQ--RildyiKPDFVHVLVDGRIVKSG------GKELALEL 231
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
11-235 |
1.62e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 70.13 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 11 EQLTLGYGK-YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQN 89
Cdd:PRK10790 344 DNVSFAYRDdNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQD 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 90 ATTLGDiTVQELVARGryphqplftrwRKEDEEAVTKAMQAT-----------GI-THLADQSvDTLSGGQRQRAWIAMV 157
Cdd:PRK10790 424 PVVLAD-TFLANVTLG-----------RDISEEQVWQALETVqlaelarslpdGLyTPLGEQG-NNLSVGQKQLLALARV 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15829881 158 LAQETAIMLLDEPTTWLDISHQIDLLELLSELnREKGyTLAAVLHDLNQACRyASHLIALREGKIVAQGAPKEIVTAE 235
Cdd:PRK10790 491 LVQTPQILILDEATANIDSGTEQAIQQALAAV-REHT-TLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLLAAQ 565
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
23-235 |
1.70e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 69.87 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 23 AENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMtPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATtLGDITVQELV 102
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQ-LPHGTLRDNV 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 103 ARGRyPHQplftrwrkeDEEAVTKAMQATGI------------THLADQSVdTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
Cdd:PRK11174 444 LLGN-PDA---------SDEQLQQALENAWVseflpllpqgldTPIGDQAA-GLSVGQAQRLALARALLQPCQLLLLDEP 512
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15829881 171 TTWLDISHQIDLLELLSELNREKgyTLAAVLHDLNQACRYaSHLIALREGKIVAQGAPKEIVTAE 235
Cdd:PRK11174 513 TASLDAHSEQLVMQALNAASRRQ--TTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
24-221 |
2.09e-13 |
|
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: 67.11 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwldgehiqhyaskEVARRIGLLAQNATTLGDiTVQELVa 103
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV-------------SVPGSIAYVSQEPWIQNG-TIRENI- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 104 rgryphqpLFTR-WRKEDEEAVTKAMQ--------ATGI-THLADQSVdTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
Cdd:cd03250 87 --------LFGKpFDEERYEKVIKACAlepdleilPDGDlTEIGEKGI-NLSGGQKQRISLARAVYSDADIYLLDDPLSA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15829881 174 LDI---SHQIDLLeLLSELNREKgyTLAAVLHDLnQACRYASHLIALREGK 221
Cdd:cd03250 158 VDAhvgRHIFENC-ILGLLLNNK--TRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
11-228 |
2.90e-13 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 67.05 E-value: 2.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 11 EQLTLGYGKY--TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQ 88
Cdd:cd03369 10 ENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 89 NATTLGDITVQELVARGRYphqplftrwrkeDEEAVTKAMQATGithladqSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168
Cdd:cd03369 90 DPTLFSGTIRSNLDPFDEY------------SDEEIYGALRVSE-------GGLNLSQGQRQLLCLARALLKRPRVLVLD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15829881 169 EPTTWLDisHQIDllELLSELNRE--KGYTLAAVLHDLNQACRYASHLIaLREGKIVAQGAP 228
Cdd:cd03369 151 EATASID--YATD--ALIQKTIREefTNSTILTIAHRLRTIIDYDKILV-MDAGEVKEYDHP 207
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
37-244 |
6.76e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 68.01 E-value: 6.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 37 AIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHiQHYAS--KEVARRIGLLAQNATTLGDITVQELVARGRYPHQPLFT 114
Cdd:PRK11288 34 ALMGENGAGKSTLLKILSGNYQPDAGSILIDGQE-MRFASttAALAAGVAIIYQELHLVPEMTVAENLYLGQLPHKGGIV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 115 RwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDiSHQID-LLELLSELnREK 193
Cdd:PRK11288 113 N-RRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLS-AREIEqLFRVIREL-RAE 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 194 GYTLAAVLHDLNQACRYASHLIALREGKIVA-----QGAPKEIVTAELIER----IYGLR 244
Cdd:PRK11288 190 GRVILYVSHRMEEIFALCDAITVFKDGRYVAtfddmAQVDRDQLVQAMVGReigdIYGYR 249
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
8-176 |
6.86e-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: 6.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLdGEHIQhyaskevarrIGLLA 87
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK----------LAYVD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 88 QNATTL-GDITVQELVARGrypHQPLFTRWRKEDEEAVTKAMQATGithlADQS--VDTLSGGQRQRAWIAMVLAQETAI 164
Cdd:TIGR03719 392 QSRDALdPNKTVWEEISGG---LDIIKLGKREIPSRAYVGRFNFKG----SDQQkkVGQLSGGERNRVHLAKTLKSGGNV 464
|
170
....*....|..
gi 15829881 165 MLLDEPTTWLDI 176
Cdd:TIGR03719 465 LLLDEPTNDLDV 476
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
24-234 |
8.64e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 67.96 E-value: 8.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyASKEVarrIGLLAQNATTLGDI------- 96
Cdd:PRK10261 33 RNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRR-RSRQV---IELSEQSAAQMRHVrgadmam 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 97 -------------TVQELVARGRYPHQPLftrwrkEDEEAVTKAMQATGITHLADQSV------DTLSGGQRQRAWIAMV 157
Cdd:PRK10261 109 ifqepmtslnpvfTVGEQIAESIRLHQGA------SREEAMVEAKRMLDQVRIPEAQTilsrypHQLSGGMRQRVMIAMA 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15829881 158 LAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTA 234
Cdd:PRK10261 183 LSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHA 259
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
24-175 |
8.84e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 65.60 E-value: 8.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKevarriglLAQNATTLGditvqelva 103
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE--------YHQDLLYLG--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 104 rgrypHQP----LFTRW----------RKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
Cdd:PRK13538 81 -----HQPgiktELTALenlrfyqrlhGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDE 155
|
....*.
gi 15829881 170 PTTWLD 175
Cdd:PRK13538 156 PFTAID 161
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
25-232 |
1.10e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 67.38 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLS-RLMT--PAHGHVWLDGEHIQhyaSKEVARRIGLLAQNATTLGDITVQE- 100
Cdd:TIGR00955 43 NVSGVAKPGELLAVMGSSGAGKTTLMNALAfRSPKgvKGSGSVLLNGMPID---AKEMRAISAYVQQDDLFIPTLTVREh 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 101 --LVARGRYPHQPlftrWRKEDEEAVTKAMQATGITHLAD------QSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
Cdd:TIGR00955 120 lmFQAHLRMPRRV----TKKEKRERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15829881 173 WLDISHQIDLLELLSELNrEKGYTLAAVLHD-LNQACRYASHLIALREGKIVAQGAPKEIV 232
Cdd:TIGR00955 196 GLDSFMAYSVVQVLKGLA-QKGKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQAV 255
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
22-228 |
1.26e-12 |
|
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: 65.21 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTLGDiTVQE- 100
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQDPVLFSG-TIRSn 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 101 LVARGRYPhqplftrwrkeDEE--AVTKAMQ--------ATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
Cdd:cd03244 98 LDPFGEYS-----------DEElwQALERVGlkefveslPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 171 TTWLDisHQIDllELLSELNRE--KGYTLAAVLHDLNQACRYAShLIALREGKIVAQGAP 228
Cdd:cd03244 167 TASVD--PETD--ALIQKTIREafKDCTVLTIAHRLDTIIDSDR-ILVLDKGRVVEFDSP 221
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-239 |
4.10e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 65.92 E-value: 4.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 5 VARLRGeqLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVW-LDGEHIQHYASKEVARRI 83
Cdd:NF033858 1 VARLEG--VSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvLGGDMADARHRRAVCPRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 84 GLLAQNattLG-----DITVQELV---ARgryphqpLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIA 155
Cdd:NF033858 79 AYMPQG---LGknlypTLSVFENLdffGR-------LFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLC 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 156 MVLAQETAIMLLDEPTT----------WldishqidllELLSELNREK-GYTLAAVLHDLNQACRYaSHLIALREGKIVA 224
Cdd:NF033858 149 CALIHDPDLLILDEPTTgvdplsrrqfW----------ELIDRIRAERpGMSVLVATAYMEEAERF-DWLVAMDAGRVLA 217
|
250
....*....|....*
gi 15829881 225 QGAPkeivtAELIER 239
Cdd:NF033858 218 TGTP-----AELLAR 227
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
37-222 |
4.28e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 64.03 E-value: 4.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 37 AIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIqHYASKEV-----ARRIGLLAQNATTLGDITVQELVA-----RGR 106
Cdd:PRK10584 40 ALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPL-HQMDEEAraklrAKHVGFVFQSFMLIPTLNALENVElpallRGE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 107 YPHQPlftrwRKEDEEAVTKAMQATGITHLADQsvdtLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELL 186
Cdd:PRK10584 119 SSRQS-----RNGAKALLEQLGLGKRLDHLPAQ----LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLL 189
|
170 180 190
....*....|....*....|....*....|....*.
gi 15829881 187 SELNREKGYTLAAVLHDLNQACRYASHLiALREGKI 222
Cdd:PRK10584 190 FSLNREHGTTLILVTHDLQLAARCDRRL-RLVNGQL 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
43-242 |
5.67e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 65.42 E-value: 5.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 43 GCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKE-VARRIGLL---------------AQNATtlgdITVQELVARGR 106
Cdd:COG1129 288 GAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRAGIAYVpedrkgeglvldlsiRENIT----LASLDRLSRGG 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 107 yphqplFTRWRKEdEEAVTKAMQATGI-THLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLEL 185
Cdd:COG1129 364 ------LLDRRRE-RALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRL 436
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 186 LSELNREkGytlAAVL---HDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYG 242
Cdd:COG1129 437 IRELAAE-G---KAVIvisSELPELLGLSDRILVMREGRIVGELDREEATEEAIMAAATG 492
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
18-257 |
8.42e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 64.65 E-value: 8.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 18 GKYTVAENLTVEIPD-----GHFTAIIGPNGCGKSTLLRTLSRLMTPAHG-------HVW-LDGEHIQHYASKEVARR-I 83
Cdd:PRK10938 9 GTFRLSDTKTLQLPSltlnaGDSWAFVGANGSGKSALARALAGELPLLSGerqsqfsHITrLSFEQLQKLVSDEWQRNnT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 84 GLLAQNATTLGDiTVQELVARGryphqplftrwrKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETA 163
Cdd:PRK10938 89 DMLSPGEDDTGR-TTAEIIQDE------------VKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 164 IMLLDEPTTWLDISHQIDLLELLSELNReKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELI------ 237
Cdd:PRK10938 156 LLILDEPFDGLDVASRQQLAELLASLHQ-SGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQALVaqlahs 234
|
250 260
....*....|....*....|
gi 15829881 238 ERIYGLRCMIIDDPVAGTPL 257
Cdd:PRK10938 235 EQLEGVQLPEPDEPSARHAL 254
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
25-242 |
9.55e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 64.75 E-value: 9.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 25 NLTVEIPDGHftAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARR-IGLLAQNATTLGDITVQELVA 103
Cdd:PRK10982 18 NLKVRPHSIH--ALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENgISMVHQELNLVLQRSVMDNMW 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 104 RGRYPHQPLFTRWRK--EDEEAVTKAMqatGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL---DISH 178
Cdd:PRK10982 96 LGRYPTKGMFVDQDKmyRDTKAIFDEL---DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLtekEVNH 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15829881 179 QIDLLELLselnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYG 242
Cdd:PRK10982 173 LFTIIRKL----KERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMVG 232
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
33-240 |
1.07e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 64.30 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 33 GHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGeHIQHYASKEVARRIG--LLAQNATTLGDITVQELVARGRYPHQ 110
Cdd:PRK15439 37 GEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGG-NPCARLTPAKAHQLGiyLVPQEPLLFPNLSVKENILFGLPKRQ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 111 plftrwrkEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELn 190
Cdd:PRK15439 116 --------ASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIREL- 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15829881 191 REKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERI 240
Cdd:PRK15439 187 LAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDIIQAI 236
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
21-202 |
1.46e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 64.13 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLS-RLMTPAH-GHVWLDGEHIqhyaSKEVARRIGLLAQNATTLGDITV 98
Cdd:PLN03211 82 TILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNFtGTILANNRKP----TKQILKRTGFVTQDDILYPHLTV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 99 QE---LVARGRYPHqplfTRWRKEDEEAVTKAMQATGITH-----LADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
Cdd:PLN03211 158 REtlvFCSLLRLPK----SLTKQEKILVAESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEP 233
|
170 180 190
....*....|....*....|....*....|..
gi 15829881 171 TTWLDISHQIDLLELLSELnREKGYTLAAVLH 202
Cdd:PLN03211 234 TSGLDATAAYRLVLTLGSL-AQKGKTIVTSMH 264
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
14-176 |
1.96e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 63.73 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 14 TLGY-GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwldgehiqhYASKEVarRIGLLAQNATT 92
Cdd:PLN03073 515 SFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV---------FRSAKV--RMAVFSQHHVD 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 93 LGDITVQELVARGR-YPHQPlftrwrkedEEAVTKAMQATGIT-HLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
Cdd:PLN03073 584 GLDLSSNPLLYMMRcFPGVP---------EQKLRAHLGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEP 654
|
....*.
gi 15829881 171 TTWLDI 176
Cdd:PLN03073 655 SNHLDL 660
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
11-176 |
4.44e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 62.83 E-value: 4.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLdGEHIQhyaskevarrIGLLAQNA 90
Cdd:PRK11819 328 ENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVK----------LAYVDQSR 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 91 TTL-GDITVQELVARGryphQPLFTRWRKE-DEEAVTKAMQATGithlADQS--VDTLSGGQRQRAWIAMVLAQETAIML 166
Cdd:PRK11819 397 DALdPNKTVWEEISGG----LDIIKVGNREiPSRAYVGRFNFKG----GDQQkkVGVLSGGERNRLHLAKTLKQGGNVLL 468
|
170
....*....|
gi 15829881 167 LDEPTTWLDI 176
Cdd:PRK11819 469 LDEPTNDLDV 478
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
24-226 |
4.96e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 62.57 E-value: 4.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQH---YASKEVARRIGLLAQNA-------TTL 93
Cdd:PRK10261 341 EKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTlspGKLQALRRDIQFIFQDPyasldprQTV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 94 GDITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHladqsvdTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
Cdd:PRK10261 421 GDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPH-------EFSGGQRQRICIARALALNPKVIIADEAVSA 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15829881 174 LDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG 226
Cdd:PRK10261 494 LDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-243 |
5.21e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 62.66 E-value: 5.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTLGDITVQEL 101
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 102 VARGRYPHQPLFTRWRKEDEEAVTKAMQAtGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQiD 181
Cdd:TIGR00957 1381 DPFSQYSDEEVWWALELAHLKTFVSALPD-KLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETD-N 1458
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15829881 182 LLELLSELNREKgYTLAAVLHDLNQACRYaSHLIALREGKIVAQGAPKEIVTAELIerIYGL 243
Cdd:TIGR00957 1459 LIQSTIRTQFED-CTVLTIAHRLNTIMDY-TRVIVLDKGEVAEFGAPSNLLQQRGI--FYSM 1516
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
37-236 |
6.03e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 61.34 E-value: 6.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 37 AIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTlgditvqELVARGRYpHQPLFTRW 116
Cdd:PRK15112 43 AIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPST-------SLNPRQRI-SQILDFPL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 117 R-------KEDEEAVTKAMQATGIthLADQSV---DTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELL 186
Cdd:PRK15112 115 RlntdlepEQREKQIIETLRQVGL--LPDHASyypHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLM 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15829881 187 SELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAEL 236
Cdd:PRK15112 193 LELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPL 242
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
145-204 |
6.54e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 61.66 E-value: 6.54e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 145 SGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDL 204
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDL 222
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
11-203 |
8.44e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.89 E-value: 8.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwldgehiqHYASK-EVArrigLLAQN 89
Cdd:PRK11147 323 ENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI--------HCGTKlEVA----YFDQH 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 90 ATTLG-DITVQELVARGR--------------YPHQPLFTRWRkedeeavtkAMQatgithladqSVDTLSGGQRQRAWI 154
Cdd:PRK11147 391 RAELDpEKTVMDNLAEGKqevmvngrprhvlgYLQDFLFHPKR---------AMT----------PVKALSGGERNRLLL 451
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15829881 155 AMVLAQETAIMLLDEPTTWLDishqIDLLELLSELNREKGYTLAAVLHD 203
Cdd:PRK11147 452 ARLFLKPSNLLILDEPTNDLD----VETLELLEELLDSYQGTVLLVSHD 496
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
10-178 |
1.04e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 61.89 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 10 GEQLTLGYGKYTVAEN-------LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEhiqhyaskevarr 82
Cdd:TIGR00957 634 GNSITVHNATFTWARDlpptlngITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS------------- 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 83 IGLLAQNATTLGDiTVQELVARGRyphqPLFTRWRKEDEEAVT-----KAMQATGITHLADQSVDtLSGGQRQRAWIAMV 157
Cdd:TIGR00957 701 VAYVPQQAWIQND-SLRENILFGK----ALNEKYYQQVLEACAllpdlEILPSGDRTEIGEKGVN-LSGGQKQRVSLARA 774
|
170 180
....*....|....*....|.
gi 15829881 158 LAQETAIMLLDEPTTWLDiSH 178
Cdd:TIGR00957 775 VYSNADIYLFDDPLSAVD-AH 794
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
8-232 |
1.18e-10 |
|
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: 61.36 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRL--MTPAHGHV-----------WLD-----GE 69
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgYVErpskvGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 70 HIQHYAS-----------------KEVARRIGLLAQNATTL-GDITVQELVARGRypHQPLFtrwrkEDEEAVTKAMQ-- 129
Cdd:TIGR03269 81 PCPVCGGtlepeevdfwnlsdklrRRIRKRIAIMLQRTFALyGDDTVLDNVLEAL--EEIGY-----EGKEAVGRAVDli 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 130 -----ATGITHLADQsvdtLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDL 204
Cdd:TIGR03269 154 emvqlSHRITHIARD----LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWP 229
|
250 260
....*....|....*....|....*...
gi 15829881 205 NQACRYASHLIALREGKIVAQGAPKEIV 232
Cdd:TIGR03269 230 EVIEDLSDKAIWLENGEIKEEGTPDEVV 257
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
43-237 |
1.75e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 60.81 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 43 GCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVaRRIGL-----------------LAQNAtTLGDITVQELVARG 105
Cdd:COG3845 294 GNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRER-RRLGVayipedrlgrglvpdmsVAENL-ILGRYRRPPFSRGG 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 106 ryphqplFTRWRKEDEEAvTKAMQATGI-THLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS-----HQ 179
Cdd:COG3845 372 -------FLDRKAIRAFA-EELIEEFDVrTPGPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGaiefiHQ 443
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15829881 180 IdLLELlselnREKGytlAAVL---HDLNQACRYASHLIALREGKIVAQGAPKEiVTAELI 237
Cdd:COG3845 444 R-LLEL-----RDAG---AAVLlisEDLDEILALSDRIAVMYEGRIVGEVPAAE-ATREEI 494
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
25-228 |
2.01e-10 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 59.55 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 25 NLTVEIPDGHFTAIIGPNGCGKSTLL-----RTLSRLMTPAHGHVwldGEHiqhyASKEVARRIGLLAQ----------- 88
Cdd:cd03271 13 NIDVDIPLGVLTCVTGVSGSGKSSLIndtlyPALARRLHLKKEQP---GNH----DRIEGLEHIDKVIVidqspigrtpr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 89 --NATTLGDIT-VQEL---VARG-RYPHQPLFTRWRKED---------EEAVT------------KAMQATGITHLA-DQ 139
Cdd:cd03271 86 snPATYTGVFDeIRELfceVCKGkRYNRETLEVRYKGKSiadvldmtvEEALEffenipkiarklQTLCDVGLGYIKlGQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 140 SVDTLSGGQRQRAWIAMVLAQET---AIMLLDEPTTWL---DISHqidLLELLSELnREKGYTLAAVLHDLNQAcRYASH 213
Cdd:cd03271 166 PATTLSGGEAQRIKLAKELSKRStgkTLYILDEPTTGLhfhDVKK---LLEVLQRL-VDKGNTVVVIEHNLDVI-KCADW 240
|
250 260
....*....|....*....|.
gi 15829881 214 LIAL------REGKIVAQGAP 228
Cdd:cd03271 241 IIDLgpeggdGGGQVVASGTP 261
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
25-226 |
2.35e-10 |
|
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: 58.10 E-value: 2.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSrlmtpahghvwldgehiqhYASKEvARRIGLLAqnattlgditvqelvar 104
Cdd:cd03238 13 NLDVSIPLNVLVVVTGVSGSGKSTLVNEGL-------------------YASGK-ARLISFLP----------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 105 gRYPHQPLFtrwrkedeeAVT--KAMQATGITHLA-DQSVDTLSGGQRQRAWIAMVLAQET--AIMLLDEPTTWLdisHQ 179
Cdd:cd03238 56 -KFSRNKLI---------FIDqlQFLIDVGLGYLTlGQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGL---HQ 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15829881 180 IDLLELLSELNR--EKGYTLAAVLHDLNQACrYASHLIAL------REGKIVAQG 226
Cdd:cd03238 123 QDINQLLEVIKGliDLGNTVILIEHNLDVLS-SADWIIDFgpgsgkSGGKVVFSG 176
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
38-210 |
2.39e-10 |
|
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: 60.33 E-value: 2.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 38 IIGPNGCGKSTLLRTLSRLMTPAHGHVWLdgehiqhyaskEVARRIGLLAQNATTLGDITVQELVARGRYPHQPLFTRWR 117
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVDKDFNGEARP-----------QPGIKVGYLPQEPQLDPTKTVRENVEEGVAEIKDALDRFN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 118 K-------EDEE---------AVTKAMQATGITHLA---------------DQSVDTLSGGQRQRAWIAMVLAQETAIML 166
Cdd:TIGR03719 105 EisakyaePDADfdklaaeqaELQEIIDAADAWDLDsqleiamdalrcppwDADVTKLSGGERRRVALCRLLLSKPDMLL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15829881 167 LDEPTTWLDiSHQIDLLEllSELNREKGyTLAAVLHDlnqacRY 210
Cdd:TIGR03719 185 LDEPTNHLD-AESVAWLE--RHLQEYPG-TVVAVTHD-----RY 219
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
24-194 |
2.47e-10 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 59.20 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTL----SRLMTpaHGHVWLDGEHIQHYASKEVARR-IGLLAQNATTLGDITV 98
Cdd:TIGR01978 17 KGVNLTVKKGEIHAIMGPNGSGKSTLSKTIaghpSYEVT--SGTILFKGQDLLELEPDERARAgLFLAFQYPEEIPGVSN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 99 QELV-----ARGRYPHQPLFTR--WRKEdeeaVTKAMQATGIT-HLADQSVDT-LSGGQRQRAWIAMVLAQETAIMLLDE 169
Cdd:TIGR01978 95 LEFLrsalnARRSARGEEPLDLldFEKL----LKEKLALLDMDeEFLNRSVNEgFSGGEKKRNEILQMALLEPKLAILDE 170
|
170 180
....*....|....*....|....*.
gi 15829881 170 PTTWLDishqIDLLELLSE-LNREKG 194
Cdd:TIGR01978 171 IDSGLD----IDALKIVAEgINRLRE 192
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-242 |
4.07e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 59.56 E-value: 4.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 1 MTESVARLRGeqLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMtPA---HGHVWLDGEHIQHYASK 77
Cdd:PRK13549 1 MMEYLLEMKN--ITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 78 EVARR-IGLLAQNATTLGDITVQELVARGRYPHQPLFTRWRKEDEEAvTKAMQATGITHLADQSVDTLSGGQRQRAWIAM 156
Cdd:PRK13549 78 DTERAgIAIIHQELALVKELSVLENIFLGNEITPGGIMDYDAMYLRA-QKLLAQLKLDINPATPVGNLGLGQQQLVEIAK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 157 VLAQETAIMLLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAEL 236
Cdd:PRK13549 157 ALNKQARLLILDEPTASLTESETAVLLDIIRDL-KAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDI 235
|
....*.
gi 15829881 237 IERIYG 242
Cdd:PRK13549 236 ITMMVG 241
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
13-208 |
4.27e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 59.52 E-value: 4.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 13 LTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwldgehiqhyaSKEVARRIGLLAQNATT 92
Cdd:PRK15064 7 ITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNV-----------SLDPNERLGKLRQDQFA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 93 LGDITVQELVARGrypHQPLftrWR-KEDEEAVTKAMQAT---GItHLADQSV---------------DTLSG------- 146
Cdd:PRK15064 76 FEEFTVLDTVIMG---HTEL---WEvKQERDRIYALPEMSeedGM-KVADLEVkfaemdgytaearagELLLGvgipeeq 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15829881 147 ----------GQRQRAWIAMVLAQETAIMLLDEPTTWLDIsHQIDLLEllSELNrEKGYTLAAVLHD---LNQAC 208
Cdd:PRK15064 149 hyglmsevapGWKLRVLLAQALFSNPDILLLDEPTNNLDI-NTIRWLE--DVLN-ERNSTMIIISHDrhfLNSVC 219
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
38-224 |
4.59e-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: 59.43 E-value: 4.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 38 IIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQhyaskevarrigllAQNattlgditvqelvaRGRY---------- 107
Cdd:COG4615 363 IVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT--------------ADN--------------REAYrqlfsavfsd 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 108 PHqpLFTR----WRKEDEEAVT---KAMQATGITHLADQSVDT--LSGGQRQRawIAMVLA--QETAIMLLDEpttWldI 176
Cdd:COG4615 415 FH--LFDRllglDGEADPARARellERLELDHKVSVEDGRFSTtdLSQGQRKR--LALLVAllEDRPILVFDE---W--A 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15829881 177 SHQ------IDLLELLSELnREKGYTLAAVLHDlnqaCRY---ASHLIALREGKIVA 224
Cdd:COG4615 486 ADQdpefrrVFYTELLPEL-KARGKTVIAISHD----DRYfdlADRVLKMDYGKLVE 537
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
33-175 |
4.83e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 59.74 E-value: 4.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 33 GHFTAIIGPNGCGKSTLLRTLSRLMTpahGHVWLDGEHIQ--HYASKEVARRIGLLAQNATTLGDITVQELVARGRYPHQ 110
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAERVT---TGVITGGDRLVngRPLDSSFQRSIGYVQQQDLHLPTSTVRESLRFSAYLRQ 865
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 111 PLFTRwRKEDEEAVTKAMQATGITHLADQSVDT----LSGGQRQRAWIAMVL-AQETAIMLLDEPTTWLD 175
Cdd:TIGR00956 866 PKSVS-KSEKMEYVEEVIKLLEMESYADAVVGVpgegLNVEQRKRLTIGVELvAKPKLLLFLDEPTSGLD 934
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
17-242 |
8.67e-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: 58.68 E-value: 8.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPA--HGHVWLDGEHIQHYASKEVARR-IGLLAQNATTL 93
Cdd:TIGR02633 11 FGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKASNIRDTERAgIVIIHQELTLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 94 GDITVQELVARGrypHQPLFTRWRKEDEEAVTKA---MQATGITHLAD-QSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
Cdd:TIGR02633 91 PELSVAENIFLG---NEITLPGGRMAYNAMYLRAknlLRELQLDADNVtRPVGDYGGGQQQLVEIAKALNKQARLLILDE 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15829881 170 PTTWLDISHQIDLLELLSELNReKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYG 242
Cdd:TIGR02633 168 PSSSLTEKETEILLDIIRDLKA-HGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMVG 239
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
25-186 |
9.96e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.52 E-value: 9.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRiGL--LAQNATTLG---DITVQ 99
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLAR-GLvyLPEDRQSSGlylDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 100 ELVARGRYPHQPLFTRwRKEDEEAVTKAMQATGI--THlADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS 177
Cdd:PRK15439 360 WNVCALTHNRRGFWIK-PARENAVLERYRRALNIkfNH-AEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVS 437
|
....*....
gi 15829881 178 HQIDLLELL 186
Cdd:PRK15439 438 ARNDIYQLI 446
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
25-231 |
3.25e-09 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 57.33 E-value: 3.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 25 NLTVEIPDGHFTAIIGPNGCGKSTLL---------RTLSRLMTPAHGHVWLDG-EHI----------------------- 71
Cdd:TIGR00630 626 NITVSIPLGLFTCITGVSGSGKSTLIndtlypalaNRLNGAKTVPGRYTSIEGlEHLdkvihidqspigrtprsnpatyt 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 72 -------QHYASKEVARRIGLLA------------QNATTLGDITVQEL----------VARG-RYPHQPLFTRWRK--- 118
Cdd:TIGR00630 706 gvfdeirELFAETPEAKVRGYTPgrfsfnvkggrcEACQGDGVIKIEMHflpdvyvpceVCKGkRYNRETLEVKYKGkni 785
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 119 ---------------EDEEAVTKAMQA---TGITHLA-DQSVDTLSGGQRQRAWIAMVL-AQET--AIMLLDEPTTWLdi 176
Cdd:TIGR00630 786 advldmtveeayeffEAVPSISRKLQTlcdVGLGYIRlGQPATTLSGGEAQRIKLAKELsKRSTgrTLYILDEPTTGL-- 863
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15829881 177 sHQIDLLELLSELNR--EKGYTLAAVLHDLNqACRYASHLIAL------REGKIVAQGAPKEI 231
Cdd:TIGR00630 864 -HFDDIKKLLEVLQRlvDKGNTVVVIEHNLD-VIKTADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
16-233 |
3.42e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 56.82 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 16 GYGKYTVA-ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGehiqhyASKEVARRIGLLAQnATTLG 94
Cdd:PRK13545 32 KDGEYHYAlNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG------SAALIAISSGLNGQ-LTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 95 DITVQELvargryphqpLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
Cdd:PRK13545 105 NIELKGL----------MMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15829881 175 DISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVT 233
Cdd:PRK13545 175 DQTFTKKCLDKMNEF-KEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVD 232
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
144-234 |
3.72e-09 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 56.45 E-value: 3.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 144 LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIV 223
Cdd:COG4170 159 LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTV 238
|
90
....*....|.
gi 15829881 224 AQGAPKEIVTA 234
Cdd:COG4170 239 ESGPTEQILKS 249
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
24-202 |
5.99e-09 |
|
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: 54.08 E-value: 5.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTpahghvWLDGeHIQHYASKEVArrigLLAQnATTLGDITVQELVA 103
Cdd:cd03223 18 KDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWP------WGSG-RIGMPEGEDLL----FLPQ-RPYLPLGTLREQLI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 104 rgrYPhqplftrWRkedeeavtkamqatgithladqsvDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLL 183
Cdd:cd03223 86 ---YP-------WD------------------------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLY 131
|
170
....*....|....*....
gi 15829881 184 ELLselnREKGYTLAAVLH 202
Cdd:cd03223 132 QLL----KELGITVISVGH 146
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
40-176 |
1.02e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.08 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 40 GPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQhyaSKEVARRIGLLAQNATTLGDITVQELV-----ARGRYPHQplft 114
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT---RGDRSRFMAYLGHLPGLKADLSTLENLhflcgLHGRRAKQ---- 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15829881 115 rwrkedeeAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
Cdd:PRK13543 117 --------MPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
138-231 |
1.06e-08 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 55.79 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 138 DQSVDTLSGGQRQRAWIAMVL-AQETAIM-LLDEPTTWLdisHQIDLLELLSELN--REKGYTLAAVLHDlNQACRYASH 213
Cdd:TIGR00630 483 SRAAGTLSGGEAQRIRLATQIgSGLTGVLyVLDEPSIGL---HQRDNRRLINTLKrlRDLGNTLIVVEHD-EDTIRAADY 558
|
90 100
....*....|....*....|....
gi 15829881 214 LIAL------REGKIVAQGAPKEI 231
Cdd:TIGR00630 559 VIDIgpgageHGGEVVASGTPEEI 582
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
21-233 |
1.43e-08 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 55.10 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTLGDiTVQE 100
Cdd:PRK10789 329 PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSD-TVAN 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 101 LVARGRyphqPLFTRwrKEDEEAVTKAMQATGITHLAdQSVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
Cdd:PRK10789 408 NIALGR----PDATQ--QEIEHVARLASVHDDILRLP-QGYDTevgergvmLSGGQKQRISIARALLLNAEILILDDALS 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15829881 173 WLD--ISHQIdlLELLSELNREKGYTLAAvlHDLNqACRYASHLIALREGKIVAQGAPKEIVT 233
Cdd:PRK10789 481 AVDgrTEHQI--LHNLRQWGEGRTVIISA--HRLS-ALTEASEILVMQHGHIAQRGNHDQLAQ 538
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
8-175 |
1.53e-08 |
|
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: 55.40 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 8 LRGEQLTLGYGKYT--VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASkEVARRIGL 85
Cdd:TIGR01257 1938 LRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNIS-DVHQNMGY 2016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 86 LAQNATtlgditVQELVArGRyPHQPLFTRWR----KEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQE 161
Cdd:TIGR01257 2017 CPQFDA------IDDLLT-GR-EHLYLYARLRgvpaEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGC 2088
|
170
....*....|....
gi 15829881 162 TAIMLLDEPTTWLD 175
Cdd:TIGR01257 2089 PPLVLLDEPTTGMD 2102
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
22-202 |
1.70e-08 |
|
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: 55.14 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMtPAHGHVwldgehiqhyASKEVARRIGLLAQNA-TTLGdiTVQE 100
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELW-PVYGGR----------LTKPAKGKLFYVPQRPyMTLG--TLRD 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 101 LVArgrYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSV---------DTLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
Cdd:TIGR00954 534 QII---YPDSSEDMKRRGLSDKDLEQILDNVQLTHILEREGgwsavqdwmDVLSGGEKQRIAMARLFYHKPQFAILDECT 610
|
170 180 190
....*....|....*....|....*....|.
gi 15829881 172 TWLdishQIDLLELLSELNREKGYTLAAVLH 202
Cdd:TIGR00954 611 SAV----SVDVEGYMYRLCREFGITLFSVSH 637
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
8-203 |
1.84e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.79 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLdgehiqhyaSKEVarRIGLLA 87
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL---------AKGI--KLGYFA 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 88 QNATtlgditvqELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGIThlADQSVDT---LSGGQRQRAWIAMVLAQETAI 164
Cdd:PRK10636 382 QHQL--------EFLRADESPLQHLARLAPQELEQKLRDYLGGFGFQ--GDKVTEEtrrFSGGEKARLVLALIVWQRPNL 451
|
170 180 190
....*....|....*....|....*....|....*....
gi 15829881 165 MLLDEPTTWLDISHQIDLLELLSELNRekgyTLAAVLHD 203
Cdd:PRK10636 452 LLLDEPTNHLDLDMRQALTEALIDFEG----ALVVVSHD 486
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
13-202 |
1.97e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 53.42 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 13 LTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLM--TPAHGHVWLDGEHIqhyaskevarrigllAQNA 90
Cdd:COG2401 36 VELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQF---------------GREA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 91 TTLGDItvqelvargryphqplftrWRKEDEEAVTKAMQATGithLAD-----QSVDTLSGGQRQRAWIAMVLAQETAIM 165
Cdd:COG2401 101 SLIDAI-------------------GRKGDFKDAVELLNAVG---LSDavlwlRRFKELSTGQKFRFRLALLLAERPKLL 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 15829881 166 LLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLH 202
Cdd:COG2401 159 VIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATH 195
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
33-202 |
3.33e-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: 52.25 E-value: 3.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 33 GHFTAIIGPNGCGKSTLLRTLSRLMTPAH--GHVWLDGEHIQhyasKEVARRIGLLAQNATTLGDITVQELVargryphq 110
Cdd:cd03232 33 GTLTALMGESGAGKTTLLDVLAGRKTAGVitGEILINGRPLD----KNFQRSTGYVEQQDVHSPNLTVREAL-------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 111 pLFTRWRKEdeeavtkamqatgithladqsvdtLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELN 190
Cdd:cd03232 101 -RFSALLRG------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLA 155
|
170
....*....|..
gi 15829881 191 REkGYTLAAVLH 202
Cdd:cd03232 156 DS-GQAILCTIH 166
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
139-232 |
3.70e-08 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 53.88 E-value: 3.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 139 QSVDTLSGGQRQRAWIAMVLAQET---AIMLLDEPTTWL---DISHqidLLELLSELnREKGYTLAAVLHDLNqACRYAS 212
Cdd:COG0178 822 QPATTLSGGEAQRVKLASELSKRStgkTLYILDEPTTGLhfhDIRK---LLEVLHRL-VDKGNTVVVIEHNLD-VIKTAD 896
|
90 100
....*....|....*....|....*.
gi 15829881 213 HLIAL------REGKIVAQGAPKEIV 232
Cdd:COG0178 897 WIIDLgpeggdGGGEIVAEGTPEEVA 922
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-180 |
4.73e-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: 53.76 E-value: 4.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 19 KYT-----VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTpAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTL 93
Cdd:TIGR01271 1226 KYTeagraVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIF 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 94 GDITVQELVARGRYPHQPLftrWRKEDEEAVtKAMQATGITHLADQSVD---TLSGGQRQRAWIAMVLAQETAIMLLDEP 170
Cdd:TIGR01271 1305 SGTFRKNLDPYEQWSDEEI---WKVAEEVGL-KSVIEQFPDKLDFVLVDggyVLSNGHKQLMCLARSILSKAKILLLDEP 1380
|
170
....*....|.
gi 15829881 171 TTWLD-ISHQI 180
Cdd:TIGR01271 1381 SAHLDpVTLQI 1391
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1-245 |
5.86e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 53.70 E-value: 5.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 1 MTESVARLRGEQLTlGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPA---HGHVWLDGEHIQHYASK 77
Cdd:PLN03140 160 IAESALGMLGINLA-KKTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRLNEFVPR 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 78 EVARRIgllAQNATTLGDITVQELV---ARGryphQPLFTRW-------RKED------EEAVTKAMQATGI-------- 133
Cdd:PLN03140 239 KTSAYI---SQNDVHVGVMTVKETLdfsARC----QGVGTRYdllselaRREKdagifpEAEVDLFMKATAMegvkssli 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 134 ---------------THLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNRekgYTLA 198
Cdd:PLN03140 312 tdytlkilgldickdTIVGDEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVH---LTEA 388
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 15829881 199 AVLHDLNQACRYASHL----IALREGKIVAQGaPKEIVTaELIERiYGLRC 245
Cdd:PLN03140 389 TVLMSLLQPAPETFDLfddiILLSEGQIVYQG-PRDHIL-EFFES-CGFKC 436
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
33-226 |
5.95e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.57 E-value: 5.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 33 GHFTAIIGPNGCGKSTLLRTLSrlMTPAHGHVWLDGE-----HIQHYASKEVARRIGLLAQNATTLGDITVQE---LVAR 104
Cdd:TIGR00956 87 GELTVVLGRPGSGCSTLLKTIA--SNTDGFHIGVEGVitydgITPEEIKKHYRGDVVYNAETDVHFPHLTVGEtldFAAR 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 105 GRYPHqplfTRWRKEDEEAVTK-----AMQATGITHLADQSVDT-----LSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
Cdd:TIGR00956 165 CKTPQ----NRPDGVSREEYAKhiadvYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKIQCWDNATRGL 240
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15829881 175 DIShqiDLLELLSELNREKGYTLAAVLHDLNQACRYASHL----IALREGKIVAQG 226
Cdd:TIGR00956 241 DSA---TALEFIRALKTSANILDTTPLVAIYQCSQDAYELfdkvIVLYEGYQIYFG 293
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
25-240 |
6.35e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 53.05 E-value: 6.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 25 NLTVEipDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQhyASKEVARRigllAQNATTLGDItvqelvar 104
Cdd:PRK10522 343 NLTIK--RGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT--AEQPEDYR----KLFSAVFTDF-------- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 105 grypHqpLFTRWRKEDEEAVTKAMQATGITHLADQS---------VDT-LSGGQRQRAWIAMVLAQETAIMLLDE----- 169
Cdd:PRK10522 407 ----H--LFDQLLGPEGKPANPALVEKWLERLKMAHkleledgriSNLkLSKGQKKRLALLLALAEERDILLLDEwaadq 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15829881 170 -PTTwldisHQIDLLELLSELnREKGYTLAAVLHD---LNQACRyashLIALREGKIVA-QGAPKEIVTAELIERI 240
Cdd:PRK10522 481 dPHF-----RREFYQVLLPLL-QEMGKTIFAISHDdhyFIHADR----LLEMRNGQLSElTGEERDAASRDAVART 546
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
43-225 |
7.58e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.99 E-value: 7.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 43 GCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARR-IGLLAQNATTLGDI---TVQE---LVARGRYPHQPLFTR 115
Cdd:PRK11288 289 GAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAgIMLCPEDRKAEGIIpvhSVADninISARRHHLRAGCLIN 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 116 WRKEDEEAvTKAMQATGI-THLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELnREKG 194
Cdd:PRK11288 369 NRWEAENA-DRFIRSLNIkTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYEL-AAQG 446
|
170 180 190
....*....|....*....|....*....|.
gi 15829881 195 YTLAAVLHDLNQACRYASHLIALREGKIVAQ 225
Cdd:PRK11288 447 VAVLFVSSDLPEVLGVADRIVVMREGRIAGE 477
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
25-226 |
8.35e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 53.24 E-value: 8.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWldgehiqhyaskeVARRIGLLAQ-----NATTLGDItvq 99
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-------------AERSIAYVPQqawimNATVRGNI--- 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 100 elvargryphqpLFtrWRKEDEEAVTKAMQATGI------------THLADQSVDtLSGGQRQRAWIAMVLAQETAIMLL 167
Cdd:PTZ00243 742 ------------LF--FDEEDAARLADAVRVSQLeadlaqlgggleTEIGEKGVN-LSGGQKARVSLARAVYANRDVYLL 806
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15829881 168 DEPTTWLD--ISHQIdLLELLseLNREKGYTLAAVLHDLNQACRyASHLIALREGKIVAQG 226
Cdd:PTZ00243 807 DDPLSALDahVGERV-VEECF--LGALAGKTRVLATHQVHVVPR-ADYVVALGDGRVEFSG 863
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
25-175 |
8.76e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 51.03 E-value: 8.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYAsKEVARRIGllaQNATTLGDITVQELVar 104
Cdd:PRK13541 18 DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA-KPYCTYIG---HNLGLKLEMTVFENL-- 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15829881 105 gryphqplfTRWRK--EDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
Cdd:PRK13541 92 ---------KFWSEiyNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
22-203 |
9.15e-08 |
|
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: 51.07 E-value: 9.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 22 VAENLTVEIPDGhFTAIIGPNGCGKSTLLRTLSRLMTpahGHVWLDGEHIQHYASkevarriglLAQNATTLGDITVQEL 101
Cdd:cd03240 12 FHERSEIEFFSP-LTLIVGQNGAGKTTIIEALKYALT---GELPPNSKGGAHDPK---------LIREGEVRAQVKLAFE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 102 VARG------RYPHQPLFTRWRKEDEeavtkamqatgITHLADQSVDTLSGGQRQ------RAWIAMVLAQETAIMLLDE 169
Cdd:cd03240 79 NANGkkytitRSLAILENVIFCHQGE-----------SNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDE 147
|
170 180 190
....*....|....*....|....*....|....*
gi 15829881 170 PTTWLDISH-QIDLLELLSELNREKGYTLAAVLHD 203
Cdd:cd03240 148 PTTNLDEENiEESLAEIIEERKSQKNFQLIVITHD 182
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
23-207 |
1.14e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 50.44 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 23 AENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSrlmtpahghvwldgehiqhyaskevarrigllaqnattlgditvqeLV 102
Cdd:cd03227 11 FVPNDVTFGEGSLTIITGPNGSGKSTILDAIG----------------------------------------------LA 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 103 ARGRYPHqplfTRWRKEDEEAVTKAMQATGIThladQSVDTLSGGQRQRAWIAMVLA----QETAIMLLDEPTTWLDISH 178
Cdd:cd03227 45 LGGAQSA----TRRRSGVKAGCIVAAVSAELI----FTRLQLSGGEKELSALALILAlaslKPRPLYILDEIDRGLDPRD 116
|
170 180
....*....|....*....|....*....
gi 15829881 179 QIDLLELLSELnREKGYTLAAVLHDLNQA 207
Cdd:cd03227 117 GQALAEAILEH-LVKGAQVIVITHLPELA 144
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
144-234 |
1.27e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 51.73 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 144 LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIV 223
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
90
....*....|.
gi 15829881 224 AQGAPKEIVTA 234
Cdd:PRK15093 239 ETAPSKELVTT 249
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
22-217 |
1.84e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.95 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEH-IQHYASKEVARRIGLLAQNATTLGD----- 95
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHnLKDINLKWWRSKIGVVSQDPLLFSNsiknn 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 96 -----ITVQELVARGRYPHQPLFTRWRKEDEEA------------VTKAMQATGITH----------------------- 135
Cdd:PTZ00265 480 ikyslYSLKDLEALSNYYNEDGNDSQENKNKRNscrakcagdlndMSNTTDSNELIEmrknyqtikdsevvdvskkvlih 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 136 ------------LADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHD 203
Cdd:PTZ00265 560 dfvsalpdkyetLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHR 639
|
250
....*....|....
gi 15829881 204 LNqACRYASHLIAL 217
Cdd:PTZ00265 640 LS-TIRYANTIFVL 652
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
139-235 |
2.52e-07 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 51.61 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 139 QSVDTLSGGQRQRawiaMVLAQE--------TaIMLLDEPTTWL---DISHqidLLELLSELnREKGYTLAAVLHDLNqA 207
Cdd:PRK00349 826 QPATTLSGGEAQR----VKLAKElskrstgkT-LYILDEPTTGLhfeDIRK---LLEVLHRL-VDKGNTVVVIEHNLD-V 895
|
90 100 110
....*....|....*....|....*....|....
gi 15829881 208 CRYASHLIAL------REGKIVAQGAPKEIVTAE 235
Cdd:PRK00349 896 IKTADWIIDLgpeggdGGGEIVATGTPEEVAKVE 929
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
24-222 |
2.84e-07 |
|
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: 49.35 E-value: 2.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKE-VARRIGLLAQNattlgditvqelv 102
Cdd:cd03215 17 RDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDaIRAGIAYVPED------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 103 argryphqplftrwRKEDeeavtkamqatGIthLADQSV-------DTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
Cdd:cd03215 84 --------------RKRE-----------GL--VLDLSVaenialsSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVD 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15829881 176 ISHQIDLLELLSELnREKGytlAAVL---HDLNQACRYASHLIALREGKI 222
Cdd:cd03215 137 VGAKAEIYRLIREL-ADAG---KAVLlisSELDELLGLCDRILVMYEGRI 182
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
38-210 |
3.70e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.89 E-value: 3.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 38 IIGPNGCGKSTLLRTLSRLMTPAHGHVWL-DGehiqhyaskevaRRIGLLAQNATTLGDITVQELVARGRYPHQPLFTRW 116
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGEARPaPG------------IKVGYLPQEPQLDPEKTVRENVEEGVAEVKAALDRF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 117 RK---------EDEEAVTKAM-------QATGITHL---------------ADQSVDTLSGGQRQRAWIAMVLAQETAIM 165
Cdd:PRK11819 106 NEiyaayaepdADFDALAAEQgelqeiiDAADAWDLdsqleiamdalrcppWDAKVTKLSGGERRRVALCRLLLEKPDML 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15829881 166 LLDEPTTWLDiSHQIDLLEllSELNREKGyTLAAVLHDlnqacRY 210
Cdd:PRK11819 186 LLDEPTNHLD-AESVAWLE--QFLHDYPG-TVVAVTHD-----RY 221
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
12-201 |
6.19e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 48.79 E-value: 6.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 12 QLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQhyasKEVA---RRIGLLAQ 88
Cdd:PRK13540 6 ELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK----KDLCtyqKQLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 89 NATTLGDITVQElvargryphQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168
Cdd:PRK13540 82 RSGINPYLTLRE---------NCLYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLD 152
|
170 180 190
....*....|....*....|....*....|....*
gi 15829881 169 EPTTWLDishQIDLLELLSEL--NREKGytlAAVL 201
Cdd:PRK13540 153 EPLVALD---ELSLLTIITKIqeHRAKG---GAVL 181
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
25-226 |
7.26e-07 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 48.79 E-value: 7.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 25 NLTVEIPDGHFTAIIGPNGCGKSTL----------LRTLSRLMTPAHghvwldgEHIQHYASKEVARRIGL-----LAQN 89
Cdd:cd03270 13 NVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqRRYVESLSAYAR-------QFLGQMDKPDVDSIEGLspaiaIDQK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 90 AT------TLGDITvqELVARGR--YPHQPLFTRWRkedeeavtkAMQATGITHLA-DQSVDTLSGGQRQRAWIAMVLAQ 160
Cdd:cd03270 86 TTsrnprsTVGTVT--EIYDYLRllFARVGIRERLG---------FLVDVGLGYLTlSRSAPTLSGGEAQRIRLATQIGS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15829881 161 ETA--IMLLDEPTTWLdisHQID---LLELLSELnREKGYTLAAVLHDLnQACRYASHLIAL------REGKIVAQG 226
Cdd:cd03270 155 GLTgvLYVLDEPSIGL---HPRDndrLIETLKRL-RDLGNTVLVVEHDE-DTIRAADHVIDIgpgagvHGGEIVAQG 226
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
38-235 |
8.39e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 49.97 E-value: 8.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 38 IIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTLGDiTVqelvargRYPHQPlftrWR 117
Cdd:PLN03232 1267 VVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSG-TV-------RFNIDP----FS 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 118 KEDEEAVTKAMQATGITHLADQSV-----------DTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIshQIDllELL 186
Cdd:PLN03232 1335 EHNDADLWEALERAHIKDVIDRNPfgldaevseggENFSVGQRQLLSLARALLRRSKILVLDEATASVDV--RTD--SLI 1410
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15829881 187 SELNRE--KGYTLAAVLHDLNQACRyASHLIALREGKIVAQGAPKEIVTAE 235
Cdd:PLN03232 1411 QRTIREefKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRD 1460
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
33-193 |
8.48e-07 |
|
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: 47.37 E-value: 8.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 33 GHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHV-WLDGEHIQHYASKEVarrigllaqnattlgditvqelvargryphqp 111
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGViYIDGEDILEEVLDQL-------------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 112 lftrwrkedeeavtkamqatgITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNR 191
Cdd:smart00382 50 ---------------------LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLL 108
|
..
gi 15829881 192 EK 193
Cdd:smart00382 109 LL 110
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
16-226 |
8.79e-07 |
|
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: 48.41 E-value: 8.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 16 GYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRlmtpahghvwldgeHIQHYASKEvarrigllaqNATTLGD 95
Cdd:cd03233 16 GRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALAN--------------RTEGNVSVE----------GDIHYNG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 96 ITVQElvARGRYPHQPLFTRwrKED--------EEAVTKAMQATGithlaDQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
Cdd:cd03233 72 IPYKE--FAEKYPGEIIYVS--EEDvhfptltvRETLDFALRCKG-----NEFVRGISGGERKRVSIAEALVSRASVLCW 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 168 DEPTTWLDISHQIDLLELLSELNRE-KGYTLAAVLHDLNQACRYASHLIALREGKIVAQG 226
Cdd:cd03233 143 DNSTRGLDSSTALEILKCIRTMADVlKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
138-235 |
1.06e-06 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 49.69 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 138 DQSVDTLSGG--QRQRawiamvLAQE-----TAIM-LLDEPTTWLdisHQID---LLELLSELnREKGYTLAAVLHDlNQ 206
Cdd:PRK00349 484 SRSAGTLSGGeaQRIR------LATQigsglTGVLyVLDEPSIGL---HQRDndrLIETLKHL-RDLGNTLIVVEHD-ED 552
|
90 100 110
....*....|....*....|....*....|....*
gi 15829881 207 ACRYASHLIAL------REGKIVAQGAPKEIVTAE 235
Cdd:PRK00349 553 TIRAADYIVDIgpgagvHGGEVVASGTPEEIMKNP 587
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
13-180 |
1.30e-06 |
|
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: 48.70 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 13 LTLGY--GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTpAHGHVWLDGEHIQHYASKEVARRIGLLAQNA 90
Cdd:cd03289 8 LTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 91 TTLGDITVQELVARGRYPHQPLftrWRKEDEEAVTKAM-QATGitHLADQSVD---TLSGGQRQRAWIAMVLAQETAIML 166
Cdd:cd03289 87 FIFSGTFRKNLDPYGKWSDEEI---WKVAEEVGLKSVIeQFPG--QLDFVLVDggcVLSHGHKQLMCLARSVLSKAKILL 161
|
170
....*....|....*
gi 15829881 167 LDEPTTWLD-ISHQI 180
Cdd:cd03289 162 LDEPSAHLDpITYQV 176
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
29-221 |
1.32e-06 |
|
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: 47.57 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 29 EIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGehiqhyaskevarrigllaqnattlgdITVQelvargryp 108
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG---------------------------ITPV--------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 109 HQPlftrwrkedeeavtkamqatgithladQSVDtLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSE 188
Cdd:cd03222 65 YKP---------------------------QYID-LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRR 116
|
170 180 190
....*....|....*....|....*....|...
gi 15829881 189 LNREKGYTLAAVLHDLNQAcRYASHLIALREGK 221
Cdd:cd03222 117 LSEEGKKTALVVEHDLAVL-DYLSDRIHVFEGE 148
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
117-233 |
2.89e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 47.81 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 117 RKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREkGYT 196
Cdd:NF000106 118 RKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GAT 196
|
90 100 110
....*....|....*....|....*....|....*..
gi 15829881 197 LAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVT 233
Cdd:NF000106 197 VLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKT 233
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
25-223 |
7.89e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 46.71 E-value: 7.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 25 NLTVEipDGHFTAIIGPNGCGKSTLLRTLSRLmtpaHGHVWLDGEhIqHYASKEV---------ARRIGLLAQNATTLGD 95
Cdd:NF040905 21 NLSVR--EGEIHALCGENGAGKSTLMKVLSGV----YPHGSYEGE-I-LFDGEVCrfkdirdseALGIVIIHQELALIPY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 96 ITVQELVARGRYPHQPLFTRWRKEDEEAvTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
Cdd:NF040905 93 LSIAENIFLGNERAKRGVIDWNETNRRA-RELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALN 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15829881 176 ISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIV 223
Cdd:NF040905 172 EEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRTI 218
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
24-194 |
8.20e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.65 E-value: 8.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQ-HYASKEVARRIGLLAQNATTLG-----DIT 97
Cdd:PRK10982 265 RDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINnHNANEAINHGFALVTEERRSTGiyaylDIG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 98 VQELVARGRYPHQP---LFTRWRKEDEEAVTKAMQATGITHlaDQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
Cdd:PRK10982 345 FNSLISNIRNYKNKvglLDNSRMKSDTQWVIDSMRVKTPGH--RTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGI 422
|
170 180
....*....|....*....|.
gi 15829881 175 DISHQIDLLELLSEL-NREKG 194
Cdd:PRK10982 423 DVGAKFEIYQLIAELaKKDKG 443
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
17-175 |
8.62e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.55 E-value: 8.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLrtlsRLMTpahghvwldGEHIQHYASKEV--ARRIGllaqNATTLG 94
Cdd:PRK10938 270 YNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLL----SLIT---------GDHPQGYSNDLTlfGRRRG----SGETIW 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 95 DI-------------------TVQELVARGRYP----HQPLFTRWRKedeeavtKAMQATGITHL----ADQSVDTLSGG 147
Cdd:PRK10938 333 DIkkhigyvssslhldyrvstSVRNVILSGFFDsigiYQAVSDRQQK-------LAQQWLDILGIdkrtADAPFHSLSWG 405
|
170 180
....*....|....*....|....*...
gi 15829881 148 QRQRAWIAMVLAQETAIMLLDEPTTWLD 175
Cdd:PRK10938 406 QQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
22-184 |
8.68e-06 |
|
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: 46.83 E-value: 8.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHvwldgehIQHyaskevARRIGLLAQNATTLGDiTVQEL 101
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGK-------IKH------SGRISFSPQTSWIMPG-TIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 102 VARGRYPHQPLFTRWRK--EDEEAVTKAMQATGIThLADQSVdTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQ 179
Cdd:TIGR01271 507 IIFGLSYDEYRYTSVIKacQLEEDIALFPEKDKTV-LGEGGI-TLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTE 584
|
....*
gi 15829881 180 IDLLE 184
Cdd:TIGR01271 585 KEIFE 589
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
15-184 |
9.44e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.48 E-value: 9.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 15 LGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSrlmtpahGHVWLDGEHIQHYASKEVARriglLAQNATTLG 94
Cdd:PRK11147 11 LSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILN-------GEVLLDDGRIIYEQDLIVAR----LQQDPPRNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 95 DITVQELVARG---------RYpHQPLFTRWRKEDEEAVTKAMQATG-ITHL-------------------ADQSVDTLS 145
Cdd:PRK11147 80 EGTVYDFVAEGieeqaeylkRY-HDISHLVETDPSEKNLNELAKLQEqLDHHnlwqlenrinevlaqlgldPDAALSSLS 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 15829881 146 GGQRQRAWIAMVLAQETAIMLLDEPTTWLDIShQIDLLE 184
Cdd:PRK11147 159 GGWLRKAALGRALVSNPDVLLLDEPTNHLDIE-TIEWLE 196
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-235 |
9.61e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 46.65 E-value: 9.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQnATTLGDITVqel 101
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQ-APVLFSGTV--- 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 102 vargRYPHQPlFTRWRKED-EEAVTKAmqatgitHLAD--------------QSVDTLSGGQRQRAWIAMVLAQETAIML 166
Cdd:PLN03130 1330 ----RFNLDP-FNEHNDADlWESLERA-------HLKDvirrnslgldaevsEAGENFSVGQRQLLSLARALLRRSKILV 1397
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15829881 167 LDEPTTWLDISHQIdlleLLSELNRE--KGYTLAAVLHDLNQA--CryaSHLIALREGKIVAQGAPKEIVTAE 235
Cdd:PLN03130 1398 LDEATAAVDVRTDA----LIQKTIREefKSCTMLIIAHRLNTIidC---DRILVLDAGRVVEFDTPENLLSNE 1463
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
24-193 |
1.26e-05 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 45.76 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 24 ENLTVEIPDGhFTAIIGPNGCGKSTLLRTLSRLMTPAHG--------HVWLDGEHI----------------QHYASKEV 79
Cdd:COG3593 15 KDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSrkfdeedfYLGDDPDLPeieieltfgsllsrllRLLLKEED 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 80 ARRIGLLAQNATT-----LGDIT--VQELVARGRYPHQP--LFTRWRKEDEEAVTKAMQATGITHLADQSvdtlsgGQRQ 150
Cdd:COG3593 94 KEELEEALEELNEelkeaLKALNelLSEYLKELLDGLDLelELSLDELEDLLKSLSLRIEDGKELPLDRL------GSGF 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15829881 151 RAWIAMVLAQETA---------IMLLDEPTTWLDISHQIDLLELLSELNREK 193
Cdd:COG3593 168 QRLILLALLSALAelkrapanpILLIEEPEAHLHPQAQRRLLKLLKELSEKP 219
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
25-231 |
1.41e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.12 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGhvwldgehiqhyASKEVARRIGLLAQ-----NATTLGDITVQ 99
Cdd:PLN03232 635 DINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAET------------SSVVIRGSVAYVPQvswifNATVRENILFG 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 100 ELVARGRYphqplftrWRKEDEEAVTKAMQ---ATGITHLADQSVDtLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD- 175
Cdd:PLN03232 703 SDFESERY--------WRAIDVTALQHDLDllpGRDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDa 773
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15829881 176 -ISHQIDLLELLSELNREKGYTLAAVLHDLNQACRyashLIALREGKIVAQGAPKEI 231
Cdd:PLN03232 774 hVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDR----IILVSEGMIKEEGTFAEL 826
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
138-235 |
2.08e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 45.40 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 138 DQSVDTLSGG--QRQRawiamvLAqeTAI------ML--LDEPTTWLdisHQID---LLELLSELnREKGYTLAAVLHDL 204
Cdd:COG0178 480 DRSAGTLSGGeaQRIR------LA--TQIgsglvgVLyvLDEPSIGL---HQRDndrLIETLKRL-RDLGNTVIVVEHDE 547
|
90 100 110
....*....|....*....|....*....|....*..
gi 15829881 205 nQACRYASHLIAL------REGKIVAQGAPKEIVTAE 235
Cdd:COG0178 548 -DTIRAADYIIDIgpgageHGGEVVAQGTPEEILKNP 583
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
27-61 |
2.18e-05 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 41.43 E-value: 2.18e-05
10 20 30
....*....|....*....|....*....|....*
gi 15829881 27 TVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAH 61
Cdd:pfam13555 16 TIPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVPAK 50
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
23-47 |
2.38e-05 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 43.99 E-value: 2.38e-05
10 20
....*....|....*....|....*
gi 15829881 23 AENLTVEIPDGhFTAIIGPNGCGKS 47
Cdd:cd03278 13 ADKTTIPFPPG-LTAIVGPNGSGKS 36
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
24-59 |
2.52e-05 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 44.60 E-value: 2.52e-05
10 20 30
....*....|....*....|....*....|....*..
gi 15829881 24 ENLTVEIP-DGHFTAIIGPNGCGKSTLLRTLSRLMTP 59
Cdd:COG3950 15 EDLEIDFDnPPRLTVLVGENGSGKTTLLEAIALALSG 51
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
33-175 |
4.45e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.84 E-value: 4.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 33 GHFTAIIGPNGCGKSTLLRTLSRLMTPAhghvWLDGE-HIQHYASKE--VARRIGLLAQNATTLGDITVQE-LVARGryp 108
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGRKTGG----YIEGDiRISGFPKKQetFARISGYCEQNDIHSPQVTVREsLIYSA--- 978
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15829881 109 hqplFTRWRKE--DEEA---VTKAMQATGITHLADQ-----SVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
Cdd:PLN03140 979 ----FLRLPKEvsKEEKmmfVDEVMELVELDNLKDAivglpGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
38-232 |
6.19e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 44.38 E-value: 6.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 38 IIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNAtTLGDITVQELVargryphQPLFtrwr 117
Cdd:PTZ00243 1341 IVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDP-VLFDGTVRQNV-------DPFL---- 1408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 118 KEDEEAVTKAMQATGI-THLADQS--VDT--------LSGGQRQRAWIA-MVLAQETAIMLLDEPTTwlDISHQIDLLEL 185
Cdd:PTZ00243 1409 EASSAEVWAALELVGLrERVASESegIDSrvleggsnYSVGQRQLMCMArALLKKGSGFILMDEATA--NIDPALDRQIQ 1486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15829881 186 LSELNREKGYTLAAVLHDLNQACRYaSHLIALREGKIVAQGAPKEIV 232
Cdd:PTZ00243 1487 ATVMSAFSAYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPRELV 1532
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
27-50 |
6.54e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 44.19 E-value: 6.54e-05
10 20
....*....|....*....|....*
gi 15829881 27 TVEIP-DGHFTAIIGPNGCGKSTLL 50
Cdd:pfam02463 16 TVILPfSPGFTAIVGPNGSGKSNIL 40
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
24-203 |
6.75e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.01 E-value: 6.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvarrigllaqnaTTLGDITVQELVA 103
Cdd:PRK10636 18 DNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQE------------TPALPQPALEYVI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 104 RG----RYPHQPLFTRWRKEDEEAVT------KAMQATGITHLA--------------DQSVDTLSGGQRQRAWIAMVLA 159
Cdd:PRK10636 86 DGdreyRQLEAQLHDANERNDGHAIAtihgklDAIDAWTIRSRAasllhglgfsneqlERPVSDFSGGWRMRLNLAQALI 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15829881 160 QETAIMLLDEPTTWLDISHQIDLLELLselnreKGY--TLAAVLHD 203
Cdd:PRK10636 166 CRSDLLLLDEPTNHLDLDAVIWLEKWL------KSYqgTLILISHD 205
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
11-189 |
7.45e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 42.69 E-value: 7.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 11 EQLTL-GYGKYtvAENLTVEIPDGhFTAIIGPNGCGKSTLL---------------RTLSRLMTP--AHGHVWLDGEHI- 71
Cdd:COG0419 3 LRLRLeNFRSY--RDTETIDFDDG-LNLIVGPNGAGKSTILeairyalygkarsrsKLRSDLINVgsEEASVELEFEHGg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 72 QHYaskEVARRIG----LLAQNATTLGDItVQELVARGRYphQPLFTRWRKEDEEAVTKAMQATGITHLADQ-------- 139
Cdd:COG0419 80 KRY---RIERRQGefaeFLEAKPSERKEA-LKRLLGLEIY--EELKERLKELEEALESALEELAELQKLKQEilaqlsgl 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15829881 140 -SVDTLSGGQRQRAWIAMVLAqetaiMLLDepTTWLDISHQIDLLELLSEL 189
Cdd:COG0419 154 dPIETLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEEL 197
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
21-188 |
7.61e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 42.86 E-value: 7.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLS--RLMTPAHGHVWLDGEHIQHYASKEVARRIGLLA-QNATTLGDIT 97
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPEDRAGEGIFMAfQYPVEIPGVS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 98 VQ-----ELVARGRYPHQPLFTRWRKED---EEAVTKAMQATGIThladQSVDT-LSGGQRQRAWIAMVLAQETAIMLLD 168
Cdd:PRK09580 95 NQfflqtALNAVRSYRGQEPLDRFDFQDlmeEKIALLKMPEDLLT----RSVNVgFSGGEKKRNDILQMAVLEPELCILD 170
|
170 180
....*....|....*....|
gi 15829881 169 EPTTWLDishqIDLLELLSE 188
Cdd:PRK09580 171 ESDSGLD----IDALKIVAD 186
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
24-224 |
9.02e-05 |
|
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: 43.27 E-value: 9.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAH-GHVWLDGEHIQ-HYASKEVARRIGLLAQNATTLGDITVQEL 101
Cdd:TIGR02633 277 DDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKFeGNVFINGKPVDiRNPAQAIRAGIAMVPEDRKRHGIVPILGV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 102 VARGRYPHQPLFTRWRKEDEEAVTKAMQAtGITHLA------DQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
Cdd:TIGR02633 357 GKNITLSVLKSFCFKMRIDAAAELQIIGS-AIQRLKvktaspFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15829881 176 ISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVA 224
Cdd:TIGR02633 436 VGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLKG 483
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
23-47 |
9.34e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 9.34e-05
10 20
....*....|....*....|....*
gi 15829881 23 AENLTVEIPDGhFTAIIGPNGCGKS 47
Cdd:COG1196 15 ADPTTIPFEPG-ITAIVGPNGSGKS 38
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
143-235 |
1.05e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.48 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 143 TLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRyaSHLIAL----- 217
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR--SDKIVVfnnpd 1435
|
90
....*....|....*....
gi 15829881 218 REGKIV-AQGAPKEIVTAE 235
Cdd:PTZ00265 1436 RTGSFVqAHGTHEELLSVQ 1454
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
132-230 |
1.81e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 132 GITHLA-DQSVDTLSGGQRQRAWIAMVLAQE-TAIM-LLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDlNQAC 208
Cdd:PRK00635 464 GLPYLTpERALATLSGGEQERTALAKHLGAElIGITyILDEPSIGLHPQDTHKLINVIKKL-RDQGNTVLLVEHD-EQMI 541
|
90 100
....*....|....*....|....*...
gi 15829881 209 RYASHLI------ALREGKIVAQGAPKE 230
Cdd:PRK00635 542 SLADRIIdigpgaGIFGGEVLFNGSPRE 569
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
35-56 |
2.72e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 41.61 E-value: 2.72e-04
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
7-242 |
4.61e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 41.14 E-value: 4.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 7 RLRGEQLTlGYGkytvAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQH------------Y 74
Cdd:PRK10762 257 RLKVDNLS-GPG----VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTrspqdglangivY 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 75 ASkEVARRIGLLaqnattLGdITVQE---LVARGRYPHQPLFTRwRKEDEEAVTKAMQATGI-THLADQSVDTLSGGQRQ 150
Cdd:PRK10762 332 IS-EDRKRDGLV------LG-MSVKEnmsLTALRYFSRAGGSLK-HADEQQAVSDFIRLFNIkTPSMEQAIGLLSGGNQQ 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 151 RAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIV----AQG 226
Cdd:PRK10762 403 KVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRISgeftREQ 481
|
250
....*....|....*.
gi 15829881 227 APKEIVTAELIERIYG 242
Cdd:PRK10762 482 ATQEKLMAAAVGKLNR 497
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
13-50 |
4.75e-04 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 40.17 E-value: 4.75e-04
10 20 30
....*....|....*....|....*....|....*....
gi 15829881 13 LTL-GYGKYtvaENLTVEiPDGHFTAIIGPNGCGKSTLL 50
Cdd:pfam13476 1 LTIeNFRSF---RDQTID-FSKGLTLITGPNGSGKTTIL 35
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
135-237 |
4.85e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 41.31 E-value: 4.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 135 HLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNrEKGYTLAAVLHDLNQACRYASHL 214
Cdd:PRK09700 401 HSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLA-DDGKVILMVSSELPEIITVCDRI 479
|
90 100
....*....|....*....|...
gi 15829881 215 IALREGKIVAQGAPKEIVTAELI 237
Cdd:PRK09700 480 AVFCEGRLTQILTNRDDMSEEEI 502
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
24-56 |
5.00e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 41.07 E-value: 5.00e-04
10 20 30
....*....|....*....|....*....|...
gi 15829881 24 ENLTVEIPDghFTAIIGPNGCGKSTLLRTLSRL 56
Cdd:COG4637 14 RDLELPLGP--LTVLIGANGSGKSNLLDALRFL 44
|
|
| BMS1 |
COG5192 |
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ... |
29-58 |
1.22e-03 |
|
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227519 [Multi-domain] Cd Length: 1077 Bit Score: 40.11 E-value: 1.22e-03
10 20 30
....*....|....*....|....*....|
gi 15829881 29 EIPDGHFTAIIGPNGCGKSTLLRTLSRLMT 58
Cdd:COG5192 65 DLPPPFIVAVVGPPGTGKSTLIRSLVRRFT 94
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-201 |
1.65e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 38.85 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 1 MTESVARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRlmTPAH----GHVWLDGEHIQHYAS 76
Cdd:CHL00131 1 MNKNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAYkileGDILFKGESILDLEP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 77 KEVARR-IGLLAQNATTLGDITVQELV---------ARGRYPHQPL-FTRWRKEDEEAVtkAMQATGITHLADqsvDTLS 145
Cdd:CHL00131 79 EERAHLgIFLAFQYPIEIPGVSNADFLrlaynskrkFQGLPELDPLeFLEIINEKLKLV--GMDPSFLSRNVN---EGFS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15829881 146 GGQRQRAWIAMVLAQETAIMLLDEPTTWLDishqIDLLELLSE-LNREKGYTLAAVL 201
Cdd:CHL00131 154 GGEKKRNEILQMALLDSELAILDETDSGLD----IDALKIIAEgINKLMTSENSIIL 206
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
31-61 |
2.98e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 38.74 E-value: 2.98e-03
10 20 30
....*....|....*....|....*....|.
gi 15829881 31 PDGHFTAIIGPNGCGKSTLLRTLSRLMTPAH 61
Cdd:COG4913 22 FDGRGTLLTGDNGSGKSTLLDAIQTLLVPAK 52
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
113-192 |
4.14e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 38.37 E-value: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829881 113 FTRWRKEDEEAVTKAMQaTGITHL------ADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELL 186
Cdd:PRK13549 370 FTGGSRIDDAAELKTIL-ESIQRLkvktasPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLI 448
|
....*.
gi 15829881 187 SELNRE 192
Cdd:PRK13549 449 NQLVQQ 454
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
35-54 |
5.45e-03 |
|
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213242 [Multi-domain] Cd Length: 247 Bit Score: 37.55 E-value: 5.45e-03
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| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
23-47 |
8.52e-03 |
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chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 37.34 E-value: 8.52e-03
10 20
....*....|....*....|....*
gi 15829881 23 AENLTVEIPDGhFTAIIGPNGCGKS 47
Cdd:TIGR02168 14 ADPTTINFDKG-ITGIVGPNGCGKS 37
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