|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1-264 |
0e+00 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 539.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 1 MTAVTSRLRGDQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVA 80
Cdd:PRK10253 1 MTESVARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 81 KRIGLLAQNATTPGDITVQELVARGRYPHQPLFTRWRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQ 160
Cdd:PRK10253 81 RRIGLLAQNATTPGDITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 161 ETAIMLLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVSAELIEKI 240
Cdd:PRK10253 161 ETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERI 240
|
250 260
....*....|....*....|....
gi 490237141 241 YGLRCTIIEDPVAHTPLVVPLGRR 264
Cdd:PRK10253 241 YGLRCMIIDDPVAGTPLVVPLGRT 264
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
7-260 |
8.52e-139 |
|
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: 390.56 E-value: 8.52e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 7 RLRGDQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIGLL 86
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 87 AQNATTPGDITVQELVARGRYPHQPLFTRWRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIML 166
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGRYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 167 LDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVSAELIEKIYGLRCT 246
Cdd:COG1120 161 LDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVYGVEAR 240
|
250
....*....|....
gi 490237141 247 IIEDPVAHTPLVVP 260
Cdd:COG1120 241 VIEDPVTGRPLVLP 254
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
8-259 |
9.61e-117 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 334.67 E-value: 9.61e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 8 LRGDQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIGLLA 87
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 88 QNATTPGDITVQELVARGRYPHQPLFTRWRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
Cdd:PRK11231 83 QHHLTPEGITVRELVAYGRSPWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 168 DEPTTWLDISHQIDLLELLSELNQQkGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVSAELIEKIYGLRCTI 247
Cdd:PRK11231 163 DEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVFDVEAEI 241
|
250
....*....|..
gi 490237141 248 IEDPVAHTPLVV 259
Cdd:PRK11231 242 HPEPVSGTPMCV 253
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
11-260 |
4.52e-89 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 264.25 E-value: 4.52e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 11 DQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIGLLAQNA 90
Cdd:COG4604 5 KNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQEN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 91 TTPGDITVQELVARGRYPHqplfTRWR--KEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168
Cdd:COG4604 85 HINSRLTVRELVAFGRFPY----SKGRltAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 169 EPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVSAELIEKIYGLRCTII 248
Cdd:COG4604 161 EPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEVLSDIYDTDIEVE 240
|
250
....*....|..
gi 490237141 249 EdpVAHTPLVVP 260
Cdd:COG4604 241 E--IDGKRICVY 250
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
8-260 |
4.84e-84 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 251.96 E-value: 4.84e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 8 LRGDQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIGLLA 87
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 88 QNATTPGDITVQELVARGRYPHQplftRWRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQ------- 160
Cdd:COG4559 82 QHSSLAFPFTVEEVVALGRAPHG----SSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQlwepvdg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 161 ETAIMLLDEPTTWLDISHQIDLLELLSELNQQkGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVSAELIEKI 240
Cdd:COG4559 158 GPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELLERV 236
|
250 260
....*....|....*....|
gi 490237141 241 YGLRCTIIEDPVAHTPLVVP 260
Cdd:COG4559 237 YGADLRVLAHPEGGCPQVLP 256
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
8-260 |
3.17e-83 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 249.69 E-value: 3.17e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 8 LRGDQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIGLLA 87
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 88 QNATTPGDITVQELVARGRYPHqplfTRWRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQ------E 161
Cdd:PRK13548 83 QHSSLSFPFTVEEVVAMGRAPH----GLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepdgP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 162 TAIMLLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVSAELIEKIY 241
Cdd:PRK13548 159 PRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPETLRRVY 238
|
250
....*....|....*....
gi 490237141 242 GLRCTIIEDPVAHTPLVVP 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 |
1.17e-82 |
|
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: 245.42 E-value: 1.17e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 11 DQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIGLLAQna 90
Cdd:cd03214 3 ENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 91 ttpgditvqelvargryphqplftrwrkedeeavsrAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
Cdd:cd03214 81 ------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490237141 171 TTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEG 226
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
11-257 |
2.35e-77 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 235.07 E-value: 2.35e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 11 DQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIGLLAQNA 90
Cdd:PRK10575 15 RNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 91 TTPGDITVQELVARGRYPHQPLFTRWRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
Cdd:PRK10575 95 PAAEGMTVRELVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 171 TTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVSAELIEKIYGLRCTIIED 250
Cdd:PRK10575 175 TSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIYGIPMGILPH 254
|
....*..
gi 490237141 251 PVAHTPL 257
Cdd:PRK10575 255 PAGAAPV 261
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
11-244 |
7.00e-77 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 233.06 E-value: 7.00e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 11 DQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRyaskeVAKRIGLLAQNA 90
Cdd:COG1121 10 ENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRRIGYVPQRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 91 TTPGD--ITVQELVARGRYPHQPLFTRWRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168
Cdd:COG1121 85 EVDWDfpITVRDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLD 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490237141 169 EPTTWLDISHQIDLLELLSELNQQkGYTLAAVLHDLNQACRYATHLIALREGkIVAEGAPKEIVSAELIEKIYGLR 244
Cdd:COG1121 165 EPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVLTPENLSRAYGGP 238
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
13-261 |
1.02e-66 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 212.39 E-value: 1.02e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 13 LTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIGLLAQNATT 92
Cdd:PRK09536 9 LSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 93 PGDITVQELVARGRYPHQPLFTRWRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
Cdd:PRK09536 89 SFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 173 WLDISHQIDLLELLSELnQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVSAELIEKIYGLRCTIIEDPV 252
Cdd:PRK09536 169 SLDINHQVRTLELVRRL-VDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFDARTAVGTDPA 247
|
....*....
gi 490237141 253 AHTPLVVPL 261
Cdd:PRK09536 248 TGAPTVTPL 256
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
11-226 |
3.76e-66 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 204.69 E-value: 3.76e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 11 DQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRyaskeVAKRIGLLAQNA 90
Cdd:cd03235 3 EDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK-----ERKRIGYVPQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 91 TTPGD--ITVQELVARGRYPHQPLFTRWRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168
Cdd:cd03235 78 SIDRDfpISVRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490237141 169 EPTTWLDISHQIDLLELLSELNqQKGYTLAAVLHDLNQACRYATHLIALrEGKIVAEG 226
Cdd:cd03235 158 EPFAGVDPKTQEDIYELLRELR-REGMTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
8-242 |
1.19e-62 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 196.82 E-value: 1.19e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 8 LRGDQLTLAYGKKTIA-ESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAK---RI 83
Cdd:COG3638 3 LELRNLSKRYPGGTPAlDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRlrrRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 84 GLLAQNATTPGDITVQELVARGRYPHQP----LFTRWRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLA 159
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNVLAGRLGRTStwrsLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARALV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 160 QETAIMLLDEPTTWLD--ISHQIdlLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEiVSAELI 237
Cdd:COG3638 163 QEPKLILADEPVASLDpkTARQV--MDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAE-LTDAVL 239
|
....*
gi 490237141 238 EKIYG 242
Cdd:COG3638 240 REIYG 244
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
11-239 |
5.47e-62 |
|
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: 194.47 E-value: 5.47e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 11 DQLTLAYGKKTIA-ESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIGLLAQN 89
Cdd:COG1122 4 ENLSFSYPGGTPAlDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLVFQN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 90 attPGD----ITVQELVARGryphqPLFTRWRKED-EEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAI 164
Cdd:COG1122 84 ---PDDqlfaPTVEEDVAFG-----PENLGLPREEiRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490237141 165 MLLDEPTTWLDISHQIDLLELLSELNQQkGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVS-AELIEK 239
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSdYELLEE 230
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
8-241 |
1.13e-58 |
|
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: 186.62 E-value: 1.13e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 8 LRGDQLTLAYGKKTIA-ESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQI---QRYASKEVAKRI 83
Cdd:cd03256 1 IEVENLSKTYPNGKKAlKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 84 GLLAQNATTPGDITVQELVARGRYPH----QPLFTRWRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLA 159
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRLGRrstwRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 160 QETAIMLLDEPTTWLD--ISHQIdlLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIvSAELI 237
Cdd:cd03256 161 QQPKLILADEPVASLDpaSSRQV--MDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL-TDEVL 237
|
....
gi 490237141 238 EKIY 241
Cdd:cd03256 238 DEIY 241
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
8-242 |
5.49e-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: 179.80 E-value: 5.49e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 8 LRGDQLTLAYGK-KTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKE---VAKRI 83
Cdd:TIGR02315 2 LEVENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrkLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 84 GLLAQNATTPGDITVQELVARGRYPHQP----LFTRWRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLA 159
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVLHGRLGYKPtwrsLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 160 QETAIMLLDEPTTWLD--ISHQIdlLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIvSAELI 237
Cdd:TIGR02315 162 QQPDLILADEPIASLDpkTSKQV--MDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL-DDEVL 238
|
....*
gi 490237141 238 EKIYG 242
Cdd:TIGR02315 239 RHIYG 243
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
11-241 |
6.75e-53 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 171.40 E-value: 6.75e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 11 DQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRyASKEVAKRIGLLAQNA 90
Cdd:COG1131 4 RGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGYVPQEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 91 TTPGDITVQELVargRYpHQPLFTRWRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
Cdd:COG1131 83 ALYPDLTVRENL---RF-FARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490237141 171 TTWLDISHQIDLLELLSELNQQKgytlAAVL---HDLNQACRYATHLIALREGKIVAEGAPKEIVSAELiEKIY 241
Cdd:COG1131 159 TSGLDPEARRELWELLRELAAEG----KTVLlstHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLL-EDVF 227
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
11-221 |
3.01e-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: 166.49 E-value: 3.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 11 DQLTLAYGKKTIA--ESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIGLLAQ 88
Cdd:cd03225 3 KNLSFSYPDGARPalDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 89 NA----TTPgdiTVQELVARG-RYPHQPlftrwRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETA 163
Cdd:cd03225 83 NPddqfFGP---TVEEEVAFGlENLGLP-----EEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490237141 164 IMLLDEPTTWLDISHQIDLLELLSELNQQkGYTLAAVLHDLNQACRYATHLIALREGK 221
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
8-222 |
1.41e-47 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 156.90 E-value: 1.41e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 8 LRGDQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIGLLA 87
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 88 QNATTPGDiTVQELVARgryphqPLFTRWRKEDEEAVSRAMKATGIT-DLARQSVDTLSGGQRQRAWIAMVLAQETAIML 166
Cdd:COG4619 81 QEPALWGG-TVRDNLPF------PFQLRERKFDRERALELLERLGLPpDILDKPVERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490237141 167 LDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKI 222
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
8-233 |
2.34e-47 |
|
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: 157.21 E-value: 2.34e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 8 LRGDQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKR-IGLL 86
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 87 AQNATTPGDITVQE---LVARGRYPHQPLFTRWRKEDEEAVSRAM---KATGITDLARQSVDTLSGGQRQRAWIAMVLAQ 160
Cdd:cd03219 81 FQIPRLFPELTVLEnvmVAAQARTGSGLLLARARREEREARERAEellERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490237141 161 ETAIMLLDEPTTWLDISHQIDLLELLSELNQQkGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVS 233
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
11-240 |
3.73e-47 |
|
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: 158.00 E-value: 3.73e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 11 DQLTLAYGKKTIAES-----LNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQI---QRYASKEVAKR 82
Cdd:TIGR04521 4 KNVSYIYQPGTPFEKkalddVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDItakKKKKLKDLRKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 83 IGLLAQN------ATTpgditVQELVARGryPHQplFTRWRKEDEEAVSRAMKATGIT-DLARQSVDTLSGGQRQRAWIA 155
Cdd:TIGR04521 84 VGLVFQFpehqlfEET-----VYKDIAFG--PKN--LGLSEEEAEERVKEALELVGLDeEYLERSPFELSGGQMRRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 156 MVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVS-A 234
Cdd:TIGR04521 155 GVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSdV 234
|
....*.
gi 490237141 235 ELIEKI 240
Cdd:TIGR04521 235 DELEKI 240
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
8-226 |
6.19e-47 |
|
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: 155.37 E-value: 6.19e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 8 LRGDQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIqryASKEVAKR-IGLL 86
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV---TGVPPERRnIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 87 AQNATTPGDITVQELVARGRYPHqplftRWRKEDEEA-VSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIM 165
Cdd:cd03259 78 FQDYALFPHLTVAENIAFGLKLR-----GVPKAEIRArVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490237141 166 LLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEG 226
Cdd:cd03259 153 LLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
8-260 |
1.72e-46 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 156.53 E-value: 1.72e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 8 LRGDQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPA--------SGHVYLDGEQIQRYASKEV 79
Cdd:PRK13547 2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 80 AKRIGLLAQNATTPGDITVQELVARGRYPHQPLFTRWRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLA 159
Cdd:PRK13547 82 ARLRAVLPQAAQPAFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 160 Q---------ETAIMLLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKE 230
Cdd:PRK13547 162 QlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPAD 241
|
250 260 270
....*....|....*....|....*....|
gi 490237141 231 IVSAELIEKIYGLRCTIIEDPVAHTPLVVP 260
Cdd:PRK13547 242 VLTPAHIARCYGFAVRLVDAGDGVPPVIVP 271
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
7-231 |
6.23e-46 |
|
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: 153.98 E-value: 6.23e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 7 RLRGdqLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKE---VAKRI 83
Cdd:COG1127 7 EVRN--LTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyeLRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 84 GLLAQNATTPGDITVQELVArgryphQPL--FTRW-RKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQ 160
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVA------FPLreHTDLsEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490237141 161 ETAIMLLDEPTTWLDI--SHQIDllELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEI 231
Cdd:COG1127 159 DPEILLYDEPTAGLDPitSAVID--ELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL 229
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
11-231 |
6.38e-46 |
|
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: 153.86 E-value: 6.38e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 11 DQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYaSKEVAKRIGLLAQNA 90
Cdd:COG4555 5 ENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKE-PREARRQIGVLPDER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 91 TTPGDITVQELVargRYpHQPLFTRWRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
Cdd:COG4555 84 GLYDRLTVRENI---RY-FAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490237141 171 TTWLDISHQIDLLELLSELNQQKGytlaAVL---HDLNQACRYATHLIALREGKIVAEGAPKEI 231
Cdd:COG4555 160 TNGLDVMARRLLREILRALKKEGK----TVLfssHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
7-231 |
7.76e-46 |
|
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: 153.43 E-value: 7.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 7 RLRGdqLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKE---VAKRI 83
Cdd:cd03261 2 ELRG--LTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 84 GLLAQNATTPGDITVQELVArgrYPHQPLFTRWRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETA 163
Cdd:cd03261 80 GMLFQSGALFDSLTVFENVA---FPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 164 IMLLDEPTTWLD--ISHQIDllELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEI 231
Cdd:cd03261 157 LLLYDEPTAGLDpiASGVID--DLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-234 |
4.48e-45 |
|
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: 158.53 E-value: 4.48e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 1 MTAVtsrLRGDQLTLAY--GKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPA---SGHVYLDGEQIQRYA 75
Cdd:COG1123 1 MTPL---LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 76 SKEVAKRIGLLAQNATTPGD-ITVQELVARGRYphqpLFTRWRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWI 154
Cdd:COG1123 78 EALRGRRIGMVFQDPMTQLNpVTVGDQIAEALE----NLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 155 AMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVSA 234
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
8-231 |
1.19e-44 |
|
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: 157.37 E-value: 1.19e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 8 LRGDQLTLAY-----GKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRY---ASKEV 79
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLsrrSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 80 AKRIGLLAQNATT---PGDiTVQELVARGRYPHQPLftrWRKEDEEAVSRAMKATGI-TDLARQSVDTLSGGQRQRAWIA 155
Cdd:COG1123 341 RRRVQMVFQDPYSslnPRM-TVGDIIAEPLRLHGLL---SRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIA 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490237141 156 MVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEI 231
Cdd:COG1123 417 RALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEV 492
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
8-234 |
1.19e-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: 150.72 E-value: 1.19e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 8 LRGDQLTLAYGKK----TIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRI 83
Cdd:COG1124 2 LEVRNLSVSYGQGgrrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 84 GLLAQNATT---PGdITVQELVArgryphQPLFTRWRKEDEEAVSRAMKATGIT-DLARQSVDTLSGGQRQRAWIAMVLA 159
Cdd:COG1124 82 QMVFQDPYAslhPR-HTVDRILA------EPLRIHGLPDREERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490237141 160 QETAIMLLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVSA 234
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAG 229
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
7-231 |
6.60e-44 |
|
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: 148.10 E-value: 6.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 7 RLRGdqLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRL-----MTPASGHVYLDGEQI--QRYASKEV 79
Cdd:cd03260 2 ELRD--LNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIydLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 80 AKRIGLLAQNAtTPGDITVQELVARGRYPHQplfTRWRKEDEEAVSRAMKATGITDLA--RQSVDTLSGGQRQRAWIAMV 157
Cdd:cd03260 80 RRRVGMVFQKP-NPFPGSIYDNVAYGLRLHG---IKLKEELDERVEEALRKAALWDEVkdRLHALGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490237141 158 LAQETAIMLLDEPTTWLDISHQIDLLELLSELNQQkgYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEI 231
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
14-250 |
4.11e-43 |
|
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: 146.77 E-value: 4.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 14 TLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASG-HVYLDGEQIQRYASKEVAKRIGLL--AQNA 90
Cdd:COG1119 10 TVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRIGLVspALQL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 91 TTPGDITVQELVARGRYPHqplFTRWRKEDEEAVSRA---MKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
Cdd:COG1119 90 RFPRDETVLDVVLSGFFDS---IGLYREPTDEQRERArelLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLIL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 168 DEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVSAELIEKIYGLRCTI 247
Cdd:COG1119 167 DEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLTSENLSEAFGLPVEV 246
|
...
gi 490237141 248 IED 250
Cdd:COG1119 247 ERR 249
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
16-217 |
6.59e-43 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 144.68 E-value: 6.59e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 16 AYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGeqiqryaskevAKRIGLLAQNATTPGD 95
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRSEVPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 96 --ITVQELVARGRYPHQPLFTRWRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
Cdd:NF040873 70 lpLTVRDLVAMGRWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490237141 174 LDISHQIDLLELLSELNQQkGYTLAAVLHDLNQAcRYATHLIAL 217
Cdd:NF040873 150 LDAESRERIIALLAEEHAR-GATVVVVTHDLELV-RRADPCVLL 191
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
13-240 |
5.02e-42 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 144.75 E-value: 5.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 13 LTLAYG--KKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIGLLAQNa 90
Cdd:PRK13632 13 VSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIFQN- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 91 ttPGD----ITVQELVARG----RYPhqplftrwRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQET 162
Cdd:PRK13632 92 --PDNqfigATVEDDIAFGlenkKVP--------PKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490237141 163 AIMLLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRyATHLIALREGKIVAEGAPKEIV-SAELIEKI 240
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILnNKEILEKA 239
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
8-233 |
5.76e-42 |
|
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: 144.03 E-value: 5.76e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 8 LRGDQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRiGlLA 87
Cdd:COG0411 5 LEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARL-G-IA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 88 ---QNATTPGDITVQE--LVARGRYPHQPLFT------RWRKEDEEAVSRAM---KATGITDLARQSVDTLSGGQRQRAW 153
Cdd:COG0411 83 rtfQNPRLFPELTVLEnvLVAAHARLGRGLLAallrlpRARREEREARERAEellERVGLADRADEPAGNLSYGQQRRLE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 154 IAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVS 233
Cdd:COG0411 163 IARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVRA 242
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
26-250 |
1.50e-41 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 142.67 E-value: 1.50e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 26 LNVTIPDGHFTAIIGPNGCGKSTLLrtlSRL--MTPASGHVYLDGEQIQRYASKEVAKRIGLLAQNATTPGDITVQELVA 103
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLL---ARMagLLPGQGEILLNGRPLSDWSAAELARHRAYLSQQQSPPFAMPVFQYLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 104 RgrypHQPlftrwRKEDEEAVSRAM----KATGITDLARQSVDTLSGGQRQRAWIAMVLAQ-------ETAIMLLDEPTT 172
Cdd:COG4138 92 L----HQP-----AGASSEAVEQLLaqlaEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 173 WLDISHQIDLLELLSELNQQKGYTLAAVlHDLNQACRYATHLIALREGKIVAEGAPKEIVSAELIEKIYGL--RCTIIED 250
Cdd:COG4138 163 SLDVAQQAALDRLLRELCQQGITVVMSS-HDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVFGVkfRRLEVEG 241
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
8-222 |
2.61e-41 |
|
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: 141.09 E-value: 2.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 8 LRGDQLTLAYG----KKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVA--- 80
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 81 -KRIGLLAQNATTPGDITVQELVArgrYPhQPLFTRWRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLA 159
Cdd:cd03255 81 rRHIGFVFQSFNLLPDLTALENVE---LP-LLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490237141 160 QETAIMLLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQAcRYATHLIALREGKI 222
Cdd:cd03255 157 NDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
11-222 |
1.83e-40 |
|
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: 137.53 E-value: 1.83e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 11 DQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRyASKEVAKRIGLLAQNA 90
Cdd:cd03230 4 RNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLPEEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 91 TTPGDITVQELVargryphqplftrwrkedeeavsramkatgitdlarqsvdTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
Cdd:cd03230 83 SLYENLTVRENL----------------------------------------KLSGGMKQRLALAQALLHDPELLILDEP 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490237141 171 TTWLDISHQIDLLELLSELNQQKGytlaAVL---HDLNQACRYATHLIALREGKI 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 |
2.79e-40 |
|
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: 138.79 E-value: 2.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 8 LRGDQLTLAY----GKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVA--- 80
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 81 KRIGLLAQNATT---PGdITVQELVARGRYPHQPLftrwRKEDEEAVSRAMKATGI---TDLARQSVDTLSGGQRQRAWI 154
Cdd:cd03257 82 KEIQMVFQDPMSslnPR-MTIGEQIAEPLRIHGKL----SKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490237141 155 AMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEG 226
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
8-221 |
6.91e-40 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 136.16 E-value: 6.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 8 LRGDQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYA--SKEVAKRIGL 85
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 86 LAQNATTPGDITVQELVARGryphqplftrwrkedeeavsramkatgitdlarqsvdtLSGGQRQRAWIAMVLAQETAIM 165
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG--------------------------------------LSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490237141 166 LLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGK 221
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
8-226 |
4.56e-39 |
|
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: 135.31 E-value: 4.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 8 LRGDQLTLAYGkkTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGeqiQRYASKEVAKR-IGLL 86
Cdd:cd03298 1 VRLDKIRFSYG--EQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING---VDVTAAPPADRpVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 87 AQNATTPGDITVQELVARGRYPHqplfTRWRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIML 166
Cdd:cd03298 76 FQENNLFAHLTVEQNVGLGLSPG----LKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 167 LDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEG 226
Cdd:cd03298 152 LDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
12-221 |
5.23e-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: 133.52 E-value: 5.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 12 QLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIGLLAQnat 91
Cdd:cd00267 4 NLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 92 tpgditvqelvargryphqplftrwrkedeeavsramkatgitdlarqsvdtLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
Cdd:cd00267 81 ----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490237141 172 TWLDISHQIDLLELLSELNQQkGYTLAAVLHDLNQACRYATHLIALREGK 221
Cdd:cd00267 109 SGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
13-239 |
6.66e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 136.75 E-value: 6.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 13 LTLAYGKKTIA-ESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIqRYASK---EVAKRIGLLAQ 88
Cdd:PRK13639 7 LKYSYPDGTEAlKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKsllEVRKTVGIVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 89 NattPGD----ITVQELVARGryphqPLFTRWRKED-EEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETA 163
Cdd:PRK13639 86 N---PDDqlfaPTVEEDVAFG-----PLNLGLSKEEvEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490237141 164 IMLLDEPTTWLDISHQIDLLELLSELNqQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVS-AELIEK 239
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDLN-KEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSdIETIRK 233
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-225 |
1.77e-38 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 134.02 E-value: 1.77e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 1 MTAVtsrLRGDQLTLAYGKKTIA----ESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYAS 76
Cdd:COG1136 1 MSPL---LELRNLTKSYGTGEGEvtalRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 77 KEVAK----RIGLLAQNATTPGDITVQELVArgrYPHqpLFTRW-RKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQR 151
Cdd:COG1136 78 RELARlrrrHIGFVFQFFNLLPELTALENVA---LPL--LLAGVsRKERRERARELLERVGLGDRLDHRPSQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490237141 152 AWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQAcRYATHLIALREGKIVAE 225
Cdd:COG1136 153 VAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELA-ARADRVIRLRDGRIVSD 225
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
5-231 |
1.72e-37 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 134.84 E-value: 1.72e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 5 TSRLRGDQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIqryASKEVAKR-I 83
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV---TGLPPEKRnV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 84 GLLAQN-ATTPgDITVQELVA---RGRyphqplftRWRKED-EEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVL 158
Cdd:COG3842 80 GMVFQDyALFP-HLTVAENVAfglRMR--------GVPKAEiRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARAL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490237141 159 AQETAIMLLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEI 231
Cdd:COG3842 151 APEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
7-199 |
1.92e-37 |
|
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: 130.68 E-value: 1.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 7 RLRGDQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRyASKEVAKRIGLL 86
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 87 AQNATTPGDITVQELVArgryphqpLFTRWRKE--DEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAI 164
Cdd:COG4133 81 GHADGLKPELTVRENLR--------FWAALYGLraDREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPL 152
|
170 180 190
....*....|....*....|....*....|....*
gi 490237141 165 MLLDEPTTWLDISHQIDLLELLSELNQQKGYTLAA 199
Cdd:COG4133 153 WLLDEPFTALDAAGVALLAELIAAHLARGGAVLLT 187
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
33-244 |
2.70e-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: 131.13 E-value: 2.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 33 GHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEqiqryASKEVAKRIGLLAQNATTPGD--ITVQELVARGRYPHQ 110
Cdd:TIGR03771 6 GELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGA-----SPGKGWRHIGYVPQRHEFAWDfpISVAHTVMSGRTGHI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 111 PLFTRWRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELN 190
Cdd:TIGR03771 81 GWLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFIELA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490237141 191 QQkGYTLAAVLHDLNQACrYATHLIALREGKIVAEGAPKEIVSAELIEKIYGLR 244
Cdd:TIGR03771 161 GA-GTAILMTTHDLAQAM-ATCDRVVLLNGRVIADGTPQQLQDPAPWMTTFGVS 212
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-231 |
3.78e-37 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 131.70 E-value: 3.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 1 MTAVTSRLRGDQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRL--MTP---ASGHVYLDGEQIqrYA 75
Cdd:COG1117 5 ASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPgarVEGEILLDGEDI--YD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 76 SK----EVAKRIGLLAQNAtTPGDITVQELVARG-RYpHQplfTRWRKEDEEAVSRAMKATGITD-----LaRQSVDTLS 145
Cdd:COG1117 83 PDvdvvELRRRVGMVFQKP-NPFPKSIYDNVAYGlRL-HG---IKSKSELDEIVEESLRKAALWDevkdrL-KKSALGLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 146 GGQRQRAWIAMVLAQETAIMLLDEPTTWLD-IS-HQIDllELLSELNQQkgYTLAAVLHDLNQACRYATHLIALREGKIV 223
Cdd:COG1117 157 GGQQQRLCIARALAVEPEVLLMDEPTSALDpIStAKIE--ELILELKKD--YTIVIVTHNMQQAARVSDYTAFFYLGELV 232
|
....*...
gi 490237141 224 AEGAPKEI 231
Cdd:COG1117 233 EFGPTEQI 240
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
8-231 |
5.78e-37 |
|
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: 130.88 E-value: 5.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 8 LRGDQLTLAYGKKTIA-ESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIGLL 86
Cdd:cd03295 1 IEFENVTKRYGGGKKAvNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 87 AQNATTPGDITVQELVARgryphQPLFTRWRKED-EEAVSRAMKATGI--TDLARQSVDTLSGGQRQRAWIAMVLAQETA 163
Cdd:cd03295 81 IQQIGLFPHMTVEENIAL-----VPKLLKWPKEKiRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490237141 164 IMLLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEI 231
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
26-172 |
6.33e-37 |
|
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: 127.76 E-value: 6.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 26 LNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIGLLAQNATTPGDITVQELVARG 105
Cdd:pfam00005 4 VSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENLRLG 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490237141 106 RYphqpLFTRWRKEDEEAVSRAMKATGITDLARQSVD----TLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
Cdd:pfam00005 84 LL----LKGLSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
13-248 |
7.17e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 131.40 E-value: 7.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 13 LTLAYGKKTIA-ESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIGLLAQNat 91
Cdd:PRK13647 10 LHFRYKDGTKAlKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQD-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 92 tPGD----ITVQELVARGryphqPLFTRWRKED-EEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIML 166
Cdd:PRK13647 88 -PDDqvfsSTVWDDVAFG-----PVNMGLDKDEvERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 167 LDEPTTWLDISHQIDLLELLSELNQQkGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPkEIVSAELIEKIYGLRCT 246
Cdd:PRK13647 162 LDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK-SLLTDEDIVEQAGLRLP 239
|
..
gi 490237141 247 II 248
Cdd:PRK13647 240 LV 241
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
8-240 |
1.67e-36 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 129.10 E-value: 1.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 8 LRGDQLTLAYGKKTIaeSLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIqryASKEVAKR-IGLL 86
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL---TALPPAERpVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 87 AQNATTPGDITVQELVARGRYPHqplfTRWRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIML 166
Cdd:COG3840 77 FQENNLFPHLTVAQNIGLGLRPG----LKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490237141 167 LDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVSAELIEKI 240
Cdd:COG3840 153 LDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPAL 226
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
13-243 |
2.20e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 130.55 E-value: 2.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 13 LTLAYGKKTIAES-----LNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQI--QRYASKEVAKRIGL 85
Cdd:PRK13637 8 LTHIYMEGTPFEKkaldnVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 86 LAQnattpgditvqelvargrYPHQPLF------------TRWRKEDEEA---VSRAMKATGIT--DLARQSVDTLSGGQ 148
Cdd:PRK13637 88 VFQ------------------YPEYQLFeetiekdiafgpINLGLSEEEIenrVKRAMNIVGLDyeDYKDKSPFELSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 149 RQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAP 228
Cdd:PRK13637 150 KRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
250
....*....|....*.
gi 490237141 229 KEIV-SAELIEKIyGL 243
Cdd:PRK13637 230 REVFkEVETLESI-GL 244
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
26-231 |
2.33e-36 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 130.14 E-value: 2.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 26 LNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIGLLAQNattPGD----ITVQEL 101
Cdd:PRK13635 26 VSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVFQN---PDNqfvgATVQDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 102 VARGRYPHQ-PlftrwRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQI 180
Cdd:PRK13635 103 VAFGLENIGvP-----REEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRR 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490237141 181 DLLELLSELNQQKGYTLAAVLHDLNQACRyATHLIALREGKIVAEGAPKEI 231
Cdd:PRK13635 178 EVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEI 227
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
11-225 |
3.03e-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: 128.36 E-value: 3.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 11 DQLTLAYGKKTIA----ESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRyaskeVAKRIGLL 86
Cdd:cd03293 4 RNVSKTYGGGGGAvtalEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDRGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 87 AQNATTPGDITVQELVARGryphqPLFTRW-RKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIM 165
Cdd:cd03293 79 FQQDALLPWLTVLDNVALG-----LELQGVpKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490237141 166 LLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIAL--REGKIVAE 225
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAE 215
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
27-247 |
3.42e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 127.44 E-value: 3.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 27 NVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYAS----KEVAKRIGLLAQnatTPG----DITV 98
Cdd:PRK13634 27 NVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKnkklKPLRKKVGIVFQ---FPEhqlfEETV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 99 QELVARGryphqPLFTRWRKEDEEAVSRAM-KATGIT-DLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
Cdd:PRK13634 104 EKDICFG-----PMNFGVSEEDAKQKAREMiELVGLPeELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDP 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490237141 177 SHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVS--AELIEKIYGLRCTI 247
Cdd:PRK13634 179 KGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFAdpDELEAIGLDLPETV 251
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
11-226 |
7.36e-35 |
|
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: 124.23 E-value: 7.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 11 DQLTLAYGKKTIAESLNVTIPDGhFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKeVAKRIGLLAQNA 90
Cdd:cd03264 4 ENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-LRRRIGYLPQEF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 91 TTPGDITVQELVArgrypHQPLFTRWR-KEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
Cdd:cd03264 82 GVYPNFTVREFLD-----YIAWLKGIPsKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490237141 170 PTTWLDISHQIDLLELLSELNQQKGYTLAAvlHDLNQACRYATHLIALREGKIVAEG 226
Cdd:cd03264 157 PTAGLDPEERIRFRNLLSELGEDRIVILST--HIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
8-231 |
1.48e-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: 124.27 E-value: 1.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 8 LRGDQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYAskeVAKR-IGLL 86
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLP---PHKRpVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 87 AQN-ATTPgDITVQELVARGryphqpLFTRWRKEDE--EAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETA 163
Cdd:cd03300 78 FQNyALFP-HLTVFENIAFG------LRLKKLPKAEikERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490237141 164 IMLLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEI 231
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-231 |
1.56e-34 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 127.11 E-value: 1.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 1 MTAVtsRLRGdqLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRyasKEVA 80
Cdd:COG3839 1 MASL--ELEN--VSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTD---LPPK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 81 KR-IGLLAQN-AttpgditvqeLvargrYPHQ--------PLftRWRKED----EEAVSRAMKATGITDLARQSVDTLSG 146
Cdd:COG3839 74 DRnIAMVFQSyA----------L-----YPHMtvyeniafPL--KLRKVPkaeiDRRVREAAELLGLEDLLDRKPKQLSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 147 GQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEG 226
Cdd:COG3839 137 GQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVG 216
|
....*
gi 490237141 227 APKEI 231
Cdd:COG3839 217 TPEEL 221
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
6-235 |
3.50e-34 |
|
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: 129.49 E-value: 3.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 6 SRLRGDQLTLAY-GKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIG 84
Cdd:COG4988 335 PSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 85 LLAQNATTPGDiTVQELVARGRyphqplftrwRKEDEEAVSRAMKATGITDLARQS---VDT--------LSGGQRQRAW 153
Cdd:COG4988 415 WVPQNPYLFAG-TIRENLRLGR----------PDASDEELEAALEAAGLDEFVAALpdgLDTplgeggrgLSGGQAQRLA 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 154 IAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNQQKgyTLAAVLHDLNQAcRYATHLIALREGKIVAEGAPKEIVS 233
Cdd:COG4988 484 LARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALL-AQADRILVLDDGRIVEQGTHEELLA 560
|
..
gi 490237141 234 AE 235
Cdd:COG4988 561 KN 562
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
11-231 |
1.21e-33 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 122.02 E-value: 1.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 11 DQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRyASKEVAK---RIGLLA 87
Cdd:COG1126 5 ENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD-SKKDINKlrrKVGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 88 QNATTPGDITVQELVARGryphqPLFTRwRKEDEEAVSRAMKA---TGITDLARQSVDTLSGGQRQRAWIAMVLAQETAI 164
Cdd:COG1126 84 QQFNLFPHLTVLENVTLA-----PIKVK-KMSKAEAEERAMELlerVGLADKADAYPAQLSGGQQQRVAIARALAMEPKV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 165 MLLDEPTTWLD---IShqiDLLELLSELNQQkGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEI 231
Cdd:COG1126 158 MLFDEPTSALDpelVG---EVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEF 223
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
13-222 |
1.90e-33 |
|
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: 120.71 E-value: 1.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 13 LTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQI--QRYASKEVAKRIGLLAQNA 90
Cdd:cd03262 6 LHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGMVFQQF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 91 TTPGDITVQELVARGryphqpLFTRWRKEDEEAVSRAMKA---TGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
Cdd:cd03262 86 NLFPHLTVLENITLA------PIKVKGMSKAEAEERALELlekVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490237141 168 DEPTTWLDISHQIDLLELLSELnQQKGYTLAAVLHDLNQACRYATHLIALREGKI 222
Cdd:cd03262 160 DEPTSALDPELVGEVLDVMKDL-AEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
30-235 |
1.99e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 122.17 E-value: 1.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 30 IPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIGLLAQNATTP--GDItVQELVARG-- 105
Cdd:PRK13648 32 IPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQNPDNQfvGSI-VKYDVAFGle 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 106 --RYPHqplftrwrKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLL 183
Cdd:PRK13648 111 nhAVPY--------DEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490237141 184 ELLSELNQQKGYTLAAVLHDLNQACRyATHLIALREGKIVAEGAPKEIVSAE 235
Cdd:PRK13648 183 DLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHA 233
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
26-248 |
3.53e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 121.88 E-value: 3.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 26 LNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQrYASK---EVAKRIGLLAQNATTP-GDITVQEL 101
Cdd:PRK13636 25 ININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID-YSRKglmKLRESVGMVFQDPDNQlFSASVYQD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 102 VARGRYPHQ-PlftrwRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQI 180
Cdd:PRK13636 104 VSFGAVNLKlP-----EDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVS 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490237141 181 DLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVSAELIEKIYGLRCTII 248
Cdd:PRK13636 179 EIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEMLRKVNLRLPRI 246
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
25-250 |
3.70e-33 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 120.81 E-value: 3.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 25 SLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLmTPASGHVYLDGEQIQRYASKEVAKRIGLLAQNATTPGDITVQELVAR 104
Cdd:PRK03695 14 PLSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFAMPVFQYLTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 105 grypHQPLFTRWRkEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQ-------ETAIMLLDEPTTWLDIS 177
Cdd:PRK03695 93 ----HQPDKTRTE-AVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDVA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490237141 178 HQIDLLELLSELNQQKGytlaAVL---HDLNQACRYATHLIALREGKIVAEGAPKEIVSAELIEKIYGL--RCTIIED 250
Cdd:PRK03695 168 QQAALDRLLSELCQQGI----AVVmssHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVFGVnfRRLDVEG 241
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
8-230 |
7.90e-33 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 120.50 E-value: 7.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 8 LRGDQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMT----PASgHVYLDGEQIQRYA--SKEVAK 81
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksAGS-HIELLGRTVQREGrlARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 82 ---RIGLLAQNATTPGDITVQELVARGRYPHQPLFT---RW--RKEDEEAVsRAMKATGITDLARQSVDTLSGGQRQRAW 153
Cdd:PRK09984 84 sraNTGYIFQQFNLVNRLSVLENVLIGALGSTPFWRtcfSWftREQKQRAL-QALTRVGMVHFAHQRVSTLSGGQQQRVA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490237141 154 IAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKE 230
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-239 |
8.32e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 120.02 E-value: 8.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 6 SRLRGDQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLM-----TPASGHVYLDGEQIQRYASKEVA 80
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIFKMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 81 KRIGLLAQNATTPGDITVQELVARGryPHQPLFTRWRKEDEEAVSRAMKATGITDLARQSVD----TLSGGQRQRAWIAM 156
Cdd:PRK14247 82 RRVQMVFQIPNPIPNLSIFENVALG--LKLNRLVKSKKELQERVRWALEKAQLWDEVKDRLDapagKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 157 VLAQETAIMLLDEPTTWLDISHQIDLLELLSELnqQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVSA-- 234
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLEL--KKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNpr 237
|
....*.
gi 490237141 235 -ELIEK 239
Cdd:PRK14247 238 hELTEK 243
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
8-231 |
9.60e-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: 119.08 E-value: 9.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 8 LRGDQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKR-IGLL 86
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 87 AQNATTPGDITVQELVARGRYPHQPLFTRWRKEDEEAVSRAMKatgitDLARQSVDTLSGGQRQRAWIAMVLAQETAIML 166
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFPRLK-----ERRKQLAGTLSGGEQQMLAIARALMSRPKLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490237141 167 LDEPTTWL--DISHQIdlLELLSELNQQkGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEI 231
Cdd:cd03224 156 LDEPSEGLapKIVEEI--FEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-225 |
1.09e-32 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 120.19 E-value: 1.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 1 MTAVTSRLRGDQLTLAY----GKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIqryas 76
Cdd:COG1116 1 MSAAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 77 KEVAKRIGLLAQNATtpgdiTVQE-----LVARGRYphqplftrwRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQR 151
Cdd:COG1116 76 TGPGPDRGVVFQEPAllpwlTVLDnvalgLELRGVP---------KAERRERARELLELVGLAGFEDAYPHQLSGGMRQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490237141 152 AWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIAL--REGKIVAE 225
Cdd:COG1116 147 VAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLsaRPGRIVEE 222
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
27-232 |
6.91e-32 |
|
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: 118.13 E-value: 6.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 27 NVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEV----AKRIGLLAQN-ATTPgDITVQEL 101
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSfALLP-HRTVLEN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 102 VARG-RYPHQPlftrwRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQI 180
Cdd:cd03294 123 VAFGlEVQGVP-----RAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRR 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490237141 181 DLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIV 232
Cdd:cd03294 198 EMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
18-234 |
7.01e-32 |
|
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: 117.30 E-value: 7.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 18 GKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEV---AKRIGLLAQNATTPG 94
Cdd:cd03258 16 GKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaRRRIGMIFQHFNLLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 95 DITVQELVArgrYPHQPLFTRwRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
Cdd:cd03258 96 SRTVFENVA---LPLEIAGVP-KAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSAL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490237141 175 D--ISHQIdlLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVSA 234
Cdd:cd03258 172 DpeTTQSI--LALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
24-233 |
8.08e-32 |
|
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: 117.05 E-value: 8.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 24 ESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEvaKRIGLLAQNATTPGDITVQELVA 103
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK--RDISYVPQNYALFPHMTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 104 RGryphQPLFTRWRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLL 183
Cdd:cd03299 94 YG----LKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490237141 184 ELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVS 233
Cdd:cd03299 170 EELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFK 219
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
11-223 |
1.37e-31 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 115.81 E-value: 1.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 11 DQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEvaKRIGLLAQN- 89
Cdd:cd03301 4 ENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMVFQNy 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 90 ATTPgDITVQELVARG-RYPHQPlftrwRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168
Cdd:cd03301 82 ALYP-HMTVYDNIAFGlKLRKVP-----KDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490237141 169 EPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIV 223
Cdd:cd03301 156 EPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
7-235 |
1.79e-31 |
|
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: 121.80 E-value: 1.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 7 RLRGDQLTLAY--GKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIG 84
Cdd:COG4987 333 SLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 85 LLAQNAttpgDI---TVQE--LVARGRyphqplftrwrkEDEEAVSRAMKATGITDLARQSVD-----------TLSGGQ 148
Cdd:COG4987 413 VVPQRP----HLfdtTLREnlRLARPD------------ATDEELWAALERVGLGDWLAALPDgldtwlgeggrRLSGGE 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 149 RQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNQQKgyTLAAVLHDLnQACRYATHLIALREGKIVAEGAP 228
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRL-AGLERMDRILVLEDGRIVEQGTH 553
|
....*..
gi 490237141 229 KEIVSAE 235
Cdd:COG4987 554 EELLAQN 560
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
11-243 |
3.71e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 116.82 E-value: 3.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 11 DQLTLAY--GKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTP---ASGHVYLDGEQIQRYASKEVAKRIGL 85
Cdd:PRK13640 9 KHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIREKVGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 86 LAQNattPGD----ITVQELVARGryphqpLFTRW--RKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLA 159
Cdd:PRK13640 89 VFQN---PDNqfvgATVGDDVAFG------LENRAvpRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 160 QETAIMLLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQAcRYATHLIALREGKIVAEGAPKEIVSAELIEK 239
Cdd:PRK13640 160 VEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVEMLK 238
|
....
gi 490237141 240 IYGL 243
Cdd:PRK13640 239 EIGL 242
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
11-231 |
3.92e-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: 114.77 E-value: 3.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 11 DQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRyASKEVAKRIGLLAQNA 90
Cdd:cd03265 4 ENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 91 TTPGDITVQELVargrYPHQPLFTRWRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
Cdd:cd03265 83 SVDDELTGWENL----YIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490237141 171 TTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEI 231
Cdd:cd03265 159 TIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
11-235 |
9.92e-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: 120.32 E-value: 9.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 11 DQLTLAYGKKTIA--ESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIGLLAQ 88
Cdd:COG2274 477 ENVSFRYPGDSPPvlDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQ 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 89 NATtpgditvqelvargryphqpLFTR--------WRKE-DEEAVSRAMKATGITDLARQ---SVDT--------LSGGQ 148
Cdd:COG2274 557 DVF--------------------LFSGtirenitlGDPDaTDEEIIEAARLAGLHDFIEAlpmGYDTvvgeggsnLSGGQ 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 149 RQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNQQKgyTLAAVLHDLNQAcRYATHLIALREGKIVAEGAP 228
Cdd:COG2274 617 RQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGR--TVIIIAHRLSTI-RLADRIIVLDKGRIVEDGTH 693
|
....*..
gi 490237141 229 KEIVSAE 235
Cdd:COG2274 694 EELLARK 700
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
18-243 |
1.40e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 115.18 E-value: 1.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 18 GKKTIA-ESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASK-EVAKRIGLLAQN------ 89
Cdd:PRK13633 20 STEKLAlDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwDIRNKAGMVFQNpdnqiv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 90 ATTpgditVQELVARGryPH----QPlftrwrKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIM 165
Cdd:PRK13633 100 ATI-----VEEDVAFG--PEnlgiPP------EEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECI 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490237141 166 LLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRyATHLIALREGKIVAEGAPKEIVS-AELIEKIyGL 243
Cdd:PRK13633 167 IFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKeVEMMKKI-GL 243
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
18-235 |
1.69e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 114.90 E-value: 1.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 18 GKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIGLLAQNattPGD-- 95
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQN---PDDqi 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 96 --ITVQELVARGryphqPLFTRWrkeDEEA----VSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
Cdd:PRK13652 92 fsPTVEQDIAFG-----PINLGL---DEETvahrVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490237141 170 PTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVSAE 235
Cdd:PRK13652 164 PTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
11-222 |
1.80e-30 |
|
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: 113.03 E-value: 1.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 11 DQLTLAYgkKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEvaKRIGLLAQNA 90
Cdd:TIGR01277 4 DKVRYEY--EHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQ--RPVSMLFQEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 91 TTPGDITVQELVARGRYPHQPLfTRWRKEDEEAVSRAMkatGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
Cdd:TIGR01277 80 NLFAHLTVRQNIGLGLHPGLKL-NAEQQEKVVDAAQQV---GIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490237141 171 TTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKI 222
Cdd:TIGR01277 156 FSALDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
26-240 |
2.47e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 114.46 E-value: 2.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 26 LNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYAS----KEVAKRIGLLAQNATTP-GDITVQE 100
Cdd:PRK13649 26 VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdiKQIRKKVGLVFQFPESQlFEETVLK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 101 LVARGryphqPLFTRWRKEDEEAVSR-AMKATGIT-DLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISH 178
Cdd:PRK13649 106 DVAFG-----PQNFGVSQEEAEALAReKLALVGISeSLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490237141 179 QIDLLELLSELNqQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVS-AELIEKI 240
Cdd:PRK13649 181 RKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQdVDFLEEK 242
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
11-241 |
3.03e-30 |
|
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: 112.77 E-value: 3.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 11 DQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKR-IGLLAQN 89
Cdd:COG0410 7 ENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgIGYVPEG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 90 ATTPGDITVQE---LVARGRyphqplftRWRKEDEEAVSRamkatgITDL-------ARQSVDTLSGGQRQRAWIAMVLA 159
Cdd:COG0410 87 RRIFPSLTVEEnllLGAYAR--------RDRAEVRADLER------VYELfprlkerRRQRAGTLSGGEQQMLAIGRALM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 160 QETAIMLLDEPTtwLDISHQI--DLLELLSELNQQkGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVSAELI 237
Cdd:COG0410 153 SRPKLLLLDEPS--LGLAPLIveEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEV 229
|
....
gi 490237141 238 EKIY 241
Cdd:COG0410 230 REAY 233
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
9-223 |
7.55e-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: 111.19 E-value: 7.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 9 RGDQLTLAYGKKT-IAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIqryASKEVAKRIGLLA 87
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 88 QNattPGDITVQELVARGRYPHQPLFTrwrkEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
Cdd:cd03226 78 QD---VDYQLFTDSVREELLLGLKELD----AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490237141 168 DEPTTWLDISHQIDLLELLSELnQQKGYTLAAVLHDLNQACRYATHLIALREGKIV 223
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIREL-AAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
11-231 |
8.56e-30 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 114.47 E-value: 8.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 11 DQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIqrYASKEVAKR-IGLLAQN 89
Cdd:COG1118 6 RNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL--FTNLPPRERrVGFVFQH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 90 -ATTPgDITVQELVARGrYPHQPLFtrwRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168
Cdd:COG1118 84 yALFP-HMTVAENIAFG-LRVRPPS---KAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490237141 169 EPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEI 231
Cdd:COG1118 159 EPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1-211 |
9.16e-30 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 112.57 E-value: 9.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 1 MTAVTSRLRGDQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRL--MTP---ASGHVYLDGEQIqrYA 75
Cdd:PRK14243 4 LNGTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPgfrVEGKVTFHGKNL--YA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 76 SK----EVAKRIGLLAQNAtTPGDITVQELVARGryphqPLFTRWRKEDEEAVSRAMKATG----ITDLARQSVDTLSGG 147
Cdd:PRK14243 82 PDvdpvEVRRRIGMVFQKP-NPFPKSIYDNIAYG-----ARINGYKGDMDELVERSLRQAAlwdeVKDKLKQSGLSLSGG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490237141 148 QRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNQQkgYTLAAVLHDLNQACRYA 211
Cdd:PRK14243 156 QQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVS 217
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
11-222 |
1.07e-29 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 116.32 E-value: 1.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 11 DQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEqiqryaskevaKRIGLLAQNA 90
Cdd:COG0488 2 ENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG-----------LRIGYLPQEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 91 TTPGDITVQELVARGrypHQPLFTRWRKEDE----------------------------EAVSRA---MKATGIT-DLAR 138
Cdd:COG0488 71 PLDDDLTVLDTVLDG---DAELRALEAELEEleaklaepdedlerlaelqeefealggwEAEARAeeiLSGLGFPeEDLD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 139 QSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIsHQIDLLEllSELNQQKGyTLAAVLHD---LNQACryaTHLI 215
Cdd:COG0488 148 RPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL-ESIEWLE--EFLKNYPG-TVLVVSHDryfLDRVA---TRIL 220
|
....*..
gi 490237141 216 ALREGKI 222
Cdd:COG0488 221 ELDRGKL 227
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
11-221 |
1.31e-29 |
|
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: 109.39 E-value: 1.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 11 DQLTLAYG--KKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIGLLAQ 88
Cdd:cd03228 4 KNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAYVPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 89 NATtpgditvqelvargryphqpLFTrwrkedeeavsramkatgitdlarqsvDT-----LSGGQRQRAWIAMVLAQETA 163
Cdd:cd03228 84 DPF--------------------LFS---------------------------GTireniLSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490237141 164 IMLLDEPTTWLDISHQIDLLELLSELNQQKgyTLAAVLHDLNQAcRYATHLIALREGK 221
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAKGK--TVIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
11-230 |
2.36e-29 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 110.14 E-value: 2.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 11 DQLTLAYGKKTIA-ESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAK---RIG-- 84
Cdd:COG2884 5 ENVSKRYPGGREAlSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYlrrRIGvv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 85 -----LLAqnattpgDITVQE-----LVARGRYphqplftrwRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWI 154
Cdd:COG2884 85 fqdfrLLP-------DRTVYEnvalpLRVTGKS---------RKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490237141 155 AMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNQQKgytlAAVL---HDLNQACRYATHLIALREGKIVAEGAPKE 230
Cdd:COG2884 149 ARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRG----TTVLiatHDLELVDRMPKRVLELEDGRLVRDEARGV 223
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
32-226 |
4.14e-29 |
|
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: 109.31 E-value: 4.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 32 DGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGeQIQRYASKEV-----AKRIGLLAQNATTPGDITVQELVARGr 106
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNG-TVLFDSRKKInlppqQRKIGLVFQQYALFPHLNVRENLAFG- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 107 yphqpLFTRWRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELL 186
Cdd:cd03297 100 -----LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPEL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490237141 187 SELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEG 226
Cdd:cd03297 175 KQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-239 |
6.90e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 109.93 E-value: 6.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 13 LTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLM-----TPASGHVYLDGEQIqrYASK----EVAKRI 83
Cdd:PRK14267 10 LRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRNI--YSPDvdpiEVRREV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 84 GLLAQNATTPGDITVQELVARGRYPHQplFTRWRKEDEEAVSRAMKATGITDLARQSVD----TLSGGQRQRAWIAMVLA 159
Cdd:PRK14267 88 GMVFQYPNPFPHLTIYDNVAIGVKLNG--LVKSKKELDERVEWALKKAALWDEVKDRLNdypsNLSGGQRQRLVIARALA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 160 QETAIMLLDEPTTWLDISHQIDLLELLSELnqQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVSA---EL 236
Cdd:PRK14267 166 MKPKILLMDEPTANIDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENpehEL 243
|
...
gi 490237141 237 IEK 239
Cdd:PRK14267 244 TEK 246
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
26-241 |
8.15e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 110.69 E-value: 8.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 26 LNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYAS----KEVAKRIGLLAQNATTP-GDITVQE 100
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGnknlKKLRKKVSLVFQFPEAQlFENTVLK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 101 LVARGryphqPL-FTRWRKEDEEAVSRAMKATGI-TDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISH 178
Cdd:PRK13641 106 DVEFG-----PKnFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEG 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490237141 179 QIDLLELLSELnQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVS-AELIEKIY 241
Cdd:PRK13641 181 RKEMMQLFKDY-QKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSdKEWLKKHY 243
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
6-236 |
8.18e-29 |
|
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: 114.58 E-value: 8.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 6 SRLRGD----QLTLAY-GKKTIA-ESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEV 79
Cdd:TIGR03375 458 PRLQGEiefrNVSFAYpGQETPAlDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADL 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 80 AKRIGLLAQNATT-PGdiTVQELVARGRyphqPLFtrwrkeDEEAVSRAMKATGITDLARQSVD-----------TLSGG 147
Cdd:TIGR03375 538 RRNIGYVPQDPRLfYG--TLRDNIALGA----PYA------DDEEILRAAELAGVTEFVRRHPDgldmqigergrSLSGG 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 148 QRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNQQKgyTLAAVLHDLnQACRYATHLIALREGKIVAEGa 227
Cdd:TIGR03375 606 QRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGK--TLVLVTHRT-SLLDLVDRIIVMDNGRIVADG- 681
|
....*....
gi 490237141 228 PKEIVSAEL 236
Cdd:TIGR03375 682 PKDQVLEAL 690
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
13-231 |
1.26e-28 |
|
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: 108.97 E-value: 1.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 13 LTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIqryASKEVAKR-IGLLAQNAT 91
Cdd:cd03296 8 VSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA---TDVPVQERnVGFVFQHYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 92 TPGDITVQELVARGrYPHQPLFTRWRK-EDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
Cdd:cd03296 85 LFRHMTVFDNVAFG-LRVKPRSERPPEaEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490237141 171 TTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEI 231
Cdd:cd03296 164 FGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
7-231 |
1.71e-28 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 111.58 E-value: 1.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 7 RLRGdqLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKevaKR-IGL 85
Cdd:PRK09452 16 ELRG--ISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE---NRhVNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 86 LAQN-ATTPgDITVQELVARG----RYPHQplftrwrkEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQ 160
Cdd:PRK09452 91 VFQSyALFP-HMTVFENVAFGlrmqKTPAA--------EITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVN 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490237141 161 ETAIMLLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEI 231
Cdd:PRK09452 162 KPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 232
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
8-231 |
2.20e-28 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 108.71 E-value: 2.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 8 LRGDQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRL--MTP---ASGHVYLDGEQI--QRYASKEVA 80
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPevtITGSIVYNGHNIysPRTDTVDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 81 KRIGLLAQNAtTPGDITVQELVARGryphqpLFTRWRKEDE---EAVSRAMKATGI----TDLARQSVDTLSGGQRQRAW 153
Cdd:PRK14239 86 KEIGMVFQQP-NPFPMSIYENVVYG------LRLKGIKDKQvldEAVEKSLKGASIwdevKDRLHDSALGLSGGQQQRVC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 154 IAMVLAQETAIMLLDEPTTWLD-ISH-QIDllELLSELNQQkgYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEI 231
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDpISAgKIE--ETLLGLKDD--YTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
17-233 |
2.27e-28 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 108.26 E-value: 2.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 17 YGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRI--GLLAQNATTPG 94
Cdd:PRK09493 11 FGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQeaGMVFQQFYLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 95 DITVQELVARGryphqPLFTR-WRKEDEEAVSRAMKA-TGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
Cdd:PRK09493 91 HLTALENVMFG-----PLRVRgASKEEAEKQARELLAkVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490237141 173 WLDISHQIDLLELLSELNQQkGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVS 233
Cdd:PRK09493 166 ALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIK 225
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
24-226 |
3.20e-28 |
|
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: 107.29 E-value: 3.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 24 ESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIGLLAQNATT-PGdiTVQELV 102
Cdd:cd03245 21 DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQDVTLfYG--TLRDNI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 103 ARGRYPHqplftrwrkeDEEAVSRAMKATGITDLARQSVD-----------TLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
Cdd:cd03245 99 TLGAPLA----------DDERILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARALLNDPPILLLDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490237141 172 TWLDISHQIDLLELLSELNQQKgyTLAAVLHDLNqACRYATHLIALREGKIVAEG 226
Cdd:cd03245 169 SAMDMNSEERLKERLRQLLGDK--TLIIITHRPS-LLDLVDRIIVMDSGRIVADG 220
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
27-235 |
8.62e-28 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 106.59 E-value: 8.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 27 NVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGeqiQRYASKEVAKR-IGLLAQNATTPGDITVQELVARG 105
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG---QDHTTTPPSRRpVSMLFQENNLFSHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 106 RYPHQPLfTRWRKEDEEAVSRAMkatGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLEL 185
Cdd:PRK10771 96 LNPGLKL-NAAQREKLHAIARQM---GIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490237141 186 LSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVSAE 235
Cdd:PRK10771 172 VSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGK 221
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
13-231 |
1.66e-27 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 108.27 E-value: 1.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 13 LTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEvaKRIGLLAQNATT 92
Cdd:PRK11432 12 ITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ--RDICMVFQSYAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 93 PGDITVQELVARG-RYPHQPlftrwrkeDEEAVSRAMKATGITDLA---RQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168
Cdd:PRK11432 90 FPHMSLGENVGYGlKMLGVP--------KEERKQRVKEALELVDLAgfeDRYVDQISGGQQQRVALARALILKPKVLLFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490237141 169 EPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEI 231
Cdd:PRK11432 162 EPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
12-226 |
2.07e-27 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 104.99 E-value: 2.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 12 QLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRyaSKEVAKRIGLLAQNAT 91
Cdd:cd03268 5 DLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK--NIEALRRIGALIEAPG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 92 TPGDITVQE-LVARGRYPHQPlftrwrkedEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
Cdd:cd03268 83 FYPNLTAREnLRLLARLLGIR---------KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490237141 171 TTWLDISHQIDLLELLSELNQQkGYTLAAVLHDLNQACRYATHLIALREGKIVAEG 226
Cdd:cd03268 154 TNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
13-222 |
2.52e-27 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 105.92 E-value: 2.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 13 LTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVyLDGeqiqRYASKEVAKRIGLLAQNATT 92
Cdd:PRK11247 18 VSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAG----TAPLAEAREDTRLMFQDARL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 93 PGDITVQELVARGryphqpLFTRWRkedeEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
Cdd:PRK11247 93 LPWKKVIDNVGLG------LKGQWR----DAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490237141 173 WLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKI 222
Cdd:PRK11247 163 ALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
13-231 |
5.92e-27 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 105.23 E-value: 5.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 13 LTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQI---QRYASKEVAKRIGLLAQN 89
Cdd:PRK11831 13 VSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamSRSRLYTVRKRMSMLFQS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 90 ATTPGDITVQELVA-----RGRYPHQPLFTrwrkedeeAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAI 164
Cdd:PRK11831 93 GALFTDMNVFDNVAyplreHTQLPAPLLHS--------TVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490237141 165 MLLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEI 231
Cdd:PRK11831 165 IMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
26-207 |
6.57e-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: 102.89 E-value: 6.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 26 LNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQ--RYASKEVAKRIGLLAQNattPGD----ITVQ 99
Cdd:TIGR01166 11 LNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDysRKGLLERRQRVGLVFQD---PDDqlfaADVD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 100 ELVARGryphqPLfTRWRKEDE--EAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS 177
Cdd:TIGR01166 88 QDVAFG-----PL-NLGLSEAEveRRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPA 161
|
170 180 190
....*....|....*....|....*....|
gi 490237141 178 HQIDLLELLSELNQQkGYTLAAVLHDLNQA 207
Cdd:TIGR01166 162 GREQMLAILRRLRAE-GMTVVISTHDVDLA 190
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
13-231 |
7.60e-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: 103.74 E-value: 7.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 13 LTLAYGK--KTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIqRYASKEVAKRIGLLAQNA 90
Cdd:cd03263 6 LTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI-RTDRKAARQSLGYCPQFD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 91 TTPGDITVQELVArgryphqpLFTRWR----KEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIML 166
Cdd:cd03263 85 ALFDELTVREHLR--------FYARLKglpkSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490237141 167 LDEPTTWLDISHQIDLLELLSELNQQKgytlAAVL--HDLNQACRYATHLIALREGKIVAEGAPKEI 231
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVRKGR----SIILttHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
8-231 |
7.97e-27 |
|
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: 103.76 E-value: 7.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 8 LRGDQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKR-IGLL 86
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAgIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 87 AQNATTPGDITVQE-----LVARGRyphqplftRWRKEDEEA-----VSRAMkatgitdLARQSVDtLSGGQRQRAWIAM 156
Cdd:TIGR03410 81 PQGREIFPRLTVEEnlltgLAALPR--------RSRKIPDEIyelfpVLKEM-------LGRRGGD-LSGGQQQQLAIAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490237141 157 VLAQETAIMLLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEI 231
Cdd:TIGR03410 145 ALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
38-249 |
9.14e-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: 106.04 E-value: 9.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 38 IIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEvaKRIGLLAQNATTPGDITVQELVARGryphqplfTRWR 117
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHL--RHINMVFQSYALFPHMTVEENVAFG--------LKMR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 118 KED-EEAVSRAMKATG---ITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQiDLLEL-LSELNQQ 192
Cdd:TIGR01187 71 KVPrAEIKPRVLEALRlvqLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLR-DQMQLeLKTIQEQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490237141 193 KGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVS-------AELIEKIYGLRCTIIE 249
Cdd:TIGR01187 150 LGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEepanlfvARFIGEINVFEATVIE 213
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
26-233 |
9.18e-27 |
|
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: 106.35 E-value: 9.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 26 LNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRyASKEV-----AKRIGLLAQNATTPGDITVQE 100
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFD-SRKGIflppeKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 101 LVARGRYPHQPLFTRWRkedEEAVSRAMkatGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQI 180
Cdd:TIGR02142 95 NLRYGMKRARPSERRIS---FERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490237141 181 DLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVS 233
Cdd:TIGR02142 169 EILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
13-238 |
1.27e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 105.17 E-value: 1.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 13 LTLAYGKKTIAE-----SLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHV------------------YLDGE 69
Cdd:PRK13651 8 IVKIFNKKLPTElkaldNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekekVLEKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 70 QIQRYAS------KEVAKRIGLLAQNATTP-GDITVQELVARGryphqPLFTRWRKEdeEAVSRAMKATGITDLA----R 138
Cdd:PRK13651 88 VIQKTRFkkikkiKEIRRRVGVVFQFAEYQlFEQTIEKDIIFG-----PVSMGVSKE--EAKKRAAKYIELVGLDesylQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 139 QSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNQQkGYTLAAVLHDLNQACRYATHLIALR 218
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFK 239
|
250 260
....*....|....*....|..
gi 490237141 219 EGKIVAEGAPKEIVSAE--LIE 238
Cdd:PRK13651 240 DGKIIKDGDTYDILSDNkfLIE 261
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
8-224 |
2.22e-26 |
|
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: 102.43 E-value: 2.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 8 LRGDQLTLAY--GKKT--IAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAK-- 81
Cdd:TIGR02211 2 LKCENLGKRYqeGKLDtrVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKlr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 82 --RIGLLAQNATTPGDITVQELVArgryphQPLFTRwRKEDEEAVSRAM---KATGITDLARQSVDTLSGGQRQRAWIAM 156
Cdd:TIGR02211 82 nkKLGFIYQFHHLLPDFTALENVA------MPLLIG-KKSVKEAKERAYemlEKVGLEHRINHRPSELSGGERQRVAIAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490237141 157 VLAQETAIMLLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRyATHLIALREGKIVA 224
Cdd:TIGR02211 155 ALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKK-LDRVLEMKDGQLFN 221
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
37-241 |
2.40e-26 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 103.15 E-value: 2.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 37 AIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAkRIGLLA--QNATTPGDITVQE--LVARGRYPHQPL 112
Cdd:PRK11300 35 SLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA-RMGVVRtfQHVRLFREMTVIEnlLVAQHQQLKTGL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 113 FT------RWRKEDEEAVSRA---MKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLL 183
Cdd:PRK11300 114 FSgllktpAFRRAESEALDRAatwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELD 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490237141 184 ELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVSAELIEKIY 241
Cdd:PRK11300 194 ELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNPDVIKAY 251
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
11-235 |
2.65e-26 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 102.69 E-value: 2.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 11 DQLTLAYGKKTIA--ESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIGLLAQ 88
Cdd:cd03251 4 KNVTFRYPGDGPPvlRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVSQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 89 NATTPGDiTVQELVARGRyphqplftrwRKEDEEAVSRAMKATGITDLARQS---VDT--------LSGGQRQRAWIAMV 157
Cdd:cd03251 84 DVFLFND-TVAENIAYGR----------PGATREEVEEAARAANAHEFIMELpegYDTvigergvkLSGGQRQRIAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490237141 158 LAQETAIMLLDEPTTWLDISHQIDLLELLSELnqQKGYTLAAVLHDLNqACRYATHLIALREGKIVAEGAPKEIVSAE 235
Cdd:cd03251 153 LLKDPPILILDEATSALDTESERLVQAALERL--MKNRTTFVIAHRLS-TIENADRIVVLEDGKIVERGTHEELLAQG 227
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-224 |
3.03e-26 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 103.02 E-value: 3.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 6 SRLRGDQLTLAYGK----KTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQryasKEVAK 81
Cdd:COG4525 2 SMLTVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVT----GPGAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 82 RiGLLAQN-ATTPGdITVQELVARG-RYPHQPlftrwRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLA 159
Cdd:COG4525 78 R-GVVFQKdALLPW-LNVLDNVAFGlRLRGVP-----KAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490237141 160 QETAIMLLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIAL--REGKIVA 224
Cdd:COG4525 151 ADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRIVE 217
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-239 |
3.31e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 102.82 E-value: 3.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 12 QLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLM------TPASGHVYLDGEQIQRYASKEVAKRIGL 85
Cdd:PRK14246 15 RLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIeiydskIKVDGKVLYFGKDIFQIDAIKLRKEVGM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 86 LAQNATTPGDITVQELVArgrYPHQPLFTRWRKEDEEAVSRAMKATG----ITDLARQSVDTLSGGQRQRAWIAMVLAQE 161
Cdd:PRK14246 95 VFQQPNPFPHLSIYDNIA---YPLKSHGIKEKREIKKIVEECLRKVGlwkeVYDRLNSPASQLSGGQQQRLTIARALALK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 162 TAIMLLDEPTTWLDISHQIDLLELLSELNQQkgYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVSA---ELIE 238
Cdd:PRK14246 172 PKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSpknELTE 249
|
.
gi 490237141 239 K 239
Cdd:PRK14246 250 K 250
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
26-204 |
3.56e-26 |
|
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: 103.98 E-value: 3.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 26 LNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTP---ASGHVYLDGEQIQRYASKEV----AKRIGLLAQNATT---PGd 95
Cdd:COG0444 24 VSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELrkirGREIQMIFQDPMTslnPV- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 96 ITVQELVARGRYPHQPLftrWRKEDEEAVSRAMKATGITDlARQSVD----TLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
Cdd:COG0444 103 MTVGDQIAEPLRIHGGL---SKAEARERAIELLERVGLPD-PERRLDryphELSGGMRQRVMIARALALEPKLLIADEPT 178
|
170 180 190
....*....|....*....|....*....|....*
gi 490237141 172 TWLDISHQIDLLELLSELNQQKGytLAAVL--HDL 204
Cdd:COG0444 179 TALDVTIQAQILNLLKDLQRELG--LAILFitHDL 211
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
17-264 |
3.95e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 103.73 E-value: 3.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 17 YGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYAsKEVAKRIGLLAQNATTPGDI 96
Cdd:PRK13537 17 YGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA-RHARQRVGVVPQFDNLDPDF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 97 TVQE-LVARGRYphqplFTRWRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
Cdd:PRK13537 96 TVREnLLVFGRY-----FGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 176 ISHQIDLLELLSELnQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVSAEL---IEKIYGlrctiiEDPV 252
Cdd:PRK13537 171 PQARHLMWERLRSL-LARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEIgcdVIEIYG------PDPV 243
|
250
....*....|..
gi 490237141 253 AHTPLVVPLGRR 264
Cdd:PRK13537 244 ALRDELAPLAER 255
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
11-233 |
4.00e-26 |
|
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: 102.31 E-value: 4.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 11 DQLTLAYG-KKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIGLLAQN 89
Cdd:cd03253 4 ENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 90 aTTPGDITVQELVARGryphqplftRWRKEDEEaVSRAMKATGITDLA---RQSVDT--------LSGGQRQRAWIAMVL 158
Cdd:cd03253 84 -TVLFNDTIGYNIRYG---------RPDATDEE-VIEAAKAAQIHDKImrfPDGYDTivgerglkLSGGEKQRVAIARAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490237141 159 AQETAIMLLDEPTTWLDISHQIDLLELLSELNqqKGYTLAAVLHDLNQACRyATHLIALREGKIVAEGAPKEIVS 233
Cdd:cd03253 153 LKNPPILLLDEATSALDTHTEREIQAALRDVS--KGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLA 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-223 |
4.23e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 106.30 E-value: 4.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 8 LRGDQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLdGEQIqryaskevakRIGLLA 87
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------KIGYFD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 88 QNATT-PGDITVQELVARGryphqplftrwRKEDEEAVSRAMKA----TGitDLARQSVDTLSGGQRQRAWIAMVLAQET 162
Cdd:COG0488 385 QHQEElDPDKTVLDELRDG-----------APGGTEQEVRGYLGrflfSG--DDAFKPVGVLSGGEKARLALAKLLLSPP 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490237141 163 AIMLLDEPTTWLDishqIDLLELLSE-LNQQKGyTLAAVLHDlnqacRY-----ATHLIALREGKIV 223
Cdd:COG0488 452 NVLLLDEPTNHLD----IETLEALEEaLDDFPG-TVLLVSHD-----RYfldrvATRILEFEDGGVR 508
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
8-233 |
7.87e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 102.37 E-value: 7.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 8 LRGDQLTLAYGKKTIA-ESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYAS-KEVAKRIGL 85
Cdd:PRK13644 2 IRLENVSYSYPDGTPAlENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 86 LAQNATTP--GDiTVQELVARGryPHQ----PLFTRWRkedeeaVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLA 159
Cdd:PRK13644 82 VFQNPETQfvGR-TVEEDLAFG--PENlclpPIEIRKR------VDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490237141 160 QETAIMLLDEPTTWLDISHQIDLLELLSELNqQKGYTLAAVLHDLNQaCRYATHLIALREGKIVAEGAPKEIVS 233
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLH-EKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
13-226 |
1.34e-25 |
|
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: 100.05 E-value: 1.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 13 LTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQryasKEVAKRIGLLAQNatt 92
Cdd:cd03269 6 VTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD----IAARNRIGYLPEE--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 93 pgditvqelvaRGRYPHQPL------FTRWR----KEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQET 162
Cdd:cd03269 79 -----------RGLYPKMKVidqlvyLAQLKglkkEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDP 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490237141 163 AIMLLDEPTTWLDISHQIDLLELLSELnQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEG 226
Cdd:cd03269 148 ELLILDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
17-230 |
1.59e-25 |
|
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: 100.38 E-value: 1.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 17 YGKKTIA-ESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIGLLAQNATTPGD 95
Cdd:cd03254 12 YDEKKPVlKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDTFLFSG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 96 iTVQELVARGRyphqplftrwRKEDEEAVSRAMKATGITDLARQSVD-----------TLSGGQRQRAWIAMVLAQETAI 164
Cdd:cd03254 92 -TIMENIRLGR----------PNATDEEVIEAAKEAGAHDFIMKLPNgydtvlgenggNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490237141 165 MLLDEPTTWLDISHQIDLLELLSELNQQKgyTLAAVLHDLNqACRYATHLIALREGKIVAEGAPKE 230
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMKGR--TSIIIAHRLS-TIKNADKILVLDDGKIIEEGTHDE 223
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
8-238 |
1.77e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 101.32 E-value: 1.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 8 LRGDQLTLAYGKKTIAESLN---VTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIG 84
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNgvsFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 85 LLAQNATTPG-DITVQELVARGR----YPHQPLFTRwrkedeeaVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLA 159
Cdd:PRK13642 85 MVFQNPDNQFvGATVEDDVAFGMenqgIPREEMIKR--------VDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 160 QETAIMLLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRyATHLIALREGKIVAEGAPKEI--VSAELI 237
Cdd:PRK13642 157 LRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELfaTSEDMV 235
|
.
gi 490237141 238 E 238
Cdd:PRK13642 236 E 236
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
4-225 |
1.79e-25 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 101.04 E-value: 1.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 4 VTSRLRGDQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGE---QIQRYASKEVA 80
Cdd:TIGR02769 8 VTHTYRTGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQdlyQLDRKQRRAFR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 81 KRIGLLAQNAttPGDI----TVQELVARgryPHQPLFTRWRKEDEEAVSRAMKATGI-TDLARQSVDTLSGGQRQRAWIA 155
Cdd:TIGR02769 88 RDVQLVFQDS--PSAVnprmTVRQIIGE---PLRHLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 156 MVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAE 225
Cdd:TIGR02769 163 RALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEE 232
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-225 |
2.50e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 100.55 E-value: 2.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 20 KTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIGLLAQN--ATTPGDIT 97
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVFQDpmMGTAPSMT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 98 VQE--LVARGRypHQPLFTRWrkedeeAVSRAMKATGITDLAR----------QSVDTLSGGQRQrAwIAMVLA--QETA 163
Cdd:COG1101 99 IEEnlALAYRR--GKRRGLRR------GLTKKRRELFRELLATlglglenrldTKVGLLSGGQRQ-A-LSLLMAtlTKPK 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490237141 164 IMLLDEPTTWLD--ISHQIdlLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAE 225
Cdd:COG1101 169 LLLLDEHTAALDpkTAALV--LELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIILD 230
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-217 |
2.93e-25 |
|
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: 103.91 E-value: 2.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 2 TAVTSRLRGDQLTLAYGKKTIA-ESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVA 80
Cdd:TIGR02857 316 AAPASSLEFSGVSVAYPGRRPAlRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWR 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 81 KRIGLLAQNATTPGDiTVQELVARGRyphqplftrwRKEDEEAVSRAMKATGITDL---ARQSVDT--------LSGGQR 149
Cdd:TIGR02857 396 DQIAWVPQHPFLFAG-TIAENIRLAR----------PDASDAEIREALERAGLDEFvaaLPQGLDTpigeggagLSGGQA 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490237141 150 QRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNQqkGYTLAAVLHDLNQACRyATHLIAL 217
Cdd:TIGR02857 465 QRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
27-225 |
3.84e-25 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 99.50 E-value: 3.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 27 NVT--IPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAK----RIGLLAQNATTPGDITVQE 100
Cdd:PRK11629 27 NVSfsIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAElrnqKLGFIYQFHHLLPDFTALE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 101 LVArgryphQPLFT--RWRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISH 178
Cdd:PRK11629 107 NVA------MPLLIgkKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490237141 179 QIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLiALREGKIVAE 225
Cdd:PRK11629 181 ADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL-EMRDGRLTAE 226
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
17-233 |
4.81e-25 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 100.04 E-value: 4.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 17 YGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKE-------------VAKRI 83
Cdd:PRK10619 15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDgqlkvadknqlrlLRTRL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 84 GLLAQNATTPGDITVQELVARGryPHQPLFTRWRKEDEEAVsRAMKATGITDLARQSVDT-LSGGQRQRAWIAMVLAQET 162
Cdd:PRK10619 95 TMVFQHFNLWSHMTVLENVMEA--PIQVLGLSKQEARERAV-KYLAKVGIDERAQGKYPVhLSGGQQQRVSIARALAMEP 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490237141 163 AIMLLDEPTTWLDISHQIDLLELLSELNQQkGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVS 233
Cdd:PRK10619 172 EVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFG 241
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-231 |
6.46e-25 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 101.64 E-value: 6.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 1 MTAVTsrLRGdqLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGeqiQRYASKEVA 80
Cdd:PRK11000 1 MASVT--LRN--VTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGE---KRMNDVPPA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 81 KR-IGLLAQNATTpgditvqelvargrYPHQPLFTRW-------RKEDEEAVSRAMKATGITDLA----RQSVDtLSGGQ 148
Cdd:PRK11000 74 ERgVGMVFQSYAL--------------YPHLSVAENMsfglklaGAKKEEINQRVNQVAEVLQLAhlldRKPKA-LSGGQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 149 RQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAP 228
Cdd:PRK11000 139 RQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKP 218
|
...
gi 490237141 229 KEI 231
Cdd:PRK11000 219 LEL 221
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
8-241 |
6.98e-25 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 98.77 E-value: 6.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 8 LRGDQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKR-IGLL 86
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 87 AQNATTPGDITVQE---LVARGRYPHqplftrwRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETA 163
Cdd:cd03218 81 PQEASIFRKLTVEEnilAVLEIRGLS-------KKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 164 IMLLDEPTTWLD-ISHQiDLLELLSELNQQKgytlAAVL---HDLNQACRYATHLIALREGKIVAEGAPKEIVSAELIEK 239
Cdd:cd03218 154 FLLLDEPFAGVDpIAVQ-DIQKIIKILKDRG----IGVLitdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRK 228
|
..
gi 490237141 240 IY 241
Cdd:cd03218 229 VY 230
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
26-226 |
8.22e-25 |
|
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: 98.56 E-value: 8.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 26 LNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEqIQRYASKEVAKRIGL-LAQNATTPGDITVQElvar 104
Cdd:cd03267 40 ISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL-VPWKRRKKFLRRIGVvFGQKTQLWWDLPVID---- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 105 GRYPHQPLFtrwRKEDEEAVSRAMKATGITDLAR---QSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQID 181
Cdd:cd03267 115 SFYLLAAIY---DLPPARFKKRLDELSELLDLEElldTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQEN 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490237141 182 LLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEG 226
Cdd:cd03267 192 IRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-204 |
9.68e-25 |
|
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: 102.44 E-value: 9.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 2 TAVTSRLRGdqLTLAYGKKTIAES-LNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVA 80
Cdd:TIGR02868 331 GKPTLELRD--LSAGYPGAPPVLDgVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 81 KRIGLLAQNATTpGDITVQE--LVARGryphqplftrwrKEDEEAVSRAMKATGITDLARQSVD-----------TLSGG 147
Cdd:TIGR02868 409 RRVSVCAQDAHL-FDTTVREnlRLARP------------DATDEELWAALERVGLADWLRALPDgldtvlgeggaRLSGG 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490237141 148 QRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLseLNQQKGYTLAAVLHDL 204
Cdd:TIGR02868 476 ERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
26-235 |
1.11e-24 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 98.38 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 26 LNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIGLLAQNATTpGDITVQELVARG 105
Cdd:cd03249 22 LSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVL-FDGTIAENIRYG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 106 RYPhqplftRWRKEDEEAVSRAMKATGITDLArQSVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS 177
Cdd:cd03249 101 KPD------ATDEEVEEAAKKANIHDFIMSLP-DGYDTlvgergsqLSGGQKQRIAIARALLRNPKILLLDEATSALDAE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490237141 178 HQIDLLELLSELnqQKGYTLAAVLHDLNqACRYATHLIALREGKIVAEGAPKEIVSAE 235
Cdd:cd03249 174 SEKLVQEALDRA--MKGRTTIVIAHRLS-TIRNADLIAVLQNGQVVEQGTHDELMAQK 228
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
11-233 |
1.33e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 99.47 E-value: 1.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 11 DQLTLAYGKKTIAE-----SLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYAS----KEVAK 81
Cdd:PRK13646 6 DNVSYTYQKGTPYEhqaihDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkyiRPVRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 82 RIGLLAQnattpgditvqelvargrYPHQPLFtrwrkED-----------------EEAVSRA----MKATGITDLARQS 140
Cdd:PRK13646 86 RIGMVFQ------------------FPESQLF-----EDtvereiifgpknfkmnlDEVKNYAhrllMDLGFSRDVMSQS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 141 VDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREG 220
Cdd:PRK13646 143 PFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEG 222
|
250
....*....|...
gi 490237141 221 KIVAEGAPKEIVS 233
Cdd:PRK13646 223 SIVSQTSPKELFK 235
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
12-222 |
2.10e-24 |
|
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: 97.09 E-value: 2.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 12 QLTLAYGKKTIA-ESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAK---RIGLLA 87
Cdd:cd03292 5 NVTKTYPNGTAAlDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYlrrKIGVVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 88 QNATTPGDITVQELVARG-RYPHQPlftrwRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIML 166
Cdd:cd03292 85 QDFRLLPDRNVYENVAFAlEVTGVP-----PREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490237141 167 LDEPTTWLDISHQIDLLELLSELNqQKGYTLAAVLHDLNQACRYATHLIALREGKI 222
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKIN-KAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
13-264 |
2.23e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 99.52 E-value: 2.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 13 LTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYAsKEVAKRIGLLAQNATT 92
Cdd:PRK13536 47 VSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARA-RLARARIGVVPQFDNL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 93 PGDITVQE-LVARGRYphqplFTRWRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
Cdd:PRK13536 126 DLEFTVREnLLVFGRY-----FGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPT 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 172 TWLDISHQIDLLELLSELnQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKeivsaELIEKIYGlrCTIIE-- 249
Cdd:PRK13536 201 TGLDPHARHLIWERLRSL-LARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPH-----ALIDEHIG--CQVIEiy 272
|
250
....*....|....*..
gi 490237141 250 --DPVAHTPLVVPLGRR 264
Cdd:PRK13536 273 ggDPHELSSLVKPYARR 289
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
11-240 |
2.57e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 98.54 E-value: 2.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 11 DQLTLAYGKKTIAE-----SLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQI-----QRYASKEVA 80
Cdd:PRK13645 10 DNVSYTYAKKTPFEfkalnNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkKIKEVKRLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 81 KRIGLLAQnattpgditvqelvargrYPHQPLFTRWRKED------------EEAVSRAMKATGITDLARQSVD----TL 144
Cdd:PRK13645 90 KEIGLVFQ------------------FPEYQLFQETIEKDiafgpvnlgenkQEAYKKVPELLKLVQLPEDYVKrspfEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 145 SGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVA 224
Cdd:PRK13645 152 SGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVIS 231
|
250
....*....|....*..
gi 490237141 225 EGAPKEIVS-AELIEKI 240
Cdd:PRK13645 232 IGSPFEIFSnQELLTKI 248
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
11-239 |
3.10e-24 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 101.39 E-value: 3.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 11 DQLTLAYGKKTIA-ESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIGLLAQN 89
Cdd:COG1132 343 ENVSFSYPGDRPVlKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 90 ATtpgditvqelvargryphqpLFT-------RWRKED--EEAVSRAMKATGITDLAR---QSVDT--------LSGGQR 149
Cdd:COG1132 423 TF--------------------LFSgtireniRYGRPDatDEEVEEAAKAAQAHEFIEalpDGYDTvvgergvnLSGGQR 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 150 QRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELnqQKGYTLAAVLHDLNQAcRYATHLIALREGKIVAEGAPk 229
Cdd:COG1132 483 QRIAIARALLKDPPILILDEATSALDTETEALIQEALERL--MKGRTTIVIAHRLSTI-RNADRILVLDDGRIVEQGTH- 558
|
250
....*....|
gi 490237141 230 eivsAELIEK 239
Cdd:COG1132 559 ----EELLAR 564
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
8-226 |
3.34e-24 |
|
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: 96.67 E-value: 3.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 8 LRGDQLTLAYG--KKTIA--ESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRyASKEVAKRI 83
Cdd:cd03266 2 ITADALTKRFRdvKKTVQavDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 84 GLLAQNATTPGDITVQELVAR-GRyphqpLFTRWRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQET 162
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYfAG-----LYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490237141 163 AIMLLDEPTTWLDISHQIDLLELLSELNQQkGYTLAAVLHDLNQACRYATHLIALREGKIVAEG 226
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
33-233 |
3.52e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 97.88 E-value: 3.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 33 GHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIGLLAQNattPGD----ITVQELVARGR-- 106
Cdd:PRK13650 33 GEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQN---PDNqfvgATVEDDVAFGLen 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 107 --YPHQplftrwrkEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLE 184
Cdd:PRK13650 110 kgIPHE--------EMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIK 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490237141 185 LLSELNQQKGYTLAAVLHDLNQACrYATHLIALREGKIVAEGAPKEIVS 233
Cdd:PRK13650 182 TIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELFS 229
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-237 |
3.93e-24 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 99.52 E-value: 3.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 3 AVTSRLRGDQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEvaKR 82
Cdd:PRK11607 15 ALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ--RP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 83 IGLLAQNATTPGDITVQELVARG----RYPhqplftrwRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVL 158
Cdd:PRK11607 93 INMMFQSYALFPHMTVEQNIAFGlkqdKLP--------KAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 159 AQETAIMLLDEPTTWLDIS----HQIDLLELLselnQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEI--- 231
Cdd:PRK11607 165 AKRPKLLLLDEPMGALDKKlrdrMQLEVVDIL----ERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIyeh 240
|
250
....*....|
gi 490237141 232 ----VSAELI 237
Cdd:PRK11607 241 pttrYSAEFI 250
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
11-241 |
4.21e-24 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 97.65 E-value: 4.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 11 DQLTLAY-GKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVakrIGLLAQN 89
Cdd:PRK15056 10 NDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 90 ATTPGD--ITVQELVARGRYPHQPLFTRWRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
Cdd:PRK15056 87 EEVDWSfpVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490237141 168 DEPTTWLDISHQIDLLELLSELnQQKGYTLAAVLHDLNQACRYATHLIALReGKIVAEGAPKEIVSAELIEKIY 241
Cdd:PRK15056 167 DEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDYTVMVK-GTVLASGPTETTFTAENLELAF 238
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
11-231 |
4.96e-24 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 99.00 E-value: 4.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 11 DQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEvaKRIGLLAQNA 90
Cdd:PRK10851 6 ANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVFQHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 91 TTPGDITVQELVARGryphQPLFTRWRKEDEEAVSRamKATGITD------LARQSVDTLSGGQRQRAWIAMVLAQETAI 164
Cdd:PRK10851 84 ALFRHMTVFDNIAFG----LTVLPRRERPNAAAIKA--KVTQLLEmvqlahLADRYPAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490237141 165 MLLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEI 231
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
17-226 |
5.99e-24 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 96.62 E-value: 5.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 17 YGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQrYASKEVAKRIGLLAQNAttpGDI 96
Cdd:PRK11124 12 YGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFD-FSKTPSDKAIRELRRNV---GMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 97 TVQELVargrYPH----QPLFTRWRK----EDEEAVSRAMKATG---ITDLARQSVDTLSGGQRQRAWIAMVLAQETAIM 165
Cdd:PRK11124 88 FQQYNL----WPHltvqQNLIEAPCRvlglSKDQALARAEKLLErlrLKPYADRFPLHLSGGQQQRVAIARALMMEPQVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490237141 166 LLDEPTTWLD--ISHQIdlLELLSELnQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEG 226
Cdd:PRK11124 164 LFDEPTAALDpeITAQI--VSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
26-189 |
1.08e-23 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 95.42 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 26 LNVTIPDGHFTAIIGPNGCGKSTLLRTLSRL-----MTpaSGHVYLDGEQIQRYaskEVAKRIGLLAQNATTPGDITVQE 100
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRvegggTT--SGQILFNGQPRKPD---QFQKCVAYVRQDDILLPGLTVRE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 101 LV---ARGRYP-HQPLFTRwrkeDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
Cdd:cd03234 101 TLtytAILRLPrKSSDAIR----KKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
170
....*....|...
gi 490237141 177 SHQIDLLELLSEL 189
Cdd:cd03234 177 FTALNLVSTLSQL 189
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
8-228 |
1.58e-23 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 95.19 E-value: 1.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 8 LRGDQLTLAY----GKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAK-- 81
Cdd:COG4181 9 IELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 82 --RIGLLAQNATTPGDITVQELVArgryphQPLFTRWRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLA 159
Cdd:COG4181 89 arHVGFVFQSFQLLPTLTALENVM------LPLELAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490237141 160 QETAIMLLDEPTTWLD--ISHQIdlLELLSELNQQKGYTLAAVLHDLNQACRyATHLIALREGKIVAEGAP 228
Cdd:COG4181 163 TEPAILFADEPTGNLDaaTGEQI--IDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTAA 230
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
8-226 |
1.61e-23 |
|
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: 93.92 E-value: 1.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 8 LRGDQLTLAYG--KKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYaSKEVAKRIGL 85
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL-EKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 86 LAQNattpgditvqelvargryPHqpLFTrwrkedeeavsramkATGITDLARQsvdtLSGGQRQRAWIAMVLAQETAIM 165
Cdd:cd03247 80 LNQR------------------PY--LFD---------------TTLRNNLGRR----FSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490237141 166 LLDEPTTWLDISHQIDLLELLSElnQQKGYTLAAVLHDLnQACRYATHLIALREGKIVAEG 226
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFE--VLKDKTLIWITHHL-TGIEHMDKILFLENGKIIMQG 178
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
26-234 |
1.75e-23 |
|
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: 98.99 E-value: 1.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 26 LNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMtPASGHVYLDGEQIQRYASKE---VAKRIGLLAQnattpgD------- 95
Cdd:COG4172 305 VSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRAlrpLRRRMQVVFQ------Dpfgslsp 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 96 -ITVQELVARGRYPHQPLFTRwrKEDEEAVSRAMKATGitdLARQSVD----TLSGGQRQRAWIAMVLAQETAIMLLDEP 170
Cdd:COG4172 378 rMTVGQIIAEGLRVHGPGLSA--AERRARVAEALEEVG---LDPAARHryphEFSGGQRQRIAIARALILEPKLLVLDEP 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490237141 171 TTWLDISHQIDLLELLSELnqQKGYTLAAVL--HDLnQACRYATH-LIALREGKIVAEGAPKEIVSA 234
Cdd:COG4172 453 TSALDVSVQAQILDLLRDL--QREHGLAYLFisHDL-AVVRALAHrVMVMKDGKVVEQGPTEQVFDA 516
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
26-231 |
1.81e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 96.34 E-value: 1.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 26 LNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLdGEQIQRYASKE-----VAKRIGLLAQnatTPGDITVQE 100
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVSSTSKQkeikpVRKKVGVVFQ---FPESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 101 LVARGRYPHQPLFTRWRKEDEEAVSRAMKATGIT-DLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQ 179
Cdd:PRK13643 101 TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKAR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490237141 180 IDLLELLSELNqQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEI 231
Cdd:PRK13643 181 IEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDV 231
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
7-208 |
1.85e-23 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 94.17 E-value: 1.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 7 RLRGDQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIGll 86
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 87 AQNATTPgDITVQELVArgryphqplFtrWRK---EDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETA 163
Cdd:PRK13539 80 HRNAMKP-ALTVAENLE---------F--WAAflgGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRP 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490237141 164 IMLLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQAC 208
Cdd:PRK13539 148 IWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATHIPLGLPG 192
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
2-225 |
1.88e-23 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 95.91 E-value: 1.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 2 TAVTSRLRGDQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGE---QIQRYASKE 78
Cdd:PRK10419 7 SGLSHHYAHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEplaKLNRAQRKA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 79 VAKRIGLLAQNAttPGDITVQELVarGRYPHQPL--FTRWRKEDEEAVSRAM-KATGITD-LARQSVDTLSGGQRQRAWI 154
Cdd:PRK10419 87 FRRDIQMVFQDS--ISAVNPRKTV--REIIREPLrhLLSLDKAERLARASEMlRAVDLDDsVLDKRPPQLSGGQLQRVCL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490237141 155 AMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAE 225
Cdd:PRK10419 163 ARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVET 233
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
27-233 |
2.31e-23 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 96.69 E-value: 2.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 27 NVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVA---KRIG-------LLAQNattpgdi 96
Cdd:COG1135 25 SLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRaarRKIGmifqhfnLLSSR------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 97 TVQELVARgryphqPL-FTRWRKEDEEA-VSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
Cdd:COG1135 98 TVAENVAL------PLeIAGVPKAEIRKrVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSAL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490237141 175 D--ISHQIdlLELLSELNQQKGYTLAAVLHDLN---QACryatHLIA-LREGKIVAEGAPKEIVS 233
Cdd:COG1135 172 DpeTTRSI--LDLLKDINRELGLTIVLITHEMDvvrRIC----DRVAvLENGRIVEQGPVLDVFA 230
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-234 |
2.50e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 95.55 E-value: 2.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 13 LTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVY-----LDGEQIQRYASK-EVAKRIGLL 86
Cdd:PRK14271 27 LTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYsgdvlLGGRSIFNYRDVlEFRRRVGML 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 87 AQNAtTPGDITVQELVARGRYPHQPLFtrwRKEDEEAVSRAMKATGITDLARQSVDT----LSGGQRQRAWIAMVLAQET 162
Cdd:PRK14271 107 FQRP-NPFPMSIMDNVLAGVRAHKLVP---RKEFRGVAQARLTEVGLWDAVKDRLSDspfrLSGGQQQLLCLARTLAVNP 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490237141 163 AIMLLDEPTTWLDISHQIDLLELLSELNQQkgYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVSA 234
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSS 252
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
19-231 |
3.05e-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: 3.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 19 KKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIGLLAQnattpgditv 98
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQ---------- 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 99 QELVARGRYPHQPLFTRWRKEDEEAVSRAMKA---TGITDLArQSVDT--------LSGGQRQRAWIAMVLAQETAIMLL 167
Cdd:TIGR00958 563 EPVLFSGSVRENIAYGLTDTPDEEIMAAAKAAnahDFIMEFP-NGYDTevgekgsqLSGGQKQRIAIARALVRKPRVLIL 641
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490237141 168 DEPTTWLDISHQidllELLSELNQQKGYTLAAVLHDLnQACRYATHLIALREGKIVAEGAPKEI 231
Cdd:TIGR00958 642 DEATSALDAECE----QLLQESRSRASRTVLLIAHRL-STVERADQILVLKKGSVVEMGTHKQL 700
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
27-233 |
3.32e-23 |
|
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: 96.71 E-value: 3.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 27 NVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRyASKEV-----AKRIGLLAQNATTPGDITVQEL 101
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQD-SARGIflpphRRRIGYVFQEARLFPHLSVRGN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 102 VargRYPHQPLFTRWRKEDEEAVSRAMkatGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQID 181
Cdd:COG4148 98 L---LYGRKRAPRAERRISFDEVVELL---GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490237141 182 LLELLSELNQQKG----YtlaaVLHDLNQACRYATHLIALREGKIVAEGAPKEIVS 233
Cdd:COG4148 172 ILPYLERLRDELDipilY----VSHSLDEVARLADHVVLLEQGRVVASGPLAEVLS 223
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
24-220 |
3.42e-23 |
|
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: 94.45 E-value: 3.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 24 ESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVakrigLLAQNATTPGDITVQELVA 103
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPWLTVRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 104 RGryPHQPLFTRWRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLL 183
Cdd:TIGR01184 77 LA--VDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQ 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 490237141 184 ELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREG 220
Cdd:TIGR01184 155 EELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
7-235 |
3.74e-23 |
|
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: 98.10 E-value: 3.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 7 RLRG----DQLTLAYGKKT--IAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVA 80
Cdd:TIGR03797 447 KLSGaievDRVTFRYRPDGplILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVR 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 81 KRIGLLAQNAT-TPGDItVQELVARGRYPHqplftrwrKEDEEAVSRAMKATGITDLA-------RQSVDTLSGGQRQRA 152
Cdd:TIGR03797 527 RQLGVVLQNGRlMSGSI-FENIAGGAPLTL--------DEAWEAARMAGLAEDIRAMPmgmhtviSEGGGTLSGGQRQRL 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 153 WIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNqqkgYTLAAVLHDLNqACRYATHLIALREGKIVAEGAPKEIV 232
Cdd:TIGR03797 598 LIARALVRKPRILLFDEATSALDNRTQAIVSESLERLK----VTRIVIAHRLS-TIRNADRIYVLDAGRVVQQGTYDELM 672
|
...
gi 490237141 233 SAE 235
Cdd:TIGR03797 673 ARE 675
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-234 |
5.08e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 97.47 E-value: 5.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 18 GKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMtPASGHVYLDGEQIQRYASKE---VAKRIGLLAQ--NATT 92
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQllpVRHRIQVVFQdpNSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 93 PGDITVQELVARGRYPHQPLFTRwrKEDEEAVSRAMKATGITDLARQSVDT-LSGGQRQRAWIAMVLAQETAIMLLDEPT 171
Cdd:PRK15134 376 NPRLNVLQIIEEGLRVHQPTLSA--AQREQQVIAVMEEVGLDPETRHRYPAeFSGGQRQRIAIARALILKPSLIILDEPT 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490237141 172 TWLDISHQIDLLELLSELNQQKGYTLAAVLHDLnQACRYATH-LIALREGKIVAEGAPKEIVSA 234
Cdd:PRK15134 454 SSLDKTVQAQILALLKSLQQKHQLAYLFISHDL-HVVRALCHqVIVLRQGEVVEQGDCERVFAA 516
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
8-222 |
5.74e-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: 92.28 E-value: 5.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 8 LRGDQLTLAYG--KKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIGL 85
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 86 LAQNATtpgditvqelvargryphqpLFtrwrkedeeavsramkATGITDlarqsvDTLSGGQRQRAWIAMVLAQETAIM 165
Cdd:cd03246 81 LPQDDE--------------------LF----------------SGSIAE------NILSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 166 LLDEPTTWLDISHQIDLLELLSELnQQKGYTLAAVLHD---LNQACRyathLIALREGKI 222
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRpetLASADR----ILVLEDGRV 173
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
6-241 |
5.81e-23 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 93.94 E-value: 5.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 6 SRLRGDQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKR-IG 84
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLgIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 85 LLAQNATTPGDITVQE---LVARGRYPHqplftrwRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQE 161
Cdd:COG1137 82 YLPQEASIFRKLTVEDnilAVLELRKLS-------KKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 162 TAIMLLDEPTTWLD-IShQIDLLELLSELnQQKGY-----------TL-----AAVLHdlnqacryathlialrEGKIVA 224
Cdd:COG1137 155 PKFILLDEPFAGVDpIA-VADIQKIIRHL-KERGIgvlitdhnvreTLgicdrAYIIS----------------EGKVLA 216
|
250
....*....|....*..
gi 490237141 225 EGAPKEIVSAELIEKIY 241
Cdd:COG1137 217 EGTPEEILNNPLVRKVY 233
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
11-231 |
9.86e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 94.41 E-value: 9.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 11 DQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRyaskEVAKRIGLLaqna 90
Cdd:COG4152 5 KGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP----EDRRRIGYL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 91 ttPgditvQElvaRGRYPHQPL------FTRWR----KEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQ 160
Cdd:COG4152 77 --P-----EE---RGLYPKMKVgeqlvyLARLKglskAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLH 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490237141 161 ETAIMLLDEPTTWLD-ISHQIdLLELLSELNqQKGytlAAVL---HDLNQACRYATHLIALREGKIVAEGAPKEI 231
Cdd:COG4152 147 DPELLILDEPFSGLDpVNVEL-LKDVIRELA-AKG---TTVIfssHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
7-236 |
1.12e-22 |
|
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: 96.65 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 7 RLRGDQLTLAY--GKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIG 84
Cdd:TIGR01842 316 HLSVENVTIVPpgGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIG 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 85 LLAQNATT-PGdiTVQELVARgryphqplFTRwrKEDEEAVSRAMKATGITDLAR---QSVDT--------LSGGQRQRA 152
Cdd:TIGR01842 396 YLPQDVELfPG--TVAENIAR--------FGE--NADPEKIIEAAKLAGVHELILrlpDGYDTvigpggatLSGGQRQRI 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 153 WIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNQQKGYTLaAVLHDLNqACRYATHLIALREGKIVAEGaPKEIV 232
Cdd:TIGR01842 464 ALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVV-VITHRPS-LLGCVDKILVLQDGRIARFG-ERDEV 540
|
....
gi 490237141 233 SAEL 236
Cdd:TIGR01842 541 LAKL 544
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
17-226 |
1.62e-22 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 92.77 E-value: 1.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 17 YGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQ------IQRYASKEVAKRIGLLAQNA 90
Cdd:COG4161 12 YGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdfsqkPSEKAIRLLRQKVGMVFQQY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 91 TTPGDITV-QELVARgryPHQPLftrwRKEDEEAVSRAMK---ATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIML 166
Cdd:COG4161 92 NLWPHLTVmENLIEA---PCKVL----GLSKEQAREKAMKllaRLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490237141 167 LDEPTTWLD--ISHQIdlLELLSELnQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEG 226
Cdd:COG4161 165 FDEPTAALDpeITAQV--VEIIREL-SQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG 223
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-206 |
1.88e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 92.08 E-value: 1.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 1 MTAVTSRLRGDQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVA 80
Cdd:PRK10247 1 MQENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 81 KRIGLLAQNATTPGDITVQELVargrYPHQplfTRWRKEDEEAVSRAMKATGITD-LARQSVDTLSGGQRQRAWIAMVLA 159
Cdd:PRK10247 81 QQVSYCAQTPTLFGDTVYDNLI----FPWQ---IRNQQPDPAIFLDDLERFALPDtILTKNIAELSGGEKQRISLIRNLQ 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490237141 160 QETAIMLLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQ 206
Cdd:PRK10247 154 FMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE 200
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
18-202 |
4.60e-22 |
|
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: 90.30 E-value: 4.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 18 GKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLS-RLMTPA-SGHVYLDGEQIQRYASKevaKRIGLLAQNATTPGD 95
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgRRTGLGvSGEVLINGRPLDKRSFR---KIIGYVPQDDILHPT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 96 ITVQelvargryphqplftrwrkedeEAVSRAMKATGItdlarqsvdtlSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
Cdd:cd03213 97 LTVR----------------------ETLMFAAKLRGL-----------SGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
170 180
....*....|....*....|....*..
gi 490237141 176 ISHQIDLLELLSELNQQkGYTLAAVLH 202
Cdd:cd03213 144 SSSALQVMSLLRRLADT-GRTIICSIH 169
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
7-234 |
5.77e-22 |
|
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: 94.81 E-value: 5.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 7 RLRGDQLTLAY--GKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIG 84
Cdd:COG4618 330 RLSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIG 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 85 LLAQNATT-PGdiTVQELVARgryphqplFTrwrKEDEEAVSRAMKATGITDL-AR--QSVDT--------LSGGQRQRA 152
Cdd:COG4618 410 YLPQDVELfDG--TIAENIAR--------FG---DADPEKVVAAAKLAGVHEMiLRlpDGYDTrigeggarLSGGQRQRI 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 153 WIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNQQKGyTLAAVLHDLNqACRYATHLIALREGKIVAEGAPKEIV 232
Cdd:COG4618 477 GLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGA-TVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDEVL 554
|
..
gi 490237141 233 SA 234
Cdd:COG4618 555 AR 556
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-234 |
1.20e-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: 93.63 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 4 VTSRLRGDQLTLAYGKKTIA--ESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAK 81
Cdd:TIGR02203 327 ARGDVEFRNVTFRYPGRDRPalDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 82 RIGLLAQNATTPGDiTVQELVARGRYphqplftrwRKEDEEAVSRAMKATGITDLARQS---VDT--------LSGGQRQ 150
Cdd:TIGR02203 407 QVALVSQDVVLFND-TIANNIAYGRT---------EQADRAEIERALAAAYAQDFVDKLplgLDTpigengvlLSGGQRQ 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 151 RAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELnqQKGYTLAAVLHDLNqACRYATHLIALREGKIVAEGAPKE 230
Cdd:TIGR02203 477 RLAIARALLKDAPILILDEATSALDNESERLVQAALERL--MQGRTTLVIAHRLS-TIEKADRIVVMDDGRIVERGTHNE 553
|
....
gi 490237141 231 IVSA 234
Cdd:TIGR02203 554 LLAR 557
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
8-207 |
1.44e-21 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 89.46 E-value: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 8 LRGDQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTP---ASGHVYLDGEQIQRYASKevAKRIG 84
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAE--QRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 85 LLAQNAttpgditvqelvargryphqPLFTRW---------------RKEDEEAVSRAMKATGITDLARQSVDTLSGGQR 149
Cdd:COG4136 80 ILFQDD--------------------LLFPHLsvgenlafalpptigRAQRRARVEQALEEAGLAGFADRDPATLSGGQR 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490237141 150 QRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLEL-LSELNQQKGYTLaAVLHDLNQA 207
Cdd:COG4136 140 ARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFvFEQIRQRGIPAL-LVTHDEEDA 197
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
32-234 |
1.59e-21 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 90.25 E-value: 1.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 32 DGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQI--------QRYAS--KEVAK---RIGLLAQNATTPGDITV 98
Cdd:COG4598 33 KGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkpdrdgELVPAdrRQLQRirtRLGMVFQSFNLWSHMTV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 99 QELVARGryPHQPLftrwRKEDEEAVSRAMK---ATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
Cdd:COG4598 113 LENVIEA--PVHVL----GRPKAEAIERAEAllaKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALD 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490237141 176 ISHQIDLLELLSELNQQkGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVSA 234
Cdd:COG4598 187 PELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGN 244
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
27-233 |
1.69e-21 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 92.40 E-value: 1.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 27 NVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVA----KRIGLLAQNATTPGDITVQELV 102
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 103 ARGryphQPLFTRWRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDL 182
Cdd:PRK10070 128 AFG----MELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490237141 183 LELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVS 233
Cdd:PRK10070 204 QDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-239 |
2.15e-21 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 93.16 E-value: 2.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 2 TAVTSRLRGD----QLTLAY-GKKTIA-ESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYA 75
Cdd:PRK11176 332 KRVIERAKGDiefrNVTFTYpGKEVPAlRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYT 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 76 SKEVAKRIGLLAQNATTPGDiTVQELVArgrYPHQPLFTRwrkEDEEAVSRAMKATGITDLARQSVDT--------LSGG 147
Cdd:PRK11176 412 LASLRNQVALVSQNVHLFND-TIANNIA---YARTEQYSR---EQIEEAARMAYAMDFINKMDNGLDTvigengvlLSGG 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 148 QRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELnqQKGYTLAAVLHDLNqACRYATHLIALREGKIVAEGa 227
Cdd:PRK11176 485 QRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLS-TIEKADEILVVEDGEIVERG- 560
|
250
....*....|..
gi 490237141 228 pkeiVSAELIEK 239
Cdd:PRK11176 561 ----THAELLAQ 568
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
8-207 |
2.33e-21 |
|
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: 88.57 E-value: 2.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 8 LRGDQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASkEVAKRIGLLA 87
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD-EPHENILYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 88 QNATTPGDITVQELVARGRYPHQPlftrwrkeDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
Cdd:TIGR01189 80 HLPGLKPELSALENLHFWAAIHGG--------AQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWIL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490237141 168 DEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQA 207
Cdd:TIGR01189 152 DEPTTALDKAGVALLAGLLRAHLARGGIVLLTTHQDLGLV 191
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
8-223 |
2.47e-21 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 89.16 E-value: 2.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 8 LRGDQLTLAY-GKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVA---KRI 83
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPflrRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 84 GLLAQNATTPGDITVQELVArgryphQPLFTRWRKEDE--EAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQE 161
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVA------IPLIIAGASGDDirRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490237141 162 TAIMLLDEPTTWLDISHQIDLLELLSELNQQkGYTLAAVLHDLNQACRYATHLIALREGKIV 223
Cdd:PRK10908 156 PAVLLADEPTGNLDDALSEGILRLFEEFNRV-GVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
12-234 |
5.26e-21 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 89.04 E-value: 5.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 12 QLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQI--------QRYASKEVAKRI 83
Cdd:PRK11264 8 NLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslsqQKGLIRQLRQHV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 84 GLLAQNATTPGDITVQELVARGryphqPLFTRWR-KEDEEAVSRAMKA-TGITDLARQSVDTLSGGQRQRAWIAMVLAQE 161
Cdd:PRK11264 88 GFVFQNFNLFPHRTVLENIIEG-----PVIVKGEpKEEATARARELLAkVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490237141 162 TAIMLLDEPTTWLDISHQIDLLELLSELNQQKgYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVSA 234
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFAD 234
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
37-242 |
1.78e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 90.08 E-value: 1.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 37 AIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKR-IGLLAQNATTPGDITVQELVARGRYPHQPLFTR 115
Cdd:COG1129 34 ALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAgIAIIHQELNLVPNLSVAENIFLGREPRRGGLID 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 116 WRKEDEEAvSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDiSHQID-LLELLSELnQQKG 194
Cdd:COG1129 114 WRAMRRRA-RELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLT-EREVErLFRIIRRL-KAQG 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490237141 195 ytlAAVL---HDLNQACRYATHLIALREGKIVAEGAPKEIVSAELIEKIYG 242
Cdd:COG1129 191 ---VAIIyisHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLMVG 238
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
18-234 |
2.08e-20 |
|
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: 90.13 E-value: 2.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 18 GKKTIAESLNVTIPDGHFTAIIGPNGCGKS----TLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAK----RIGLLAQN 89
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgnRIAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 90 ATTPGD--ITVQELVARGRYPHQPLFtrwRKEDEEAVSRAMKATGITDLAR-------QsvdtLSGGQRQRAWIAMVLAQ 160
Cdd:COG4172 101 PMTSLNplHTIGKQIAEVLRLHRGLS---GAAARARALELLERVGIPDPERrldayphQ----LSGGQRQRVMIAMALAN 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490237141 161 ETAIMLLDEPTTWLDISHQIDLLELLSELNQQKGytlAAVL---HDLNQACRYATHLIALREGKIVAEGAPKEIVSA 234
Cdd:COG4172 174 EPDLLIADEPTTALDVTVQAQILDLLKDLQRELG---MALLlitHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAA 247
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
8-207 |
3.34e-20 |
|
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: 85.62 E-value: 3.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 8 LRGDQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRyASKEVAKRIGLLA 87
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDF-QRDSIARGLLYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 88 QNATTPGDITVQELVargRYPHqplftrwRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
Cdd:cd03231 80 HAPGIKTTLSVLENL---RFWH-------ADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWIL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490237141 168 DEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQA 207
Cdd:cd03231 150 DEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLS 189
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
29-230 |
4.54e-20 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 87.48 E-value: 4.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 29 TIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQR--------------------YAS----KEVAKRIG 84
Cdd:COG4608 40 DIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGlsgrelrplrrrmqmvfqdpYASlnprMTVGDIIA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 85 --LLAQNATTPGDIT--VQELVAR--------GRYPHQplftrwrkedeeavsramkatgitdlarqsvdtLSGGQRQRA 152
Cdd:COG4608 120 epLRIHGLASKAERRerVAELLELvglrpehaDRYPHE---------------------------------FSGGQRQRI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 153 WIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNqACRYATHLIA---LreGKIVaEGAPK 229
Cdd:COG4608 167 GIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLS-VVRHISDRVAvmyL--GKIV-EIAPR 242
|
.
gi 490237141 230 E 230
Cdd:COG4608 243 D 243
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-239 |
5.42e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 86.60 E-value: 5.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 13 LTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIqryaskEVAKRiGLLA---QN 89
Cdd:PRK13638 7 LWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL------DYSKR-GLLAlrqQV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 90 ATTPGDitvqelvargryPHQPLFTRWRKED------------EEAVSRAMKATGITDLAR---QSVDTLSGGQRQRAWI 154
Cdd:PRK13638 80 ATVFQD------------PEQQIFYTDIDSDiafslrnlgvpeAEITRRVDEALTLVDAQHfrhQPIQCLSHGQKKRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 155 AMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVlHDLNQACRYATHLIALREGKIVAEGAPKEIVS- 233
Cdd:PRK13638 148 AGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISS-HDIDLIYEISDAVYVLRQGQILTHGAPGEVFAc 226
|
....*.
gi 490237141 234 AELIEK 239
Cdd:PRK13638 227 TEAMEQ 232
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
8-221 |
5.60e-20 |
|
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: 83.27 E-value: 5.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 8 LRGDQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVyldgEQIQRYaskevakRIGLLA 87
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV----TWGSTV-------KIGYFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 88 QnattpgditvqelvargryphqplftrwrkedeeavsramkatgitdlarqsvdtLSGGQRQRAWIAMVLAQETAIMLL 167
Cdd:cd03221 70 Q-------------------------------------------------------LSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490237141 168 DEPTTWLDISHqIDLLEllSELNQQKGyTLAAVLHD---LNQACryaTHLIALREGK 221
Cdd:cd03221 95 DEPTNHLDLES-IEALE--EALKEYPG-TVILVSHDryfLDQVA---TKIIELEDGK 144
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-231 |
8.24e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 85.86 E-value: 8.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 1 MTAVTSRLRGDQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRlMTPASGHVYLDGeQIQRYASKEVA 80
Cdd:PRK14258 1 MSKLIPAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNR-MNELESEVRVEG-RVEFFNQNIYE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 81 KRIGL------LAQNATTPG--DITVQELVARGRYphqplFTRWRK--EDEEAVSRAMKATGITDLAR----QSVDTLSG 146
Cdd:PRK14258 79 RRVNLnrlrrqVSMVHPKPNlfPMSVYDNVAYGVK-----IVGWRPklEIDDIVESALKDADLWDEIKhkihKSALDLSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 147 GQRQRAWIAMVLAQETAIMLLDEPTTWLD------ISHQIDLLELLSELnqqkgyTLAAVLHDLNQACRYAT-----HLI 215
Cdd:PRK14258 154 GQQQRLCIARALAVKPKVLLMDEPCFGLDpiasmkVESLIQSLRLRSEL------TMVIVSHNLHQVSRLSDftaffKGN 227
|
250
....*....|....*.
gi 490237141 216 ALREGKIVAEGAPKEI 231
Cdd:PRK14258 228 ENRIGQLVEFGLTKKI 243
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-225 |
1.73e-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: 82.48 E-value: 1.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 7 RLRGdqLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEvAKRIGLl 86
Cdd:cd03216 2 ELRG--ITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD-ARRAGI- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 87 aqnattpgditvqELVargrypHQplftrwrkedeeavsramkatgitdlarqsvdtLSGGQRQRAWIAMVLAQETAIML 166
Cdd:cd03216 78 -------------AMV------YQ---------------------------------LSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490237141 167 LDEPTTWLDISHQIDLLELLSELnQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAE 225
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
22-235 |
4.04e-19 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 86.33 E-value: 4.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 22 IAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIGLLAQ-NATTPGdiTVQE 100
Cdd:TIGR01846 472 VLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQeNVLFSR--SIRD 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 101 LVARGRyPHQPlftrwrkedEEAVSRAMKATGITDLA---RQSVDT--------LSGGQRQRAWIAMVLAQETAIMLLDE 169
Cdd:TIGR01846 550 NIALCN-PGAP---------FEHVIHAAKLAGAHDFIselPQGYNTevgekganLSGGQRQRIAIARALVGNPRILIFDE 619
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490237141 170 PTTWLDISHQIDLLELLSELNQqkGYTLAAVLHDLNqACRYATHLIALREGKIVAEGAPKEIVSAE 235
Cdd:TIGR01846 620 ATSALDYESEALIMRNMREICR--GRTVIIIAHRLS-TVRACDRIIVLEKGQIAESGRHEELLALQ 682
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
8-220 |
8.41e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 82.83 E-value: 8.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 8 LRGDQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYAskevAKRIGLLA 87
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG----AERGVVFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 88 QNATTPGDiTVQELVARGryphQPLFTRWRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
Cdd:PRK11248 78 NEGLLPWR-NVQDNVAFG----LQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490237141 168 DEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREG 220
Cdd:PRK11248 153 DEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
13-222 |
1.39e-18 |
|
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: 81.75 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 13 LTLAYGKKT---IAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIGLLAQN 89
Cdd:cd03248 17 VTFAYPTRPdtlVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 90 ATTPGDiTVQELVARGryphqpLFTRWRKEDEEAVSRAMKATGITDLArQSVDT--------LSGGQRQRAWIAMVLAQE 161
Cdd:cd03248 97 PVLFAR-SLQDNIAYG------LQSCSFECVKEAAQKAHAHSFISELA-SGYDTevgekgsqLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490237141 162 TAIMLLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAvlHDLNQACRyATHLIALREGKI 222
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIA--HRLSTVER-ADQILVLDGGRI 226
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
6-241 |
1.40e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 82.25 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 6 SRLRGDQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKR-IG 84
Cdd:PRK10895 2 ATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 85 LLAQNATTPGDITVQELVARGRYPHQPLFTRWRKEDEEAVSRAMKATGITDLARQSvdtLSGGQRQRAWIAMVLAQETAI 164
Cdd:PRK10895 82 YLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQS---LSGGERRRVEIARALAANPKF 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490237141 165 MLLDEPTTWLDISHQIDLLELLSELnQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVSAELIEKIY 241
Cdd:PRK10895 159 ILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVY 234
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
17-234 |
2.77e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 81.28 E-value: 2.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 17 YGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGeqiqryaskevakRIG-LLAQNATTPGD 95
Cdd:COG1134 36 REEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-------------RVSaLLELGAGFHPE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 96 ITVQE---LVAR--GRYPHQPLftrwRKEDE-EAVSramkatGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
Cdd:COG1134 103 LTGREniyLNGRllGLSRKEID----EKFDEiVEFA------ELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490237141 170 pttWL---DISHQIDLLELLSELnQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVSA 234
Cdd:COG1134 173 ---VLavgDAAFQKKCLARIREL-RESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
27-237 |
7.05e-18 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 81.77 E-value: 7.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 27 NVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAK---RIG-------LLAQNattpgdi 96
Cdd:PRK11153 25 SLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKarrQIGmifqhfnLLSSR------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 97 TVQELVArgryphQPL-FTRWRKEDEEA-VSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
Cdd:PRK11153 98 TVFDNVA------LPLeLAGTPKAEIKArVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSAL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490237141 175 D--ISHQIdlLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGA-------PKEIVSAELI 237
Cdd:PRK11153 172 DpaTTRSI--LELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTvsevfshPKHPLTREFI 241
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
13-223 |
7.21e-18 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 82.63 E-value: 7.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 13 LTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVyldgeqiqRYASKevaKRIGLLAQNATT 92
Cdd:PRK15064 325 LTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV--------KWSEN---ANIGYYAQDHAY 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 93 --PGDITVQELVArgryphqplftRWRKE-DEEAVSRAMKA----TGitDLARQSVDTLSGGQRQRAWIAMVLAQETAIM 165
Cdd:PRK15064 394 dfENDLTLFDWMS-----------QWRQEgDDEQAVRGTLGrllfSQ--DDIKKSVKVLSGGEKGRMLFGKLMMQKPNVL 460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490237141 166 LLDEPTTWLDIsHQIDLLELlsELNQQKGyTLAAVLHDLNQACRYATHLIALREGKIV 223
Cdd:PRK15064 461 VMDEPTNHMDM-ESIESLNM--ALEKYEG-TLIFVSHDREFVSSLATRIIEITPDGVV 514
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
8-226 |
8.90e-18 |
|
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: 80.26 E-value: 8.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 8 LRGDQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYL---DGEQIQRYASKEVAKRI- 83
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYimrSGAELELYQLSEAERRRl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 84 -----GLLAQNattPGDITVQELVARGRYPHQPL------FTRWRKEDEEAVSRA-MKATGITDLARqsvdTLSGGQRQR 151
Cdd:TIGR02323 84 mrtewGFVHQN---PRDGLRMRVSAGANIGERLMaigarhYGNIRATAQDWLEEVeIDPTRIDDLPR----AFSGGMQQR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490237141 152 AWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEG 226
Cdd:TIGR02323 157 LQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
8-226 |
1.10e-17 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 79.97 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 8 LRGDQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHV-YL--DGEQIQRYASKEVAKRI- 83
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhYRmrDGQLRDLYALSEAERRRl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 84 -----GLLAQNA-------TTPGDITVQELVARGRYPHQPL---FTRWRKEDEEAVSRamkatgITDLARqsvdTLSGGQ 148
Cdd:PRK11701 87 lrtewGFVHQHPrdglrmqVSAGGNIGERLMAVGARHYGDIratAGDWLERVEIDAAR------IDDLPT----TFSGGM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 149 RQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNQQKGytLAAVL--HDLNQACRYATHLIALREGKIVAEG 226
Cdd:PRK11701 157 QQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELG--LAVVIvtHDLAVARLLAHRLLVMKQGRVVESG 234
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
4-235 |
1.36e-17 |
|
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: 79.45 E-value: 1.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 4 VTSRLRGDQltlaygkKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRI 83
Cdd:cd03252 6 VRFRYKPDG-------PVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 84 GLLAQNATTPGDiTVQELVARGRyPHQPlftrwRKEDEEAVSRAMKATGITDLaRQSVDT--------LSGGQRQRAWIA 155
Cdd:cd03252 79 GVVLQENVLFNR-SIRDNIALAD-PGMS-----MERVIEAAKLAGAHDFISEL-PEGYDTivgeqgagLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 156 MVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNqqKGYTLAAVLHDLNqACRYATHLIALREGKIVAEGAPKEIVSAE 235
Cdd:cd03252 151 RALIHNPRILIFDEATSALDYESEHAIMRNMHDIC--AGRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDELLAEN 227
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
11-234 |
1.46e-17 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 80.56 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 11 DQLTLAYGKKTI----AESLNVTIPDGHFTAIIGPNGCGKST-------LLRTLSRLMTPAsghVYLDGEQIQRYASKEV 79
Cdd:PRK11022 7 DKLSVHFGDESApfraVDRISYSVKQGEVVGIVGESGSGKSVsslaimgLIDYPGRVMAEK---LEFNGQDLQRISEKER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 80 AKRIG----LLAQNATTPGD--ITVQELVARGRYPHQPLFTRWRKEdeeavsRA---MKATGITDLA-RQSV--DTLSGG 147
Cdd:PRK11022 84 RNLVGaevaMIFQDPMTSLNpcYTVGFQIMEAIKVHQGGNKKTRRQ------RAidlLNQVGIPDPAsRLDVypHQLSGG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 148 QRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGA 227
Cdd:PRK11022 158 MSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGK 237
|
....*..
gi 490237141 228 PKEIVSA 234
Cdd:PRK11022 238 AHDIFRA 244
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-204 |
3.23e-17 |
|
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: 78.56 E-value: 3.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 32 DGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHV-----------YLDGEQIQRYASKEVAKRIGLL--AQN-----ATTP 93
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeildEFRGSELQNYFTKLLEGDVKVIvkPQYvdlipKAVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 94 GdiTVQELVARgryphqplftrwrKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
Cdd:cd03236 105 G--KVGELLKK-------------KDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSY 169
|
170 180 190
....*....|....*....|....*....|.
gi 490237141 174 LDISHQIDLLELLSELNQQKGYTLaAVLHDL 204
Cdd:cd03236 170 LDIKQRLNAARLIRELAEDDNYVL-VVEHDL 199
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
6-234 |
4.36e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 78.20 E-value: 4.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 6 SRLRGDQLTLaYGKKTIAESLNVTIPDGHFTAIIGPNGCGKS----TLLRTLSRLMTPASGHVYLDGEQIQryASKEVAK 81
Cdd:PRK10418 3 QQIELRNIAL-QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVA--PCALRGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 82 RIGLLAQN---ATTPgditVQELVARGRyphQPLFTRWRKEDEEAVSRAMKATGITDLAR--QSVD-TLSGGQRQRAWIA 155
Cdd:PRK10418 80 KIATIMQNprsAFNP----LHTMHTHAR---ETCLALGKPADDATLTAALEAVGLENAARvlKLYPfEMSGGMLQRMMIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490237141 156 MVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVSA 234
Cdd:PRK10418 153 LALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNA 231
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
25-220 |
5.00e-17 |
|
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: 77.37 E-value: 5.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 25 SLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVY-----------LDGEQIQRYASKEVAKRIGLLaqNATTP 93
Cdd:cd03290 19 NINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnknesepsfEATRSRNRYSVAYAAQKPWLL--NATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 94 GDITVQELVARGRYphqplftrwrkedeEAVSRAMKATGITDLARQSVDT--------LSGGQRQRAWIAMVLAQETAIM 165
Cdd:cd03290 97 ENITFGSPFNKQRY--------------KAVTDACSLQPDIDLLPFGDQTeigerginLSGGQRQRICVARALYQNTNIV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490237141 166 LLDEPTTWLDIsHQIDLL--ELLSELNQQKGYTLAAVLHDLnQACRYATHLIALREG 220
Cdd:cd03290 163 FLDDPFSALDI-HLSDHLmqEGILKFLQDDKRTLVLVTHKL-QYLPHADWIIAMKDG 217
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
19-228 |
5.83e-17 |
|
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: 77.83 E-value: 5.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 19 KKTIAE-SLNV---TIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQrYASKEVakrigllaqNATTPG 94
Cdd:cd03237 7 KKTLGEfTLEVeggSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-YKPQYI---------KADYEG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 95 diTVQELVA---RGRYPHqplfTRWRKEdeeavsrAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
Cdd:cd03237 77 --TVRDLLSsitKDFYTH----PYFKTE-------IAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPS 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490237141 172 TWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLialregkIVAEGAP 228
Cdd:cd03237 144 AYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRL-------IVFEGEP 193
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
13-239 |
6.15e-17 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 77.41 E-value: 6.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 13 LTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTlsrLM-----TPASGHVYLDGEQIQRYASKEVAKR-IGLL 86
Cdd:COG0396 6 LHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKV---LMghpkyEVTSGSILLDGEDILELSPDERARAgIFLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 87 AQNATT-PGdITVQEL----VARGRYPHQPLFTrWRKEdeeaVSRAMKATGI-TDLARQSVD-TLSGGQRQRAWIAMVLA 159
Cdd:COG0396 83 FQYPVEiPG-VSVSNFlrtaLNARRGEELSARE-FLKL----LKEKMKELGLdEDFLDRYVNeGFSGGEKKRNEILQMLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 160 QETAIMLLDEPTTWLDishqIDLLELLSE-LNQqkgytlaavLHDLNQAC----------RY--ATHLIALREGKIVAEG 226
Cdd:COG0396 157 LEPKLAILDETDSGLD----IDALRIVAEgVNK---------LRSPDRGIliithyqrilDYikPDFVHVLVDGRIVKSG 223
|
250
....*....|...
gi 490237141 227 aPKEIvsAELIEK 239
Cdd:COG0396 224 -GKEL--ALELEE 233
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
24-240 |
1.18e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 77.82 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 24 ESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRyASKEVAKRIGLLAqnattpG-------DI 96
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFK-RRKEFARRIGVVF------GqrsqlwwDL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 97 TVQE----LVARGRYPHQplftRWRKEDEEAVSRamkaTGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
Cdd:COG4586 112 PAIDsfrlLKAIYRIPDA----EYKKRLDELVEL----LDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 173 WLDISHQIDLLELLSELNQQKGYTLaaVL--HDLN---QACRyatHLIALREGKIVAEG---------APKEIVSAELIE 238
Cdd:COG4586 184 GLDVVSKEAIREFLKEYNRERGTTI--LLtsHDMDdieALCD---RVIVIDHGRIIYDGsleelkerfGPYKTIVLELAE 258
|
..
gi 490237141 239 KI 240
Cdd:COG4586 259 PV 260
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
27-238 |
1.40e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.92 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 27 NVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKE-VAKRIGLLAQNATTPGDITVQELVARG 105
Cdd:COG3845 25 SLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaIALGIGMVHQHFMLVPNLTVAENIVLG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 106 RYPHQPLFTRWRKEDEEaVSRAMKATGIT-DLARQsVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLE 184
Cdd:COG3845 105 LEPTKGGRLDRKAARAR-IRELSERYGLDvDPDAK-VEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFE 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490237141 185 LLSELNQQkGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVSAELIE 238
Cdd:COG3845 183 ILRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELAE 235
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
27-204 |
1.52e-16 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 77.82 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 27 NVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASK---EVAKRIGLLAQNA-------TTPGDI 96
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDewrAVRSDIQMIFQDPlaslnprMTIGEI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 97 TVQELvaRGRYPHQPlftrwRKEDEEAVSRAMKATGI-TDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
Cdd:PRK15079 121 IAEPL--RTYHPKLS-----RQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
170 180
....*....|....*....|....*....
gi 490237141 176 ISHQIDLLELLSELNQQKGYTLAAVLHDL 204
Cdd:PRK15079 194 VSIQAQVVNLLQQLQREMGLSLIFIAHDL 222
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-242 |
2.61e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 77.90 E-value: 2.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 4 VTSRLRGDQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKR- 82
Cdd:PRK09700 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 83 IGLLAQNATTPGDITVQELVARGRYPHQPLF----TRWRKEDEEAvSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVL 158
Cdd:PRK09700 82 IGIIYQELSVIDELTVLENLYIGRHLTKKVCgvniIDWREMRVRA-AMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 159 AQETAIMLLDEPTTWLdISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVSAELIE 238
Cdd:PRK09700 161 MLDAKVIIMDEPTSSL-TNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVR 239
|
....
gi 490237141 239 KIYG 242
Cdd:PRK09700 240 LMVG 243
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
24-233 |
2.74e-16 |
|
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: 77.92 E-value: 2.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 24 ESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLD-GEQI-----QRYASKEVAKR-IGLLAQNATTpgdi 96
Cdd:TIGR03269 301 DNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWvdmtkPGPDGRGRAKRyIGILHQEYDL---- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 97 tvqelvargrYPHQPLFTRWRKE------DEEAVSRA---MKATGITDLARQSV-----DTLSGGQRQRAWIAMVLAQET 162
Cdd:TIGR03269 377 ----------YPHRTVLDNLTEAiglelpDELARMKAvitLKMVGFDEEKAEEIldkypDELSEGERHRVALAQVLIKEP 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 163 AIMLLDEPT------TWLDISHQIdlLELLSELNQqkgyTLAAVLHDL---NQACRYAThliALREGKIVAEGAPKEIVS 233
Cdd:TIGR03269 447 RIVILDEPTgtmdpiTKVDVTHSI--LKAREEMEQ----TFIIVSHDMdfvLDVCDRAA---LMRDGKIVKIGDPEEIVE 517
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
13-239 |
3.30e-16 |
|
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: 74.87 E-value: 3.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 13 LTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLM--TPASGHVYLDGEQIQRYASKEVAKR-IGLLAQN 89
Cdd:cd03217 6 LHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERARLgIFLAFQY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 90 attPGDItvqelvargryphqplftrwrkedeeavsramkaTGIT--DLARQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
Cdd:cd03217 86 ---PPEI----------------------------------PGVKnaDFLRYVNEGFSGGEKKRNEILQLLLLEPDLAIL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 168 DEPTTWLDishqIDLLELLSElnqqkgytLAAVLHDLNQACRYATHL--IA----------LREGKIVAEGaPKEIvsAE 235
Cdd:cd03217 129 DEPDSGLD----IDALRLVAE--------VINKLREEGKSVLIITHYqrLLdyikpdrvhvLYDGRIVKSG-DKEL--AL 193
|
....
gi 490237141 236 LIEK 239
Cdd:cd03217 194 EIEK 197
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
26-235 |
3.75e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 77.56 E-value: 3.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 26 LNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIGLLAQ-----NATTPGDItvqe 100
Cdd:PRK11160 359 LSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQrvhlfSATLRDNL---- 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 101 LVArgryphQPlftrwrKEDEEAVSRAMKATGITDLA--RQSVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEP 170
Cdd:PRK11160 435 LLA------AP------NASDEALIEVLQQVGLEKLLedDKGLNAwlgeggrqLSGGEQRRLGIARALLHDAPLLLLDEP 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490237141 171 TTWLDISHQIDLLELLSELNQQKgyTLAAVLHDLNqACRYATHLIALREGKIVAEGAPKEIVSAE 235
Cdd:PRK11160 503 TEGLDAETERQILELLAEHAQNK--TVLMITHRLT-GLEQFDRICVMDNGQIIEQGTHQELLAQQ 564
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
17-228 |
7.94e-16 |
|
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: 76.98 E-value: 7.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 17 YGKKTIaESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRyASKEVAKRIGLLAQNATTPGDI 96
Cdd:TIGR01257 941 SGRPAV-DRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHHL 1018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 97 TVQElvargrypHQPLFTRWRKEDEEAVSRAMKA----TGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
Cdd:TIGR01257 1019 TVAE--------HILFYAQLKGRSWEEAQLEMEAmledTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTS 1090
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490237141 173 WLDISHQIDLLELLseLNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAP 228
Cdd:TIGR01257 1091 GVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-204 |
8.00e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 76.77 E-value: 8.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 32 DGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDG---EQIQRYASKEVAKRIGLLAQNATTPG-------------D 95
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPswdEVLKRFRGTELQNYFKKLYNGEIKVVhkpqyvdlipkvfK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 96 ITVQELVARgryphqplfTRWRKEDEEAVSRamkaTGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
Cdd:PRK13409 178 GKVRELLKK---------VDERGKLDEVVER----LGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
170 180
....*....|....*....|....*....
gi 490237141 176 ISHQIDLLELLSELNQQKgYTLaAVLHDL 204
Cdd:PRK13409 245 IRQRLNVARLIRELAEGK-YVL-VVEHDL 271
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
11-235 |
1.06e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 76.30 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 11 DQLTLAYGK-KTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIGLLAQN 89
Cdd:PRK10790 344 DNVSFAYRDdNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQD 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 90 ATTPGDiTVQELVARGryphqplftrwRKEDEEAVSRAMKATGITDLARQSVD-----------TLSGGQRQRAWIAMVL 158
Cdd:PRK10790 424 PVVLAD-TFLANVTLG-----------RDISEEQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALARVL 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490237141 159 AQETAIMLLDEPTTWLDISHQIDLLELLSELNQQKgyTLAAVLHDLNQACRyATHLIALREGKIVAEGAPKEIVSAE 235
Cdd:PRK10790 492 VQTPQILILDEATANIDSGTEQAIQQALAAVREHT--TLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLLAAQ 565
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
37-204 |
1.21e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 75.39 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 37 AIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVA---KRIGLLAQNA-------TTPGDI---------- 96
Cdd:PRK11308 45 AVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKllrQKIQIVFQNPygslnprKKVGQIleepllints 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 97 --------TVQELVAR--------GRYPHqpLFtrwrkedeeavsramkatgitdlarqsvdtlSGGQRQRAWIAMVLAQ 160
Cdd:PRK11308 125 lsaaerreKALAMMAKvglrpehyDRYPH--MF-------------------------------SGGQRQRIAIARALML 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490237141 161 ETAIMLLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDL 204
Cdd:PRK11308 172 DPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDL 215
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
6-188 |
1.28e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 76.00 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 6 SRLRGDQLTLA-YGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHvyldgeqIQRYASKEVAkrig 84
Cdd:COG4178 361 GALALEDLTLRtPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGR-------IARPAGARVL---- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 85 LLAQNATTPGDiTVQELVArgrYPHQPlftrwRKEDEEAVSRAMKATGITDLARQsVDT-------LSGGQRQRAWIAMV 157
Cdd:COG4178 430 FLPQRPYLPLG-TLREALL---YPATA-----EAFSDAELREALEAVGLGHLAER-LDEeadwdqvLSLGEQQRLAFARL 499
|
170 180 190
....*....|....*....|....*....|.
gi 490237141 158 LAQETAIMLLDEPTTWLDISHQIDLLELLSE 188
Cdd:COG4178 500 LLHKPDWLFLDEATSALDEENEAALYQLLRE 530
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
15-235 |
1.39e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 76.04 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 15 LAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMtPASGHVYLDGEQIQRYASKEVAKRIGLLAQNATTPG 94
Cdd:PRK11174 358 LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPH 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 95 DiTVQELVARGRyPHQplftrwrkeDEEAVSRAMKATGITD-LARQS--VDT--------LSGGQRQRAWIAMVLAQETA 163
Cdd:PRK11174 437 G-TLRDNVLLGN-PDA---------SDEQLQQALENAWVSEfLPLLPqgLDTpigdqaagLSVGQAQRLALARALLQPCQ 505
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490237141 164 IMLLDEPTTWLDISHQIDLLELLSELNQQKgyTLAAVLHDLNQACRYATHLIaLREGKIVAEGAPKEIVSAE 235
Cdd:PRK11174 506 LLLLDEPTASLDAHSEQLVMQALNAASRRQ--TTLMVTHQLEDLAQWDQIWV-MQDGQIVQQGDYAELSQAG 574
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
7-226 |
3.19e-15 |
|
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: 74.98 E-value: 3.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 7 RLRG----DQLTLAYG--KKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVA 80
Cdd:TIGR03796 473 RLSGyvelRNITFGYSplEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLA 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 81 KRIGLLAQnattpgDI-----TVQELVargryphqplfTRW-RKEDEEAVSRAMKATGITD--LAR---------QSVDT 143
Cdd:TIGR03796 553 NSVAMVDQ------DIflfegTVRDNL-----------TLWdPTIPDADLVRACKDAAIHDviTSRpggydaelaEGGAN 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 144 LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLselnQQKGYTLAAVLHDLNqACRYATHLIALREGKIV 223
Cdd:TIGR03796 616 LSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNL----RRRGCTCIIVAHRLS-TIRDCDEIIVLERGKVV 690
|
...
gi 490237141 224 AEG 226
Cdd:TIGR03796 691 QRG 693
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
11-234 |
3.20e-15 |
|
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: 75.16 E-value: 3.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 11 DQLTLAYG-KKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIGLLAQn 89
Cdd:TIGR01193 477 NDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQ- 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 90 attpgditvQELVARGRYPHQPLFTRWRKEDEEAVSRAMKATGI------------TDLARQSvDTLSGGQRQRAWIAMV 157
Cdd:TIGR01193 556 ---------EPYIFSGSILENLLLGAKENVSQDEIWAACEIAEIkddienmplgyqTELSEEG-SSISGGQKQRIALARA 625
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490237141 158 LAQETAIMLLDEPTTWLDISHQIDLLELLSELNQQkgyTLAAVLHDLNQACRyATHLIALREGKIVAEGAPKEIVSA 234
Cdd:TIGR01193 626 LLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDELLDR 698
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
11-234 |
3.90e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 72.84 E-value: 3.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 11 DQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGhvyldgeQIQRyaskEVAKRIGLLAQNA 90
Cdd:PRK09544 8 ENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG-------VIKR----NGKLRIGYVPQKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 91 TTpgDITVQELVARgryphqplFTRWRKEDEEA-VSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
Cdd:PRK09544 77 YL--DTTLPLTVNR--------FLRLRPGTKKEdILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDE 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490237141 170 PTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALrEGKIVAEGAPkEIVSA 234
Cdd:PRK09544 147 PTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTP-EVVSL 209
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
33-204 |
7.36e-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: 73.67 E-value: 7.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 33 GHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQ---IQRYASKEVAKRIGLLAQnattpGDITV----Q--ELVA 103
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPSWdevLKRFRGTELQDYFKKLAN-----GEIKVahkpQyvDLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 104 R---GRyphqplfTR--WRKEDEEAVSR-AMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS 177
Cdd:COG1245 174 KvfkGT-------VRelLEKVDERGKLDeLAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIY 246
|
170 180
....*....|....*....|....*..
gi 490237141 178 HQIDLLELLSELNQQKGYTLaAVLHDL 204
Cdd:COG1245 247 QRLNVARLIRELAEEGKYVL-VVEHDL 272
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
8-241 |
7.37e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 71.83 E-value: 7.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 8 LRGDQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKR-IGLL 86
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREaVAIV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 87 AQNATTPGDITVQELVARGRyphqplFTRWRKEDEEAVSRAMKA-TGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIM 165
Cdd:PRK11614 86 PEGRRVFSRMTVEENLAMGG------FFAERDQFQERIKWVYELfPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490237141 166 LLDEPTTWLD--ISHQI-DLLELLSElnqqKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVSAELIEKIY 241
Cdd:PRK11614 160 LLDEPSLGLApiIIQQIfDTIEQLRE----QGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAY 234
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
8-231 |
7.59e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 72.96 E-value: 7.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 8 LRGDQLTLAYGKKTIAESlnVTIPDGHFT-------AIIGPNGCGKSTLLRTLSRLMTPASGHV---------------- 64
Cdd:PRK13631 22 LRVKNLYCVFDEKQENEL--VALNNISYTfeknkiyFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyigdkknnhel 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 65 --YLDGEQIQRYasKEVAKRIGLLAQnattpgditvqelvargrYPHQPLFTRWRKED------------EEAVSRA--- 127
Cdd:PRK13631 100 itNPYSKKIKNF--KELRRRVSMVFQ------------------FPEYQLFKDTIEKDimfgpvalgvkkSEAKKLAkfy 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 128 MKATGITD--LARQSVDtLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNQQkGYTLAAVLHDLN 205
Cdd:PRK13631 160 LNKMGLDDsyLERSPFG-LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTME 237
|
250 260
....*....|....*....|....*.
gi 490237141 206 QACRYATHLIALREGKIVAEGAPKEI 231
Cdd:PRK13631 238 HVLEVADEVIVMDKGKILKTGTPYEI 263
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
17-226 |
9.54e-15 |
|
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: 71.02 E-value: 9.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 17 YGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGeqiqryaskEVAkriGLLAQNATTPGDI 96
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG---------RVS---SLLGLGGGFNPEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 97 TVQE---LVARgryphqpLFTRWRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEpttW 173
Cdd:cd03220 100 TGREniyLNGR-------LLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDE---V 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490237141 174 L---DISHQIDLLELLSELnQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEG 226
Cdd:cd03220 170 LavgDAAFQEKCQRRLREL-LKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
26-231 |
1.21e-14 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 72.57 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 26 LNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRyasKEVAKR-IGLLAQN-ATTPgDITVQELVA 103
Cdd:PRK11650 23 IDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNE---LEPADRdIAMVFQNyALYP-HMSVRENMA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 104 RGryphqpLFTRW--RKEDEEAVSRAMKATGITDL----ARQsvdtLSGGQRQRawIAM--VLAQETAIMLLDEPTTWLD 175
Cdd:PRK11650 99 YG------LKIRGmpKAEIEERVAEAARILELEPLldrkPRE----LSGGQRQR--VAMgrAIVREPAVFLFDEPLSNLD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490237141 176 ISHQIDL-LELLsELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEI 231
Cdd:PRK11650 167 AKLRVQMrLEIQ-RLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEV 222
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
18-232 |
2.52e-14 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 72.30 E-value: 2.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 18 GKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIGLLAQNATtpgdit 97
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAG------ 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 98 vqelvargryphqpLFTR-------WRKED--EEAVSRAMKATGITD-LARQS--VDT--------LSGGQRQRAWIAMV 157
Cdd:PRK13657 420 --------------LFNRsiednirVGRPDatDEEMRAAAERAQAHDfIERKPdgYDTvvgergrqLSGGERQRLAIARA 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490237141 158 LAQETAIMLLDEPTTWLDISHQIDLLELLSELnqQKGYTLAAVLHDLNqACRYATHLIALREGKIVAEGAPKEIV 232
Cdd:PRK13657 486 LLKDPPILILDEATSALDVETEAKVKAALDEL--MKGRTTFIIAHRLS-TVRNADRILVFDNGRVVESGSFDELV 557
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
24-221 |
5.74e-14 |
|
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: 68.65 E-value: 5.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 24 ESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYldgeqiqryaskeVAKRIGLLAQ-----NAttpgdiTV 98
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVS-------------VPGSIAYVSQepwiqNG------TI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 99 QELVargryphqpLFTrwRKEDEEAVSRAMKATGI-TDLArQSVD-----------TLSGGQRQRAWIAMVLAQETAIML 166
Cdd:cd03250 83 RENI---------LFG--KPFDEERYEKVIKACALePDLE-ILPDgdlteigekgiNLSGGQKQRISLARAVYSDADIYL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490237141 167 LDEPTTWLDI---SHQIDLLeLLSELNQQKgyTLAAVLHDLnQACRYATHLIALREGK 221
Cdd:cd03250 151 LDDPLSAVDAhvgRHIFENC-ILGLLLNNK--TRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
131-234 |
6.48e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 70.89 E-value: 6.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 131 TGITDLARQSVD---TLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQA 207
Cdd:PRK15134 141 VGIRQAAKRLTDyphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIV 220
|
90 100
....*....|....*....|....*..
gi 490237141 208 CRYATHLIALREGKIVAEGAPKEIVSA 234
Cdd:PRK15134 221 RKLADRVAVMQNGRCVEQNRAATLFSA 247
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
26-230 |
6.73e-14 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 70.91 E-value: 6.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 26 LNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAK-----------RIGLL-----AQN 89
Cdd:PRK10535 27 ISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQlrrehfgfifqRYHLLshltaAQN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 90 ATTPGDITVQELVARgRYPHQPLFTRwrkedeeavsramkaTGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
Cdd:PRK10535 107 VEVPAVYAGLERKQR-LLRAQELLQR---------------LGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490237141 170 PTTWLDISHQIDLLELLSELNQQkGYTLAAVLHDLNQACRyATHLIALREGKIVAEGAPKE 230
Cdd:PRK10535 171 PTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPPAQE 229
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
24-234 |
6.83e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 71.04 E-value: 6.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 24 ESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKR--------------IGLLAQN 89
Cdd:PRK10261 33 RNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVIELSeqsaaqmrhvrgadMAMIFQE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 90 ATTPGD--ITVQELVARGRYPHQPLftrWRKEDEEAVSRAMKATGITD----LARQSvDTLSGGQRQRAWIAMVLAQETA 163
Cdd:PRK10261 113 PMTSLNpvFTVGEQIAESIRLHQGA---SREEAMVEAKRMLDQVRIPEaqtiLSRYP-HQLSGGMRQRVMIAMALSCRPA 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490237141 164 IMLLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVSA 234
Cdd:PRK10261 189 VLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHA 259
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
43-242 |
7.90e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 70.82 E-value: 7.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 43 GCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKE-VAKRIGLL---------------AQNATtpgdITVQELVARGR 106
Cdd:COG1129 288 GAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRAGIAYVpedrkgeglvldlsiRENIT----LASLDRLSRGG 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 107 yphqplFTRWRKEdEEAVSRAMKATGI-TDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLEL 185
Cdd:COG1129 364 ------LLDRRRE-RALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRL 436
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 186 LSELNQQkGytlAAVL---HDLNQACRYATHLIALREGKIVAEGAPKEIVSAELIEKIYG 242
Cdd:COG1129 437 IRELAAE-G---KAVIvisSELPELLGLSDRILVMREGRIVGELDREEATEEAIMAAATG 492
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
33-204 |
9.33e-14 |
|
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: 68.61 E-value: 9.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 33 GHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYL--DGEQIQ--RYASKEV----AKRIGLLAQNATTPGDITVQELVAr 104
Cdd:COG4778 37 GECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDlaQASPREIlalrRRTIGYVSQFLRVIPRVSALDVVA- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 105 gryphQPLFtRWRKEDEEAVSRAMKAtgitdLARQSVD---------TLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
Cdd:COG4778 116 -----EPLL-ERGVDREEARARAREL-----LARLNLPerlwdlppaTFSGGEQQRVNIARGFIADPPLLLLDEPTASLD 184
|
170 180
....*....|....*....|....*....
gi 490237141 176 ISHQIDLLELLSELnQQKGYTLAAVLHDL 204
Cdd:COG4778 185 AANRAVVVELIEEA-KARGTAIIGIFHDE 212
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
38-204 |
2.07e-13 |
|
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: 69.43 E-value: 2.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 38 IIGPNGCGKSTLLRTLSRLMTPASGHVYLDgeqiqryaskevaKRIGLLAQNATTPGDITVQELVaRGRYPhQPLFTRWR 117
Cdd:COG1245 371 IVGPNGIGKTTFAKILAGVLKPDEGEVDED-------------LKISYKPQYISPDYDGTVEEFL-RSANT-DDFGSSYY 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 118 KEDeeaVSRAMkatGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNQQKGYTL 197
Cdd:COG1245 436 KTE---IIKPL---GLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTA 509
|
....*..
gi 490237141 198 AAVLHDL 204
Cdd:COG1245 510 MVVDHDI 516
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
13-176 |
2.32e-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: 69.19 E-value: 2.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 13 LTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLdGEQIQryaskevakrIGLLAQN-AT 91
Cdd:TIGR03719 328 LTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK----------LAYVDQSrDA 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 92 TPGDITVQELVARGrYPHQPLFTRwrkedeEAVSRAMkatgitdLAR---------QSVDTLSGGQRQRAWIAMVLAQET 162
Cdd:TIGR03719 397 LDPNKTVWEEISGG-LDIIKLGKR------EIPSRAY-------VGRfnfkgsdqqKKVGQLSGGERNRVHLAKTLKSGG 462
|
170
....*....|....
gi 490237141 163 AIMLLDEPTTWLDI 176
Cdd:TIGR03719 463 NVLLLDEPTNDLDV 476
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
8-175 |
2.72e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 66.75 E-value: 2.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 8 LRGDQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYaskevakriglla 87
Cdd:PRK13538 2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQ------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 88 qnattpGDITVQELVARGrypHQP----LFTRW----------RKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAW 153
Cdd:PRK13538 69 ------RDEYHQDLLYLG---HQPgiktELTALenlrfyqrlhGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVA 139
|
170 180
....*....|....*....|..
gi 490237141 154 IAMVLAQETAIMLLDEPTTWLD 175
Cdd:PRK13538 140 LARLWLTRAPLWILDEPFTAID 161
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
24-236 |
3.98e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 67.51 E-value: 3.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 24 ESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIGLLAQNATTpgditvqELVA 103
Cdd:PRK15112 30 KPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPST-------SLNP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 104 RGRYpHQPLFTRWR-------KEDEEAVSRAMKATGI-TDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
Cdd:PRK15112 103 RQRI-SQILDFPLRlntdlepEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLD 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490237141 176 ISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVSAEL 236
Cdd:PRK15112 182 MSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPL 242
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
7-226 |
4.29e-13 |
|
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: 68.69 E-value: 4.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 7 RLRGDQLTLAY-GKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIGL 85
Cdd:COG5265 357 EVRFENVSFGYdPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGI 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 86 LAQ-----NATtpgditVQELVARGRyPHQplftrwrkeDEEAVSRAMKATGITDLAR---QSVDT--------LSGGQR 149
Cdd:COG5265 437 VPQdtvlfNDT------IAYNIAYGR-PDA---------SEEEVEAAARAAQIHDFIEslpDGYDTrvgerglkLSGGEK 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 150 QRAWIAMVLAQETAIMLLDEPTTWLDiSH--QidllELLSELNQ-QKGYTLAAVLHDLNQAcRYATHLIALREGKIVAEG 226
Cdd:COG5265 501 QRVAIARTLLKNPPILIFDEATSALD-SRteR----AIQAALREvARGRTTLVIAHRLSTI-VDADEILVLEAGRIVERG 574
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
33-256 |
4.88e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 68.54 E-value: 4.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 33 GHFTAIIGPNGCGKSTLLRTLS-RLMT--PASGHVYLDGEQIQRyasKEVAKRIGLLAQNATTPGDITVQE---LVARGR 106
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAfRSPKgvKGSGSVLLNGMPIDA---KEMRAISAYVQQDDLFIPTLTVREhlmFQAHLR 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 107 YPHQPlftrWRKEDEEAVSRAMKATGITDLAR------QSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQI 180
Cdd:TIGR00955 128 MPRRV----TKKEKRERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAY 203
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490237141 181 DLLELLSELnQQKGYTLAAVLHD-LNQACRYATHLIALREGKIVAEGAPKEivSAELIEKIyGLRCtiiedPVAHTP 256
Cdd:TIGR00955 204 SVVQVLKGL-AQKGKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQ--AVPFFSDL-GHPC-----PENYNP 271
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
11-176 |
5.00e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 68.22 E-value: 5.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 11 DQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLdGEQIQryaskevakrIGLLAQN- 89
Cdd:PRK11819 328 ENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVK----------LAYVDQSr 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 90 ATTPGDITVQELVARGryphqplftrwrkEDE------EAVSRAMkatgitdLAR---------QSVDTLSGGQRQRAWI 154
Cdd:PRK11819 397 DALDPNKTVWEEISGG-------------LDIikvgnrEIPSRAY-------VGRfnfkggdqqKKVGVLSGGERNRLHL 456
|
170 180
....*....|....*....|..
gi 490237141 155 AMVLAQETAIMLLDEPTTWLDI 176
Cdd:PRK11819 457 AKTLKQGGNVLLLDEPTNDLDV 478
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
19-233 |
5.96e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 68.37 E-value: 5.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 19 KKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLS-RLMTPA-SGHVYLDGEQIqryaSKEVAKRIGLLAQNATTPGDI 96
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANNRKP----TKQILKRTGFVTQDDILYPHL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 97 TVQE---LVARGRYPHqplfTRWRKEDEEAVSRAMKATGITD-----LARQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168
Cdd:PLN03211 156 TVREtlvFCSLLRLPK----SLTKQEKILVAESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILD 231
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490237141 169 EPTTWLDISHQIDLLELLSELnQQKGYTLAAVLHDLNQACRYATH-LIALREGKIVAEGAPKEIVS 233
Cdd:PLN03211 232 EPTSGLDATAAYRLVLTLGSL-AQKGKTIVTSMHQPSSRVYQMFDsVLVLSEGRCLFFGKGSDAMA 296
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
26-231 |
6.35e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 67.59 E-value: 6.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 26 LNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDG-------EQIQRYASKevaKRIGLLAQNAttpgditv 98
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaeKGICLPPEK---RRIGYVFQDA-------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 99 qelvargR-YPHQplftRWRKEDEEAVSRAMKAT--------GITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
Cdd:PRK11144 86 -------RlFPHY----KVRGNLRYGMAKSMVAQfdkivallGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490237141 170 PTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEI 231
Cdd:PRK11144 155 PLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
25-244 |
6.63e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.11 E-value: 6.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 25 SLNVTipDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRY---ASKEVAkrIGLLAQNATTPGDITVQEL 101
Cdd:PRK10762 24 ALNVY--PGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNgpkSSQEAG--IGIIHQELNLIPQLTIAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 102 VARGRYPHQPlFTR--WRKEDEEAvSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQ 179
Cdd:PRK10762 100 IFLGREFVNR-FGRidWKKMYAEA-DKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTET 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490237141 180 IDLLELLSELNQQkGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVSAELIEKIYGLR 244
Cdd:PRK10762 178 ESLFRVIRELKSQ-GRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTEDSLIEMMVGRK 241
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
18-176 |
6.76e-13 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 67.96 E-value: 6.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 18 GKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYldgeqiqryASKEVakRIGLLAQNATTPGDIT 97
Cdd:PLN03073 520 GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF---------RSAKV--RMAVFSQHHVDGLDLS 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 98 VQELVARGR-YPHQPlftrwrkedEEAVSRAMKATGIT-DLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
Cdd:PLN03073 589 SNPLLYMMRcFPGVP---------EQKLRAHLGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
.
gi 490237141 176 I 176
Cdd:PLN03073 660 L 660
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
13-222 |
8.64e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 67.61 E-value: 8.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 13 LTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVyldgeqiqryaSKEVAKRIGLLAQNATT 92
Cdd:PRK15064 7 ITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNV-----------SLDPNERLGKLRQDQFA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 93 PGDITVQELVARGrypHQPLftrWR-KEDEEAV--------SRAMKAT----------GITDLARQSvDTLSG------- 146
Cdd:PRK15064 76 FEEFTVLDTVIMG---HTEL---WEvKQERDRIyalpemseEDGMKVAdlevkfaemdGYTAEARAG-ELLLGvgipeeq 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 147 ----------GQRQRAWIAMVLAQETAIMLLDEPTTWLDIsHQIDLLEllSELNQQKGyTLAAVLHD---LNQACryaTH 213
Cdd:PRK15064 149 hyglmsevapGWKLRVLLAQALFSNPDILLLDEPTNNLDI-NTIRWLE--DVLNERNS-TMIIISHDrhfLNSVC---TH 221
|
....*....
gi 490237141 214 LIALREGKI 222
Cdd:PRK15064 222 MADLDYGEL 230
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
11-203 |
1.01e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 67.67 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 11 DQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLdGEQIqryaskEVA----KRIGLl 86
Cdd:PRK11147 323 ENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKL------EVAyfdqHRAEL- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 87 aqnatTPgDITVQELVARGryphqplftrwrKEDEEAVSRAMKATG-ITDL------ARQSVDTLSGGQRQRAWIAMVLA 159
Cdd:PRK11147 395 -----DP-EKTVMDNLAEG------------KQEVMVNGRPRHVLGyLQDFlfhpkrAMTPVKALSGGERNRLLLARLFL 456
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490237141 160 QETAIMLLDEPTTWLDishqIDLLELLSELNQQKGYTLAAVLHD 203
Cdd:PRK11147 457 KPSNLLILDEPTNDLD----VETLELLEELLDSYQGTVLLVSHD 496
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
38-180 |
1.69e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 66.76 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 38 IIGPNGCGKSTLLRTLSRLMTPASGHVyldgeqiqryaSKEVakRIGLLAQNATTPGDITVQELVARGRyphQPLFTRWR 117
Cdd:PRK13409 370 IVGPNGIGKTTFAKLLAGVLKPDEGEV-----------DPEL--KISYKPQYIKPDYDGTVEDLLRSIT---DDLGSSYY 433
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490237141 118 KEDeeavsrAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQI 180
Cdd:PRK13409 434 KSE------IIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRL 490
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
8-233 |
3.36e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 65.98 E-value: 3.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 8 LRGDQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRL--MTPASGHV-----------YLD-----GE 69
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgYVErpskvGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 70 QIQRYAS-----------------KEVAKRIGLLAQNA-TTPGDITVQELVARGRypHQPLFtrwrkEDEEAVSRAMK-- 129
Cdd:TIGR03269 81 PCPVCGGtlepeevdfwnlsdklrRRIRKRIAIMLQRTfALYGDDTVLDNVLEAL--EEIGY-----EGKEAVGRAVDli 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 130 -----ATGITDLARQsvdtLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDL 204
Cdd:TIGR03269 154 emvqlSHRITHIARD----LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWP 229
|
250 260
....*....|....*....|....*....
gi 490237141 205 NQACRYATHLIALREGKIVAEGAPKEIVS 233
Cdd:TIGR03269 230 EVIEDLSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
27-257 |
3.74e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 65.81 E-value: 3.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 27 NVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGH--------VYLDGEQIQRYASKEVAKR-IGLLAQNATTPGDiT 97
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGErqsqfshiTRLSFEQLQKLVSDEWQRNnTDMLSPGEDDTGR-T 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 98 VQELVARGryphqplftrwrKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS 177
Cdd:PRK10938 102 TAEIIQDE------------VKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 178 HQIDLLELLSELNQQkGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVSAELI------EKIYGLRCTIIEDP 251
Cdd:PRK10938 170 SRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQALVaqlahsEQLEGVQLPEPDEP 248
|
....*.
gi 490237141 252 VAHTPL 257
Cdd:PRK10938 249 SARHAL 254
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
18-204 |
6.04e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 64.75 E-value: 6.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 18 GKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTP---ASGHVYLDGEQIQRYASKEV----AKRIGLLAQNA 90
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPEKELnklrAEQISMIFQDP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 91 TTP-------GDITVQELVARGRYPHQPLFtrwrkedEEAVsRAMKATGITDlARQSVDT----LSGGQRQRAWIAMVLA 159
Cdd:PRK09473 107 MTSlnpymrvGEQLMEVLMLHKGMSKAEAF-------EESV-RMLDAVKMPE-ARKRMKMypheFSGGMRQRVMIAMALL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490237141 160 QETAIMLLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDL 204
Cdd:PRK09473 178 CRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDL 222
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
37-244 |
7.79e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 64.55 E-value: 7.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 37 AIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQiQRYAS--KEVAKRIGLLAQNATTPGDITVQELVARGRYPHQPLFT 114
Cdd:PRK11288 34 ALMGENGAGKSTLLKILSGNYQPDAGSILIDGQE-MRFASttAALAAGVAIIYQELHLVPEMTVAENLYLGQLPHKGGIV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 115 RwRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDiSHQID-LLELLSELNQQk 193
Cdd:PRK11288 113 N-RRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLS-AREIEqLFRVIRELRAE- 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 194 GYTLAAVLHDLNQACRYATHLIALREGKIVA-----EGAPKEIVSAEL----IEKIYGLR 244
Cdd:PRK11288 190 GRVILYVSHRMEEIFALCDAITVFKDGRYVAtfddmAQVDRDQLVQAMvgreIGDIYGYR 249
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
27-242 |
1.06e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 64.37 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 27 NVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKR-IGLLAQNATTPGDITVQELVARG 105
Cdd:PRK10982 18 NLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENgISMVHQELNLVLQRSVMDNMWLG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 106 RYPHQPLFTrwrkeDEEAVSRAMKAT----GITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL---DISH 178
Cdd:PRK10982 98 RYPTKGMFV-----DQDKMYRDTKAIfdelDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLtekEVNH 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490237141 179 QIDLLELLSElnqqKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVSAELIEKIYG 242
Cdd:PRK10982 173 LFTIIRKLKE----RGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIAMMVG 232
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
26-243 |
1.19e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 64.58 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 26 LNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIGLLAQNATTPGDITVQELVARG 105
Cdd:TIGR00957 1305 INVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFS 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 106 RYPHQPLFTRWRKEDEEAVSRAMKAtGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIshQIDLLEL 185
Cdd:TIGR00957 1385 QYSDEEVWWALELAHLKTFVSALPD-KLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDL--ETDNLIQ 1461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490237141 186 LSELNQQKGYTLAAVLHDLNQACRYaTHLIALREGKIVAEGAPKEIVSAELIekIYGL 243
Cdd:TIGR00957 1462 STIRTQFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEVAEFGAPSNLLQQRGI--FYSM 1516
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
18-242 |
1.75e-11 |
|
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: 62.28 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 18 GKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTL----SRLMTpaSGHVYLDGEQIQRYASKEVAkRIGL-LA-QNAT 91
Cdd:TIGR01978 11 EDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIaghpSYEVT--SGTILFKGQDLLELEPDERA-RAGLfLAfQYPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 92 -TPGdITVQELV-----ARGRYPHQPLFTR--WRKEdeeaVSRAMKATGIT-DLARQSVDT-LSGGQRQRAWIAMVLAQE 161
Cdd:TIGR01978 88 eIPG-VSNLEFLrsalnARRSARGEEPLDLldFEKL----LKEKLALLDMDeEFLNRSVNEgFSGGEKKRNEILQMALLE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 162 TAIMLLDEPTTWLDishqIDLLELLSE-LNQQKGYTLAAVLHDLNQacRYATHLI-----ALREGKIVAEGAPkEIVSaE 235
Cdd:TIGR01978 163 PKLAILDEIDSGLD----IDALKIVAEgINRLREPDRSFLIITHYQ--RLLNYIKpdyvhVLLDGRIVKSGDV-ELAK-E 234
|
....*..
gi 490237141 236 LIEKIYG 242
Cdd:TIGR01978 235 LEAKGYD 241
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
8-178 |
3.25e-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: 63.43 E-value: 3.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 8 LRGDQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEqiqryaskevakrIGLLA 87
Cdd:TIGR00957 639 VHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAYVP 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 88 QNATTPGDiTVQELVARGRyphqPLFTRWRKEDEEAVS-----RAMKATGITDLARQSVDtLSGGQRQRAWIAMVLAQET 162
Cdd:TIGR00957 706 QQAWIQND-SLRENILFGK----ALNEKYYQQVLEACAllpdlEILPSGDRTEIGEKGVN-LSGGQKQRVSLARAVYSNA 779
|
170
....*....|....*.
gi 490237141 163 AIMLLDEPTTWLDiSH 178
Cdd:TIGR00957 780 DIYLFDDPLSAVD-AH 794
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
11-176 |
3.83e-11 |
|
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: 60.97 E-value: 3.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 11 DQLTLAY--GKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIGLLAQ 88
Cdd:cd03244 6 KNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 89 NATT-PGdiTVQE-LVARGRYphqplftrwrkeDEEAVSRAMKATGITDLARQSVDTL-----------SGGQRQRAWIA 155
Cdd:cd03244 86 DPVLfSG--TIRSnLDPFGEY------------SDEELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLA 151
|
170 180
....*....|....*....|.
gi 490237141 156 MVLAQETAIMLLDEPTTWLDI 176
Cdd:cd03244 152 RALLRKSKILVLDEATASVDP 172
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
5-240 |
5.55e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 62.30 E-value: 5.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 5 TSRLRGdqLTLAYGKKTIA-ESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRI 83
Cdd:PRK10522 322 TLELRN--VTFAYQDNGFSvGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 84 G-----------LLAQNATTPGDITVQELVARGRYPHQPLFTRWRkedeeavsramkatgITDLarqsvdTLSGGQRQRA 152
Cdd:PRK10522 400 SavftdfhlfdqLLGPEGKPANPALVEKWLERLKMAHKLELEDGR---------------ISNL------KLSKGQKKRL 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 153 WIAMVLAQETAIMLLDE------PTTwldisHQIDLLELLSELnQQKGYTLAAVLHD---LNQACRyathLIALREGKIV 223
Cdd:PRK10522 459 ALLLALAEERDILLLDEwaadqdPHF-----RREFYQVLLPLL-QEMGKTIFAISHDdhyFIHADR----LLEMRNGQLS 528
|
250
....*....|....*...
gi 490237141 224 A-EGAPKEIVSAELIEKI 240
Cdd:PRK10522 529 ElTGEERDAASRDAVART 546
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
26-228 |
1.35e-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: 60.97 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 26 LNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQryaskevakrigllAQNattpgditvqelvaRG 105
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT--------------ADN--------------RE 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 106 RY----------PHqpLFTR----WRKEDEEAVSRAMKA------TGITDLARQSVDtLSGGQRQRawIAMVLA--QETA 163
Cdd:COG4615 403 AYrqlfsavfsdFH--LFDRllglDGEADPARARELLERleldhkVSVEDGRFSTTD-LSQGQRKR--LALLVAllEDRP 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490237141 164 IMLLDEpttWldISHQ------IDLLELLSELnQQKGYTLAAVLHDlnqaCRY---ATHLIALREGKIVAEGAP 228
Cdd:COG4615 478 ILVFDE---W--AADQdpefrrVFYTELLPEL-KARGKTVIAISHD----DRYfdlADRVLKMDYGKLVELTGP 541
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
37-225 |
1.38e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 59.79 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 37 AIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVA----KRIGLLAQNATTPGDITVQELVargrypHQPL 112
Cdd:PRK10584 40 ALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAklraKHVGFVFQSFMLIPTLNALENV------ELPA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 113 FTRWRKEDEEAVSRA--MKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELN 190
Cdd:PRK10584 114 LLRGESSRQSRNGAKalLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLN 193
|
170 180 190
....*....|....*....|....*....|....*
gi 490237141 191 QQKGYTLAAVLHDLNQACRYATHLiALREGKIVAE 225
Cdd:PRK10584 194 REHGTTLILVTHDLQLAARCDRRL-RLVNGQLQEE 227
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
12-175 |
1.64e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 58.73 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 12 QLTLAYGKKTIAEsLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYAsKEVAKRIGllaQNAT 91
Cdd:PRK13541 6 QLQFNIEQKNLFD-LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA-KPYCTYIG---HNLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 92 TPGDITVQELVargryphqplfTRWRK--EDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
Cdd:PRK13541 81 LKLEMTVFENL-----------KFWSEiyNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDE 149
|
....*.
gi 490237141 170 PTTWLD 175
Cdd:PRK13541 150 VETNLS 155
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
13-242 |
2.23e-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: 60.22 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 13 LTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAS--GHVYLDGEQIQ-RYASKEVAKRIGLLAQN 89
Cdd:TIGR02633 7 IVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKaSNIRDTERAGIVIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 90 ATTPGDITVQELVARGrypHQPLFTRWRKEDEEAVSRA---MKATGITDL-ARQSVDTLSGGQRQRAWIAMVLAQETAIM 165
Cdd:TIGR02633 87 LTLVPELSVAENIFLG---NEITLPGGRMAYNAMYLRAknlLRELQLDADnVTRPVGDYGGGQQQLVEIAKALNKQARLL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490237141 166 LLDEPTTWLDISHQIDLLELLSELnQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVSAELIEKIYG 242
Cdd:TIGR02633 164 ILDEPSSSLTEKETEILLDIIRDL-KAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMMVG 239
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
43-225 |
4.01e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 59.54 E-value: 4.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 43 GCGKSTLLRTLSRLMTPASGHVYLDGEQIqRYASKEVAKRIGLL------AQNATTPGDiTVQE---LVARGRYPHQPLF 113
Cdd:PRK11288 289 GAGRSELMKLLYGATRRTAGQVYLDGKPI-DIRSPRDAIRAGIMlcpedrKAEGIIPVH-SVADninISARRHHLRAGCL 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 114 TRWRKEDEEAvSRAMKATGI-TDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNQQ 192
Cdd:PRK11288 367 INNRWEAENA-DRFIRSLNIkTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQ 445
|
170 180 190
....*....|....*....|....*....|...
gi 490237141 193 kGYTLAAVLHDLNQACRYATHLIALREGKIVAE 225
Cdd:PRK11288 446 -GVAVLFVSSDLPEVLGVADRIVVMREGRIAGE 477
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
18-210 |
4.65e-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: 59.56 E-value: 4.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 18 GKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDgEQIqryaskevakRIGLLAQNATTPGDIT 97
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ-PGI----------KVGYLPQEPQLDPTKT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 98 VQELVARGRYPHQPLFTRWRK-------EDEE---------AVSRAMKATGITDLARQ---------------SVDTLSG 146
Cdd:TIGR03719 85 VRENVEEGVAEIKDALDRFNEisakyaePDADfdklaaeqaELQEIIDAADAWDLDSQleiamdalrcppwdaDVTKLSG 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490237141 147 GQRQRAWIAMVLAQETAIMLLDEPTTWLDiSHQIDLLEllSELNQQKGyTLAAVLHDlnqacRY 210
Cdd:TIGR03719 165 GERRRVALCRLLLSKPDMLLLDEPTNHLD-AESVAWLE--RHLQEYPG-TVVAVTHD-----RY 219
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
144-234 |
5.69e-10 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 58.76 E-value: 5.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 144 LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIV 223
Cdd:COG4170 159 LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTV 238
|
90
....*....|.
gi 490237141 224 AEGAPKEIVSA 234
Cdd:COG4170 239 ESGPTEQILKS 249
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
33-234 |
7.60e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 58.98 E-value: 7.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 33 GHFTAI---------------IGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIqryASKEVA--KRIGLLAQNATTPGD 95
Cdd:NF033858 277 GDFTAVdhvsfrirrgeifgfLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---DAGDIAtrRRVGYMSQAFSLYGE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 96 ITVQ---ELVARgryphqpLFTRWRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQR---AwIAMVLAQEtaIMLLDE 169
Cdd:NF033858 354 LTVRqnlELHAR-------LFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRlslA-VAVIHKPE--LLILDE 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490237141 170 PTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQA--C-RyathlIAL-REGKIVAEGAPKEIVSA 234
Cdd:NF033858 424 PTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAerCdR-----ISLmHAGRVLASDTPAALVAA 487
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
13-176 |
9.08e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 57.17 E-value: 9.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 13 LTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRyasKEVAKRIGLLAQNATT 92
Cdd:PRK13543 17 LAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR---GDRSRFMAYLGHLPGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 93 PGDITVQELV-----ARGRYPHQplftrwrkedeeAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
Cdd:PRK13543 94 KADLSTLENLhflcgLHGRRAKQ------------MPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLL 161
|
....*....
gi 490237141 168 DEPTTWLDI 176
Cdd:PRK13543 162 DEPYANLDL 170
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
19-175 |
1.02e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.89 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 19 KKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLM--TPASGHVYLDGEQIqryaskevakrigllaqnattPGDI 96
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQF---------------------GREA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 97 TVQELVargryphqplftrWRKEDEEAVSRAMKATGITD--LARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
Cdd:COG2401 101 SLIDAI-------------GRKGDFKDAVELLNAVGLSDavLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHL 167
|
.
gi 490237141 175 D 175
Cdd:COG2401 168 D 168
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
22-217 |
2.16e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 57.73 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 22 IAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYL-DGEQIQRYASKEVAKRIGLLAQNA-----TTPGD 95
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPllfsnSIKNN 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 96 I-----TVQELVARGRYPHQPLFTRWRKEDEEAVSRAMKATGITDL-----------ARQSVDT---------------- 143
Cdd:PTZ00265 480 IkyslySLKDLEALSNYYNEDGNDSQENKNKRNSCRAKCAGDLNDMsnttdsnelieMRKNYQTikdsevvdvskkvlih 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 144 --------------------LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHD 203
Cdd:PTZ00265 560 dfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHR 639
|
250
....*....|....
gi 490237141 204 LNqACRYATHLIAL 217
Cdd:PTZ00265 640 LS-TIRYANTIFVL 652
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
25-240 |
2.30e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 57.37 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 25 SLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGeQIQRYASKEVAKRIG--LLAQNATTPGDITVQELV 102
Cdd:PRK15439 29 GIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGG-NPCARLTPAKAHQLGiyLVPQEPLLFPNLSVKENI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 103 ARGRYPHQplftrwrkEDEEAVSRAMKATGIT-DLARQSvDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQID 181
Cdd:PRK15439 108 LFGLPKRQ--------ASMQKMKQLLAALGCQlDLDSSA-GSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETER 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490237141 182 LLELLSELnQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVSAELIEKI 240
Cdd:PRK15439 179 LFSRIREL-LAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDIIQAI 236
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
26-192 |
2.76e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.98 E-value: 2.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 26 LNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKE-VAKRIGLLAQNATTPG---DITVQEL 101
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPEDRQSSGlylDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 102 VARGRYPHQPLFTRwRKEDEEAVSRAMKATGIT-DLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQI 180
Cdd:PRK15439 362 VCALTHNRRGFWIK-PARENAVLERYRRALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARN 440
|
170
....*....|..
gi 490237141 181 DLLELLSELNQQ 192
Cdd:PRK15439 441 DIYQLIRSIAAQ 452
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
43-237 |
2.90e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 56.96 E-value: 2.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 43 GCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAK-----------RIGLLaqnattpGDITVQELVARGRYpHQP 111
Cdd:COG3845 294 GNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRlgvayipedrlGRGLV-------PDMSVAENLILGRY-RRP 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 112 LFTRW----RKEDEEAVSRAMKATGI-TDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS-----HQId 181
Cdd:COG3845 366 PFSRGgfldRKAIRAFAEELIEEFDVrTPGPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGaiefiHQR- 444
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490237141 182 LLELlselnQQKGytlAAVL---HDLNQACRYATHLIALREGKIVAEGAPKEiVSAELI 237
Cdd:COG3845 445 LLEL-----RDAG---AAVLlisEDLDEILALSDRIAVMYEGRIVGEVPAAE-ATREEI 494
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
38-228 |
2.94e-09 |
|
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: 55.50 E-value: 2.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 38 IIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIGLLAQNATTPGDITVQELVARGRYphqplftrwr 117
Cdd:cd03369 39 IVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQDPTLFSGTIRSNLDPFDEY---------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 118 keDEEAVSRAMKATGitdlarqSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSElnQQKGYTL 197
Cdd:cd03369 109 --SDEEIYGALRVSE-------GGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIRE--EFTNSTI 177
|
170 180 190
....*....|....*....|....*....|.
gi 490237141 198 AAVLHDLNQACRYAtHLIALREGKIVAEGAP 228
Cdd:cd03369 178 LTIAHRLRTIIDYD-KILVMDAGEVKEYDHP 207
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
27-242 |
3.34e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.86 E-value: 3.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 27 NVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAS--GHVYLDGEQIQRYASKEV-AKRIGLLAQNATTPGDITVQELVA 103
Cdd:PRK13549 25 SLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQASNIRDTeRAGIAIIHQELALVKELSVLENIF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 104 RGRYPHQPLFTRWRKEDEEAvSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLL 183
Cdd:PRK13549 105 LGNEITPGGIMDYDAMYLRA-QKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490237141 184 ELLSELnQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIVSAELIEKIYG 242
Cdd:PRK13549 184 DIIRDL-KAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDIITMMVG 241
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
20-189 |
3.38e-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: 54.47 E-value: 3.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 20 KTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHvyldgeqIQRYASKEVAkrigLLAQNA-TTPGdiTV 98
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGR-------IGMPEGEDLL----FLPQRPyLPLG--TL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 99 QELVArgrYPhqplftrWRkedeeavsramkatgitdlarqsvDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISH 178
Cdd:cd03223 81 REQLI---YP-------WD------------------------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEES 126
|
170
....*....|.
gi 490237141 179 QIDLLELLSEL 189
Cdd:cd03223 127 EDRLYQLLKEL 137
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
8-203 |
3.72e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 56.72 E-value: 3.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 8 LRGDQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLdgeqiqryaSKEVakRIGLLA 87
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL---------AKGI--KLGYFA 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 88 QNATtpgditvqELVARGRYPHQPLFTRWRKEDEEAVSRAMKATGIT-DLARQSVDTLSGGQRQRAWIAMVLAQETAIML 166
Cdd:PRK10636 382 QHQL--------EFLRADESPLQHLARLAPQELEQKLRDYLGGFGFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLL 453
|
170 180 190
....*....|....*....|....*....|....*..
gi 490237141 167 LDEPTTWLDISHQIDLLELLSELNQqkgyTLAAVLHD 203
Cdd:PRK10636 454 LDEPTNHLDLDMRQALTEALIDFEG----ALVVVSHD 486
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-175 |
3.80e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 56.95 E-value: 3.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 5 TSRLRGDQLTLAY-GKKTIA-ESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASkEVAKR 82
Cdd:TIGR01257 1935 TDILRLNELTKVYsGTSSPAvDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNIS-DVHQN 2013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 83 IGLLAQNATTPGDITVQElvargrypHQPLFTRWR----KEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVL 158
Cdd:TIGR01257 2014 MGYCPQFDAIDDLLTGRE--------HLYLYARLRgvpaEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIAL 2085
|
170
....*....|....*..
gi 490237141 159 AQETAIMLLDEPTTWLD 175
Cdd:TIGR01257 2086 IGCPPLVLLDEPTTGMD 2102
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
25-228 |
4.09e-09 |
|
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: 55.70 E-value: 4.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 25 SLNVTIPDGHFTAIIGPNGCGKSTLLRTLsrLMTPASGHVYLDGEQIQRYASKEVAKRIGLLAQ-------------NAT 91
Cdd:cd03271 13 NIDVDIPLGVLTCVTGVSGSGKSSLINDT--LYPALARRLHLKKEQPGNHDRIEGLEHIDKVIVidqspigrtprsnPAT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 92 TPGDIT-VQEL---VARG-RYPHQPLFTRWRKED---------EEA---------VSRAMKAT-----GITDLArQSVDT 143
Cdd:cd03271 91 YTGVFDeIRELfceVCKGkRYNRETLEVRYKGKSiadvldmtvEEAleffenipkIARKLQTLcdvglGYIKLG-QPATT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 144 LSGGQRQRAWIAMVLAQET---AIMLLDEPTTWL---DISHQIDLLELLSElnqqKGYTLAAVLHDLNQAcRYATHLIAL 217
Cdd:cd03271 170 LSGGEAQRIKLAKELSKRStgkTLYILDEPTTGLhfhDVKKLLEVLQRLVD----KGNTVVVIEHNLDVI-KCADWIIDL 244
|
250
....*....|....*..
gi 490237141 218 ------REGKIVAEGAP 228
Cdd:cd03271 245 gpeggdGGGQVVASGTP 261
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
33-226 |
5.17e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.40 E-value: 5.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 33 GHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQR---YASKEVAKRIGLLAQN--ATTPGDITVqelvarGRY 107
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTlspGKLQALRRDIQFIFQDpyASLDPRQTV------GDS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 108 PHQPLFTRWRKEDEEAVSRA---MKATGIT-DLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLL 183
Cdd:PRK10261 424 IMEPLRVHGLLPGKAAAARVawlLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQII 503
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490237141 184 ELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAEG 226
Cdd:PRK10261 504 NLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
26-226 |
5.53e-09 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 54.25 E-value: 5.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 26 LNVTIPDGHFTAIIGPNGCGKSTLLrtlsrlmtpasghvyldgeqiqryasKEVAKRIGLLAQNATTPgditvqelvarg 105
Cdd:cd03238 14 LDVSIPLNVLVVVTGVSGSGKSTLV--------------------------NEGLYASGKARLISFLP------------ 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 106 RYPHQPLFtrwrkedeeAVS--RAMKATGITDLA-RQSVDTLSGGQRQRAWIAMVLAQET--AIMLLDEPTTWLdisHQI 180
Cdd:cd03238 56 KFSRNKLI---------FIDqlQFLIDVGLGYLTlGQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGL---HQQ 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490237141 181 DLLELLSELNQ--QKGYTLAAVLHDLNQACrYATHLIAL------REGKIVAEG 226
Cdd:cd03238 124 DINQLLEVIKGliDLGNTVILIEHNLDVLS-SADWIIDFgpgsgkSGGKVVFSG 176
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
20-232 |
9.14e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 55.49 E-value: 9.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 20 KTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIGLLAQNATTPGDiTVQ 99
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSD-TVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 100 ELVARGRyphqPLFTrwrKEDEEAVSRAmkATGITDLAR--QSVDT--------LSGGQRQRAWIAMVLAQETAIMLLDE 169
Cdd:PRK10789 407 NNIALGR----PDAT---QQEIEHVARL--ASVHDDILRlpQGYDTevgergvmLSGGQKQRISIARALLLNAEILILDD 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490237141 170 PTTWLD--ISHQIdlLELLSELNQQKGYTLAAvlHDLNqACRYATHLIALREGKIVAEGAPKEIV 232
Cdd:PRK10789 478 ALSAVDgrTEHQI--LHNLRQWGEGRTVIISA--HRLS-ALTEASEILVMQHGHIAQRGNHDQLA 537
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
7-231 |
1.15e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.52 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 7 RLRGdqLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVY-LDGEQIQRYASKEVAKRIGL 85
Cdd:NF033858 3 RLEG--VSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvLGGDMADARHRRAVCPRIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 86 LAQnattpG-------DITVQELV---ARgryphqpLFTRWRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIA 155
Cdd:NF033858 81 MPQ-----GlgknlypTLSVFENLdffGR-------LFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLC 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 156 MVLAQETAIMLLDEPTT----------WldishqidllELLSELNQQK-GYTlaaVLhdlnqacrYAT----------HL 214
Cdd:NF033858 149 CALIHDPDLLILDEPTTgvdplsrrqfW----------ELIDRIRAERpGMS---VL--------VATaymeeaerfdWL 207
|
250
....*....|....*..
gi 490237141 215 IALREGKIVAEGAPKEI 231
Cdd:NF033858 208 VAMDAGRVLATGTPAEL 224
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
33-175 |
1.26e-08 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 53.40 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 33 GHFTAIIGPNGCGKSTLLRTLS--RLMTPASGHVYLDGEQIQryasKEVAKRIGLLAQNATTPGDITVQELVargryphq 110
Cdd:cd03232 33 GTLTALMGESGAGKTTLLDVLAgrKTAGVITGEILINGRPLD----KNFQRSTGYVEQQDVHSPNLTVREAL-------- 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490237141 111 pLFTrwrkedeeAVSRAmkatgitdlarqsvdtLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
Cdd:cd03232 101 -RFS--------ALLRG----------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
10-231 |
1.91e-08 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 54.63 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 10 GDQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLL-----RTLSRL-----MTPASGH-----------VYLDG 68
Cdd:TIGR00630 611 GKFLTLKGARENNLKNITVSIPLGLFTCITGVSGSGKSTLIndtlyPALANRlngakTVPGRYTsieglehldkvIHIDQ 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 69 EQIQR-------------------YASKEVAKRIGLLAQNAT--TPG--------------------DITVQELVARG-R 106
Cdd:TIGR00630 691 SPIGRtprsnpatytgvfdeirelFAETPEAKVRGYTPGRFSfnVKGgrceacqgdgvikiemhflpDVYVPCEVCKGkR 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 107 YPHQPLFTRWRK------------------EDEEAVSRAMKAT-----GITDLArQSVDTLSGGQRQRAWIAMVL-AQET 162
Cdd:TIGR00630 771 YNRETLEVKYKGkniadvldmtveeayeffEAVPSISRKLQTLcdvglGYIRLG-QPATTLSGGEAQRIKLAKELsKRST 849
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 163 A--IMLLDEPTTWL---DISHQIDLLELLSElnqqKGYTLAAVLHDLNqACRYATHLIAL------REGKIVAEGAPKEI 231
Cdd:TIGR00630 850 GrtLYILDEPTTGLhfdDIKKLLEVLQRLVD----KGNTVVVIEHNLD-VIKTADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
37-222 |
2.22e-08 |
|
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: 52.43 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 37 AIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKE-VAKRIGLLaqnattPGDitvqelvargryphqplftr 115
Cdd:cd03215 30 GIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDaIRAGIAYV------PED-------------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 116 wRKED----EEAVSRAMkatGITDLarqsvdtLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNQ 191
Cdd:cd03215 84 -RKREglvlDLSVAENI---ALSSL-------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELAD 152
|
170 180 190
....*....|....*....|....*....|....
gi 490237141 192 QkGytlAAVL---HDLNQACRYATHLIALREGKI 222
Cdd:cd03215 153 A-G---KAVLlisSELDELLGLCDRILVMYEGRI 182
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
144-234 |
2.77e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 53.65 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 144 LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRYATHLIALREGKIV 223
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
90
....*....|.
gi 490237141 224 AEGAPKEIVSA 234
Cdd:PRK15093 239 ETAPSKELVTT 249
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
33-175 |
2.98e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.34 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 33 GHFTAIIGPNGCGKSTLLRTLSRLMTpasGHVYLDGEQIQ--RYASKEVAKRIGLLAQNATTPGDITVQELVARGRYPHQ 110
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAERVT---TGVITGGDRLVngRPLDSSFQRSIGYVQQQDLHLPTSTVRESLRFSAYLRQ 865
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 111 PLFTRwRKEDEEAVSRAMKATGITDLARQSVDT----LSGGQRQRAWIAMVL-AQETAIMLLDEPTTWLD 175
Cdd:TIGR00956 866 PKSVS-KSEKMEYVEEVIKLLEMESYADAVVGVpgegLNVEQRKRLTIGVELvAKPKLLLFLDEPTSGLD 934
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
13-180 |
3.84e-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: 54.15 E-value: 3.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 13 LTLAY--GKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTpASGHVYLDGEQIQRYASKEVAKRIGLLAQNA 90
Cdd:TIGR01271 1223 LTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKV 1301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 91 TTPGDITVQELVARGRYPHQPLftrWRKEDEEAVsRAMKATGITDLARQSVD---TLSGGQRQRAWIAMVLAQETAIMLL 167
Cdd:TIGR01271 1302 FIFSGTFRKNLDPYEQWSDEEI---WKVAEEVGL-KSVIEQFPDKLDFVLVDggyVLSNGHKQLMCLARSILSKAKILLL 1377
|
170
....*....|....
gi 490237141 168 DEPTTWLD-ISHQI 180
Cdd:TIGR01271 1378 DEPSAHLDpVTLQI 1391
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
35-203 |
4.72e-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: 51.84 E-value: 4.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 35 FTAIIGPNGCGKSTLLRTLSrlmtpasghVYLDGEQIQRyaSKEVAKRIGLLAQNATTpGDITVQELVARG------RYP 108
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEALK---------YALTGELPPN--SKGGAHDPKLIREGEVR-AQVKLAFENANGkkytitRSL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 109 HQPLFTRWRKEDEeavsramkatgITDLARQSVDTLSGGQRQ------RAWIAMVLAQETAIMLLDEPTTWLDISH-QID 181
Cdd:cd03240 92 AILENVIFCHQGE-----------SNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENiEES 160
|
170 180
....*....|....*....|..
gi 490237141 182 LLELLSELNQQKGYTLAAVLHD 203
Cdd:cd03240 161 LAEIIEERKSQKNFQLIVITHD 182
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
18-207 |
5.28e-08 |
|
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: 51.21 E-value: 5.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 18 GKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSrlmtpasghvyldgeqiqryaskevakrigllaqnattpgdit 97
Cdd:cd03227 6 RFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIG------------------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 98 vqeLVARGRYPHQplfTRWRKEDEEAVSRAMKATGItdlarQSVDTLSGGQRQRAWIAMVLA----QETAIMLLDEPTTW 173
Cdd:cd03227 43 ---LALGGAQSAT---RRRSGVKAGCIVAAVSAELI-----FTRLQLSGGEKELSALALILAlaslKPRPLYILDEIDRG 111
|
170 180 190
....*....|....*....|....*....|....
gi 490237141 174 LDISHQIDLLELLSELNqQKGYTLAAVLHDLNQA 207
Cdd:cd03227 112 LDPRDGQALAEAILEHL-VKGAQVIVITHLPELA 144
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
19-245 |
5.82e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 53.31 E-value: 5.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 19 KKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPA---SGHVYLDGEQIQRYASKEVAKRIgllAQNATTPGD 95
Cdd:PLN03140 177 KLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRLNEFVPRKTSAYI---SQNDVHVGV 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 96 ITVQELV---ARGryphQPLFTRW-------RKED------EEAVSRAMKATG--------ITDLARQSV------DT-- 143
Cdd:PLN03140 254 MTVKETLdfsARC----QGVGTRYdllselaRREKdagifpEAEVDLFMKATAmegvksslITDYTLKILgldickDTiv 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 144 -------LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNQqkgYTLAAVLHDLNQACRYATHL-- 214
Cdd:PLN03140 330 gdemirgISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVH---LTEATVLMSLLQPAPETFDLfd 406
|
250 260 270
....*....|....*....|....*....|...
gi 490237141 215 --IALREGKIVAEGaPKEIVsAELIEKiYGLRC 245
Cdd:PLN03140 407 diILLSEGQIVYQG-PRDHI-LEFFES-CGFKC 436
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
19-257 |
8.90e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.80 E-value: 8.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 19 KKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLS----RLMTPASGHVYLDG---EQIQRYASKEVAkrigLLAQNAT 91
Cdd:TIGR00956 73 TFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGitpEEIKKHYRGDVV----YNAETDV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 92 TPGDITVQE---LVARGRYPHqplfTRWrkedeEAVSRAMKATGITDLA------RQSVDT---------LSGGQRQRAW 153
Cdd:TIGR00956 149 HFPHLTVGEtldFAARCKTPQ----NRP-----DGVSREEYAKHIADVYmatyglSHTRNTkvgndfvrgVSGGERKRVS 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 154 IAMVLAQETAIMLLDEPTTWLDIShqiDLLELLSELNQQKGYTLAAVLHDLNQACRYATHL----IALREGKIVAEGAPK 229
Cdd:TIGR00956 220 IAEASLGGAKIQCWDNATRGLDSA---TALEFIRALKTSANILDTTPLVAIYQCSQDAYELfdkvIVLYEGYQIYFGPAD 296
|
250 260 270
....*....|....*....|....*....|....*...
gi 490237141 230 EivSAELIEKIyGLRC----------TIIEDPVAHTPL 257
Cdd:TIGR00956 297 K--AKQYFEKM-GFKCpdrqttadflTSLTSPAERQIK 331
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
24-202 |
9.37e-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: 52.44 E-value: 9.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 24 ESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIGLLAQNATTPGdiTVQELVA 103
Cdd:TIGR00954 469 ESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPYMTLGTLRDQIIYPD--SSEDMKR 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 104 RGryphqplftrWRKEDEEAVSRAMKATGIT------DLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLdis 177
Cdd:TIGR00954 547 RG----------LSDKDLEQILDNVQLTHILereggwSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAV--- 613
|
170 180
....*....|....*....|....*
gi 490237141 178 hQIDLLELLSELNQQKGYTLAAVLH 202
Cdd:TIGR00954 614 -SVDVEGYMYRLCREFGITLFSVSH 637
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
136-231 |
1.50e-07 |
|
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: 51.94 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 136 LARqSVDTLSGGQRQRAWIAMVL-AQETAIM-LLDEPTTWLdisHQIDLLELLSELN--QQKGYTLAAVLHDlNQACRYA 211
Cdd:TIGR00630 482 LSR-AAGTLSGGEAQRIRLATQIgSGLTGVLyVLDEPSIGL---HQRDNRRLINTLKrlRDLGNTLIVVEHD-EDTIRAA 556
|
90 100
....*....|....*....|....*.
gi 490237141 212 THLIAL------REGKIVAEGAPKEI 231
Cdd:TIGR00630 557 DYVIDIgpgageHGGEVVASGTPEEI 582
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
19-223 |
1.78e-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: 50.34 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 19 KKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPA---SGHVYLDGEQIQRYASKevakrigllaqnatTPGD 95
Cdd:cd03233 19 KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEK--------------YPGE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 96 I--TVQELVargrypHQPLFTRwrkedEEAVSRAMKATGitdlaRQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
Cdd:cd03233 85 IiyVSEEDV------HFPTLTV-----RETLDFALRCKG-----NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490237141 174 LDISHQIDLLELLSEL-NQQKGYTLAAVLhdlnQACRYATHL----IALREGKIV 223
Cdd:cd03233 149 LDSSTALEILKCIRTMaDVLKTTTFVSLY----QASDEIYDLfdkvLVLYEGRQI 199
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
20-188 |
2.32e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 50.56 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 20 KTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLS--RLMTPASGHVYLDGEQIQRYASKEVAKRIGLLAQN--ATTPG- 94
Cdd:PRK09580 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPEDRAGEGIFMAFQypVEIPGv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 95 --DITVQELV-ARGRYPHQPLFTRWRKED--EEAVSR-AMKAtgitDLARQSVDT-LSGGQRQRAWIAMVLAQETAIMLL 167
Cdd:PRK09580 94 snQFFLQTALnAVRSYRGQEPLDRFDFQDlmEEKIALlKMPE----DLLTRSVNVgFSGGEKKRNDILQMAVLEPELCIL 169
|
170 180
....*....|....*....|.
gi 490237141 168 DEPTTWLDishqIDLLELLSE 188
Cdd:PRK09580 170 DESDSGLD----IDALKIVAD 186
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
38-235 |
4.26e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 50.74 E-value: 4.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 38 IIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIGLLAQNATT-PGDItvqelvargRYPHQPlftrW 116
Cdd:PLN03232 1267 VVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLfSGTV---------RFNIDP----F 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 117 RKEDEEAVSRAMKATGITDLARQSV-----------DTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIshQIDLLEL 185
Cdd:PLN03232 1334 SEHNDADLWEALERAHIKDVIDRNPfgldaevseggENFSVGQRQLLSLARALLRRSKILVLDEATASVDV--RTDSLIQ 1411
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490237141 186 LSELNQQKGYTLAAVLHDLNQACRyATHLIALREGKIVAEGAPKEIVSAE 235
Cdd:PLN03232 1412 RTIREEFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRD 1460
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
38-210 |
4.97e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.12 E-value: 4.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 38 IIGPNGCGKSTLLRTLSRLMTPASGHVYL-DGeqiqryaskevaKRIGLLAQNATTPGDITVQELVARGRYPHQPLFTRW 116
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGEARPaPG------------IKVGYLPQEPQLDPEKTVRENVEEGVAEVKAALDRF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 117 rkedeEAVSRAM---------------------KATGITDLARQ---------------SVDTLSGGQRQRAWIAMVLAQ 160
Cdd:PRK11819 106 -----NEIYAAYaepdadfdalaaeqgelqeiiDAADAWDLDSQleiamdalrcppwdaKVTKLSGGERRRVALCRLLLE 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490237141 161 ETAIMLLDEPTTWLDiSHQIDLLEllSELNQQKGyTLAAVLHDlnqacRY 210
Cdd:PRK11819 181 KPDMLLLDEPTNHLD-AESVAWLE--QFLHDYPG-TVVAVTHD-----RY 221
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
33-189 |
5.82e-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: 48.14 E-value: 5.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 33 GHFTAIIGPNGCGKSTLLRTLSRLMTPASGHV-YLDGEQIQRYASKEVAKRIGllaqnattpgditvqelvargryphqp 111
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGViYIDGEDILEEVLDQLLLIIV--------------------------- 54
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490237141 112 lftrwrkedeeavsramkatgitdlaRQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSEL 189
Cdd:smart00382 55 --------------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELR 106
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
15-223 |
6.04e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.95 E-value: 6.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 15 LAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSrlmtpasGHVYLDGEQIQrYASKEVAKRiglLAQNAttPG 94
Cdd:PRK11147 11 LSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILN-------GEVLLDDGRII-YEQDLIVAR---LQQDP--PR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 95 DI--TVQELVARG---------RYpHQPLFTRWRKEDEEAVSRAMKATGITD--------------LARQSVD------T 143
Cdd:PRK11147 78 NVegTVYDFVAEGieeqaeylkRY-HDISHLVETDPSEKNLNELAKLQEQLDhhnlwqlenrinevLAQLGLDpdaalsS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 144 LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIShQIDLLELLseLNQQKGyTLAAVLHDLNQACRYATHLIALREGKIV 223
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIE-TIEWLEGF--LKTFQG-SIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
26-240 |
1.01e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 49.59 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 26 LNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGhvyldgeqiqryASKEVAKRIGLLAQ-----NATTPGDITVQE 100
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAET------------SSVVIRGSVAYVPQvswifNATVRENILFGS 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 101 LVARGRYphqplftrWRKEDEEAVSRAMK---ATGITDLARQSVDtLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD-- 175
Cdd:PLN03232 704 DFESERY--------WRAIDVTALQHDLDllpGRDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDah 774
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490237141 176 ISHQIDLLELLSELNQQKGYTLAAVLHDLNQACRyathLIALREGKIVAEGAPKEIV-SAELIEKI 240
Cdd:PLN03232 775 VAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDR----IILVSEGMIKEEGTFAELSkSGSLFKKL 836
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
27-223 |
2.85e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.86 E-value: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 27 NVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMtPA---SGHVYLDGEqIQRYASKEVAKRIGLLaqnattpgdITVQEL-- 101
Cdd:NF040905 21 NLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGE-VCRFKDIRDSEALGIV---------IIHQELal 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 102 -----VAR----GRYPHQPLFTRWRKEDEEAvSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
Cdd:NF040905 90 ipylsIAEniflGNERAKRGVIDWNETNRRA-RELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490237141 173 WLDISHQIDLLELLSELNQQkGYTLAAVLHDLNQACRYATHLIALREGKIV 223
Cdd:NF040905 169 ALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGRTI 218
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
139-232 |
3.28e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 48.10 E-value: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 139 QSVDTLSGGQRQRAWIAMVLAQET---AIMLLDEPTTWL---DISHqidLLELLSELnQQKGYTLAAVLHDLNqACRYAT 212
Cdd:COG0178 822 QPATTLSGGEAQRVKLASELSKRStgkTLYILDEPTTGLhfhDIRK---LLEVLHRL-VDKGNTVVVIEHNLD-VIKTAD 896
|
90 100
....*....|....*....|....*.
gi 490237141 213 HLIAL------REGKIVAEGAPKEIV 232
Cdd:COG0178 897 WIIDLgpeggdGGGEIVAEGTPEEVA 922
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-197 |
4.15e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 46.94 E-value: 4.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 1 MTAVTSRLRGDQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRlmTPA----SGHVYLDGEQIQRYAS 76
Cdd:CHL00131 1 MNKNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDLEP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 77 KEVAKR-IGLLAQNATT-PG--DITVQELVARGRYPHQ------PL-FTRWRKEDEEAVSraMKATGitdLARQSVDTLS 145
Cdd:CHL00131 79 EERAHLgIFLAFQYPIEiPGvsNADFLRLAYNSKRKFQglpeldPLeFLEIINEKLKLVG--MDPSF---LSRNVNEGFS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490237141 146 GGQRQRAWIAMVLAQETAIMLLDEPTTWLDishqIDLLELLSE-----LNQQKGYTL 197
Cdd:CHL00131 154 GGEKKRNEILQMALLDSELAILDETDSGLD----IDALKIIAEginklMTSENSIIL 206
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
30-204 |
4.34e-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: 46.03 E-value: 4.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 30 IPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIqryaskevakrigllaqnATTPgditvqelvargryph 109
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITP------------------VYKP---------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 110 qplftrwrkedeeavsramkatgitdlarQSVDtLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSEL 189
Cdd:cd03222 68 -----------------------------QYID-LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117
|
170
....*....|....*
gi 490237141 190 NQQKGYTLAAVLHDL 204
Cdd:cd03222 118 SEEGKKTALVVEHDL 132
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
61-235 |
5.77e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 47.33 E-value: 5.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 61 SGHVYLDGEQIQRYASKEVAKRIGLLAQNATTpGDITVQELVARGryphqplftrwrKED--EEAVSRAMKATGITDLAR 138
Cdd:PTZ00265 1276 SGKILLDGVDICDYNLKDLRNLFSIVSQEPML-FNMSIYENIKFG------------KEDatREDVKRACKFAAIDEFIE 1342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 139 ---QSVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNQQKGYTLAAVLHDLNQA 207
Cdd:PTZ00265 1343 slpNKYDTnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASI 1422
|
170 180 190
....*....|....*....|....*....|...
gi 490237141 208 CRyATHLIAL----REGKIV-AEGAPKEIVSAE 235
Cdd:PTZ00265 1423 KR-SDKIVVFnnpdRTGSFVqAHGTHEELLSVQ 1454
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
27-193 |
6.98e-06 |
|
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: 46.53 E-value: 6.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 27 NVTIP-DGHFTAIIGPNGCGKSTLLRTLSRLMTPASG--------HVYLDGEQIQRYASKEVAKRIGLLAQNATTPGDIT 97
Cdd:COG3593 16 DLSIElSDDLTVLVGENNSGKSSILEALRLLLGPSSSrkfdeedfYLGDDPDLPEIEIELTFGSLLSRLLRLLLKEEDKE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 98 -VQELVARGRYPHQPLFTRWRKE---------DEEAVSRAMKATGITDLAR---------QSVDTLSGGQRQRAWIAMVL 158
Cdd:COG3593 96 eLEEALEELNEELKEALKALNELlseylkellDGLDLELELSLDELEDLLKslslriedgKELPLDRLGSGFQRLILLAL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490237141 159 AQETA---------IMLLDEPTTWLDISHQIDLLELLSELNQQK 193
Cdd:COG3593 176 LSALAelkrapanpILLIEEPEAHLHPQAQRRLLKLLKELSEKP 219
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
139-235 |
7.30e-06 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 46.99 E-value: 7.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 139 QSVDTLSGGQRQRawiaMVLAQETA-------IMLLDEPTTWL---DISHqidLLELLSELnQQKGYTLAAVLHDLNqAC 208
Cdd:PRK00349 826 QPATTLSGGEAQR----VKLAKELSkrstgktLYILDEPTTGLhfeDIRK---LLEVLHRL-VDKGNTVVVIEHNLD-VI 896
|
90 100 110
....*....|....*....|....*....|...
gi 490237141 209 RYATHLIAL------REGKIVAEGAPKEIVSAE 235
Cdd:PRK00349 897 KTADWIIDLgpeggdGGGEIVATGTPEEVAKVE 929
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
20-242 |
8.96e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 46.70 E-value: 8.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 20 KTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYldgeqiqryaskeVAKRIGLLAQ-----NATTPG 94
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-------------AERSIAYVPQqawimNATVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 95 DItvqelvargryphqpLFtrWRKEDEEAVSRAMKATGI-TDLARQS--VDT--------LSGGQRQRAWIAMVLAQETA 163
Cdd:PTZ00243 740 NI---------------LF--FDEEDAARLADAVRVSQLeADLAQLGggLETeigekgvnLSGGQKARVSLARAVYANRD 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 164 IMLLDEPTTWLD--ISHQIdLLELLseLNQQKGYTLAAVLHDLNQACRyATHLIALREGKIVAEGAPKEIVSAELIEKIY 241
Cdd:PTZ00243 803 VYLLDDPLSALDahVGERV-VEECF--LGALAGKTRVLATHQVHVVPR-ADYVVALGDGRVEFSGSSADFMRTSLYATLA 878
|
.
gi 490237141 242 G 242
Cdd:PTZ00243 879 A 879
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
12-201 |
9.39e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 45.33 E-value: 9.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 12 QLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKeVAKRIGLLAQNAT 91
Cdd:PRK13540 6 ELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCT-YQKQLCFVGHRSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 92 TPGDITVQElvargryphQPLFtrwrkeDEEAVSRAMkatGITDLAR-----QSVD----TLSGGQRQRAWIAMVLAQET 162
Cdd:PRK13540 85 INPYLTLRE---------NCLY------DIHFSPGAV---GITELCRlfsleHLIDypcgLLSSGQKRQVALLRLWMSKA 146
|
170 180 190
....*....|....*....|....*....|....*....
gi 490237141 163 AIMLLDEPTTWLDishQIDLLELLSELNQQKGYTLAAVL 201
Cdd:PRK13540 147 KLWLLDEPLVALD---ELSLLTIITKIQEHRAKGGAVLL 182
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
13-180 |
1.26e-05 |
|
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: 45.62 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 13 LTLAY--GKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTpASGHVYLDGEQIQRYASKEVAKRIGLLAQNA 90
Cdd:cd03289 8 LTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 91 TTPGDITVQELVARGRYPHQPLftrWRKEDEEAVSRAMKA-TGITDLarQSVD---TLSGGQRQRAWIAMVLAQETAIML 166
Cdd:cd03289 87 FIFSGTFRKNLDPYGKWSDEEI---WKVAEEVGLKSVIEQfPGQLDF--VLVDggcVLSHGHKQLMCLARSVLSKAKILL 161
|
170
....*....|....*
gi 490237141 167 LDEPTTWLD-ISHQI 180
Cdd:cd03289 162 LDEPSAHLDpITYQV 176
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
25-235 |
1.27e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 46.27 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 25 SLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEVAKRIGLLAQnatTP----GDItvqe 100
Cdd:PLN03130 1257 GLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQ---APvlfsGTV---- 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 101 lvargRYPHQPlFTRWRKED-EEAVSRA-MKAT------GITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
Cdd:PLN03130 1330 -----RFNLDP-FNEHNDADlWESLERAhLKDVirrnslGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATA 1403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490237141 173 WLDIshQIDLLELLSELNQQKGYTLAAVLHDLNQA--CryaTHLIALREGKIVAEGAPKEIVSAE 235
Cdd:PLN03130 1404 AVDV--RTDALIQKTIREEFKSCTMLIIAHRLNTIidC---DRILVLDAGRVVEFDTPENLLSNE 1463
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
136-235 |
2.62e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 45.06 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 136 LARqSVDTLSGG--QRQRawiamvLAQE-----TAIM-LLDEPTTWLdisHQID---LLELLSELnQQKGYTLAAVLHDl 204
Cdd:PRK00349 483 LSR-SAGTLSGGeaQRIR------LATQigsglTGVLyVLDEPSIGL---HQRDndrLIETLKHL-RDLGNTLIVVEHD- 550
|
90 100 110
....*....|....*....|....*....|....*..
gi 490237141 205 NQACRYATHLIAL------REGKIVAEGAPKEIVSAE 235
Cdd:PRK00349 551 EDTIRAADYIVDIgpgagvHGGEVVASGTPEEIMKNP 587
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
117-231 |
3.27e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 44.34 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 117 RKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELnQQKGYT 196
Cdd:NF000106 118 RKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSM-VRDGAT 196
|
90 100 110
....*....|....*....|....*....|....*
gi 490237141 197 LAAVLHDLNQACRYATHLIALREGKIVAEGAPKEI 231
Cdd:NF000106 197 VLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
33-175 |
4.27e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.84 E-value: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 33 GHFTAIIGPNGCGKSTLLRTLSRLMTPAsghvYLDGE-QIQRYASK-EVAKRI-GLLAQNATTPGDITVQE-LVARGryp 108
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGRKTGG----YIEGDiRISGFPKKqETFARIsGYCEQNDIHSPQVTVREsLIYSA--- 978
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490237141 109 hqplFTRWRKE--DEEA---VSRAMKATGITDLARQ-----SVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
Cdd:PLN03140 979 ----FLRLPKEvsKEEKmmfVDEVMELVELDNLKDAivglpGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
16-47 |
5.86e-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: 42.84 E-value: 5.86e-05
10 20 30
....*....|....*....|....*....|..
gi 490237141 16 AYGKKTIAESLNVTIPDGhFTAIIGPNGCGKS 47
Cdd:cd03278 6 LKGFKSFADKTTIPFPPG-LTAIVGPNGSGKS 36
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
33-225 |
6.53e-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: 43.66 E-value: 6.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 33 GHFTAIIGPNGCGKSTLLRTLSRLMTPA-SGHVYLDGEQIQ-RYASKEVAKRIGLLAQNATTPGDITVQ------ELVAR 104
Cdd:TIGR02633 286 GEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDiRNPAQAIRAGIAMVPEDRKRHGIVPILgvgkniTLSVL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 105 GRYPHQPLFTRWRKED--EEAVSRAMKATGITDLArqsVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDL 182
Cdd:TIGR02633 366 KSFCFKMRIDAAAELQiiGSAIQRLKVKTASPFLP---IGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEI 442
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490237141 183 LELLSELNQQkGYTLAAVLHDLNQACRYATHLIALREGKIVAE 225
Cdd:TIGR02633 443 YKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLKGD 484
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
18-203 |
6.57e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.01 E-value: 6.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 18 GKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYASKEvakrigllaqnatTPG-DI 96
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQE-------------TPAlPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 97 TVQELVARG----RYPHQPLFTRWRKEDEEAVS--------------RAMKATGITDLA------RQSVDTLSGGQRQRA 152
Cdd:PRK10636 79 PALEYVIDGdreyRQLEAQLHDANERNDGHAIAtihgkldaidawtiRSRAASLLHGLGfsneqlERPVSDFSGGWRMRL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490237141 153 WIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLselnqqKGY--TLAAVLHD 203
Cdd:PRK10636 159 NLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWL------KSYqgTLILISHD 205
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
136-235 |
6.75e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.86 E-value: 6.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 136 LARQSvDTLSGG--QRQRawiamvLAqeTAI------ML--LDEPTTWLdisHQID---LLELLSELnQQKGYTLAAVLH 202
Cdd:COG0178 479 LDRSA-GTLSGGeaQRIR------LA--TQIgsglvgVLyvLDEPSIGL---HQRDndrLIETLKRL-RDLGNTVIVVEH 545
|
90 100 110
....*....|....*....|....*....|....*....
gi 490237141 203 DLnQACRYATHLIAL------REGKIVAEGAPKEIVSAE 235
Cdd:COG0178 546 DE-DTIRAADYIIDIgpgageHGGEVVAQGTPEEILKNP 583
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
36-65 |
8.42e-05 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 39.51 E-value: 8.42e-05
10 20 30
....*....|....*....|....*....|
gi 490237141 36 TAIIGPNGCGKSTLLRTLSRLMTPASGHVY 65
Cdd:pfam13555 25 TLLTGPSGSGKSTLLDAIQTLLVPAKRARF 54
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
22-184 |
9.92e-05 |
|
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: 43.36 E-value: 9.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 22 IAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGeqiqryaskevakRIGLLAQNA-TTPGdiTVQE 100
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSwIMPG--TIKD 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 101 LVARG----RYPHQPLFTRWRKEDEEAVsraMKATGITDLARQSVdTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
Cdd:TIGR01271 506 NIIFGlsydEYRYTSVIKACQLEEDIAL---FPEKDKTVLGEGGI-TLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
....*...
gi 490237141 177 SHQIDLLE 184
Cdd:TIGR01271 582 VTEKEIFE 589
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
27-59 |
1.41e-04 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 42.29 E-value: 1.41e-04
10 20 30
....*....|....*....|....*....|....*.
gi 490237141 27 NVTIP---DGHFTAIIGPNGCGKSTLLRTLSRLMTP 59
Cdd:COG3950 16 DLEIDfdnPPRLTVLVGENGSGKTTLLEAIALALSG 51
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
33-194 |
1.63e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.41 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 33 GHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQ-RYASKEVAKRIGLLAQNATTPG-----DITVQELVARGR 106
Cdd:PRK10982 274 GEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINnHNANEAINHGFALVTEERRSTGiyaylDIGFNSLISNIR 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 107 YPHQP---LFTRWRKEDEEAVSRAMKATgiTDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLL 183
Cdd:PRK10982 354 NYKNKvglLDNSRMKSDTQWVIDSMRVK--TPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIY 431
|
170
....*....|..
gi 490237141 184 ELLSEL-NQQKG 194
Cdd:PRK10982 432 QLIAELaKKDKG 443
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
140-226 |
1.73e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 41.86 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 140 SVDTLSGGQRQRAWIAMVLAQETA--IMLLDEPTTWLdisHQID---LLELLSELnQQKGYTLAAVLHDLnQACRYATHL 214
Cdd:cd03270 134 SAPTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGL---HPRDndrLIETLKRL-RDLGNTVLVVEHDE-DTIRAADHV 208
|
90
....*....|....*...
gi 490237141 215 IAL------REGKIVAEG 226
Cdd:cd03270 209 IDIgpgagvHGGEIVAQG 226
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
12-47 |
1.81e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 1.81e-04
10 20 30
....*....|....*....|....*....|....*.
gi 490237141 12 QLTLAyGKKTIAESLNVTIPDGhFTAIIGPNGCGKS 47
Cdd:COG1196 5 RLELA-GFKSFADPTTIPFEPG-ITAIVGPNGSGKS 38
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
20-239 |
2.47e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 42.08 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 20 KTIAESLNVTIPD-------------GHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQ-RYASKEVAKRIGL 85
Cdd:PRK09700 263 ETVFEVRNVTSRDrkkvrdisfsvcrGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKGMAY 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 86 LAQNATTPG---------DITVQELVARGRYPHQPLFTRWRKE----DEEAVSRAMKATGITdlarQSVDTLSGGQRQRA 152
Cdd:PRK09700 343 ITESRRDNGffpnfsiaqNMAISRSLKDGGYKGAMGLFHEVDEqrtaENQRELLALKCHSVN----QNITELSGGNQQKV 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 153 WIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNQQkGYTLAAVLHDLNQACRYATHLIALREGKIVAEGAPKEIV 232
Cdd:PRK09700 419 LISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDM 497
|
....*..
gi 490237141 233 SAELIEK 239
Cdd:PRK09700 498 SEEEIMA 504
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
35-56 |
2.58e-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: 2.58e-04
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
3-184 |
3.10e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.77 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 3 AVTSRLRGDQLTLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSrlMTPASG--------HV---------- 64
Cdd:PLN03073 173 PAIKDIHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMA--MHAIDGipkncqilHVeqevvgddtt 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 65 ----YLDGE--------------QIQRYASKEVAKRIGLLAQNATTPGDITVQELvargryphQPLFTRWRKEDeeAVSR 126
Cdd:PLN03073 251 alqcVLNTDiertqlleeeaqlvAQQRELEFETETGKGKGANKDGVDKDAVSQRL--------EEIYKRLELID--AYTA 320
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490237141 127 AMKATGI-------TDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIsHQIDLLE 184
Cdd:PLN03073 321 EARAASIlaglsftPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL-HAVLWLE 384
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
43-242 |
3.84e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 41.53 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 43 GCGKSTLLRTLSRLMTPASGHVYLDGEQIQR------------YASkEVAKRIGLLAqnattpgDITVQE---LVARGRY 107
Cdd:PRK10762 288 GAGRTELMKVLYGALPRTSGYVTLDGHEVVTrspqdglangivYIS-EDRKRDGLVL-------GMSVKEnmsLTALRYF 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 108 PHQPLFTRwRKEDEEAVSRAMKATGI-TDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELL 186
Cdd:PRK10762 360 SRAGGSLK-HADEQQAVSDFIRLFNIkTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLI 438
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 187 SELnQQKGYTLAAVLHDLNQACRYATHLIALREGKIVAE----GAPKEIVSAELIEKIYG 242
Cdd:PRK10762 439 NQF-KAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGEftreQATQEKLMAAAVGKLNR 497
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
28-50 |
4.41e-04 |
|
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: 41.50 E-value: 4.41e-04
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
27-56 |
5.00e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 40.68 E-value: 5.00e-04
10 20 30
....*....|....*....|....*....|
gi 490237141 27 NVTIPDGHFTAIIGPNGCGKSTLLRTLSRL 56
Cdd:COG4637 15 DLELPLGPLTVLIGANGSGKSNLLDALRFL 44
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
27-63 |
6.48e-04 |
|
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: 40.25 E-value: 6.48e-04
10 20 30
....*....|....*....|....*....|....*...
gi 490237141 27 NVTIPDGH-FTAIIGPNGCGKSTLLRTLSRLMTPASGH 63
Cdd:cd03275 15 RHVIGPFDrFTCIIGPNGSGKSNLMDAISFVLGEKSSH 52
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
14-175 |
1.05e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.00 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 14 TLAYGKKTIAESLNVTIPDGHFTAIIGPNGCGKSTLLrtlsRLMT---PA--SGHVYLDGeqiQRYASKE----VAKRIG 84
Cdd:PRK10938 267 VVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLL----SLITgdhPQgySNDLTLFG---RRRGSGEtiwdIKKHIG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 85 LLAQN------ATTpgdiTVQELVARGRYP----HQPLFTRWRKEDEEAVSRamkaTGITD-LARQSVDTLSGGQRQRAW 153
Cdd:PRK10938 340 YVSSSlhldyrVST----SVRNVILSGFFDsigiYQAVSDRQQKLAQQWLDI----LGIDKrTADAPFHSLSWGQQRLAL 411
|
170 180
....*....|....*....|..
gi 490237141 154 IAMVLAQETAIMLLDEPTTWLD 175
Cdd:PRK10938 412 IVRALVKHPTLLILDEPLQGLD 433
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
24-222 |
1.17e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 39.41 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 24 ESLNVTIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEqiqryaskevakrIGLLAQNATTPGDITVQE--- 100
Cdd:PRK13546 41 DDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-------------VSVIAISAGLSGQLTGIEnie 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 101 --LVARGryphqplFTrwRKEDEEAVSRAMKATGITDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISH 178
Cdd:PRK13546 108 fkMLCMG-------FK--RKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTF 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490237141 179 QIDLLELLSELNQQkGYTLAAVLHDLNQACRYATHLIALREGKI 222
Cdd:PRK13546 179 AQKCLDKIYEFKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
27-50 |
1.36e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 38.63 E-value: 1.36e-03
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
113-192 |
1.55e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 39.53 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 113 FTRWRKEDEEA----VSRAMKATGI-TDLARQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLS 187
Cdd:PRK13549 370 FTGGSRIDDAAelktILESIQRLKVkTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLIN 449
|
....*
gi 490237141 188 ELNQQ 192
Cdd:PRK13549 450 QLVQQ 454
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
38-104 |
1.73e-03 |
|
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit of the type VII secretion protein EccC as found in the Actinobacteria. Type VII secretion is defined more broadly as including secretion systems for ESAT-6-like proteins in the Firmicutes as well as in the Actinobacteria, but this family does not show close homologs in the Firmicutes. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274859 [Multi-domain] Cd Length: 566 Bit Score: 39.59 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 38 IIGPNGCGKSTLLRTLSR--------------LMTPASGHV-YLDGEQIQRYA--SKEVAKRIGLLAQ--NATTPG-DIT 97
Cdd:TIGR03925 368 IFGDSESGKTTLLRTIARgivrryspdqarlvVVDYRRTLLgAVPEDYLAGYAatSAALTELIAALAAllERRLPGpDVT 447
|
....*..
gi 490237141 98 VQELVAR 104
Cdd:TIGR03925 448 PQQLRAR 454
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
139-230 |
2.72e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.04 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 139 QSVDTLSGGQRQRAWIAMVLAQE-TAIM-LLDEPTTWLDISHQIDLLELLSELNQQkGYTLAAVLHDlNQACRYATHLI- 215
Cdd:PRK00635 472 RALATLSGGEQERTALAKHLGAElIGITyILDEPSIGLHPQDTHKLINVIKKLRDQ-GNTVLLVEHD-EQMISLADRIId 549
|
90 100
....*....|....*....|
gi 490237141 216 -----ALREGKIVAEGAPKE 230
Cdd:PRK00635 550 igpgaGIFGGEVLFNGSPRE 569
|
|
| BMS1 |
COG5192 |
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ... |
31-58 |
2.75e-03 |
|
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227519 [Multi-domain] Cd Length: 1077 Bit Score: 38.95 E-value: 2.75e-03
10 20
....*....|....*....|....*...
gi 490237141 31 PDGHFTAIIGPNGCGKSTLLRTLSRLMT 58
Cdd:COG5192 67 PPPFIVAVVGPPGTGKSTLIRSLVRRFT 94
|
|
| AAA_14 |
pfam13173 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
37-75 |
2.82e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 463799 [Multi-domain] Cd Length: 128 Bit Score: 36.80 E-value: 2.82e-03
10 20 30
....*....|....*....|....*....|....*....
gi 490237141 37 AIIGPNGCGKSTLLRTLSRLMTPASGHVYLDGEQIQRYA 75
Cdd:pfam13173 6 VITGPRQVGKTTLLLQLIKELLPPENILYINLDDPRLLK 44
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
143-233 |
3.19e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 38.66 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490237141 143 TLSGGQRQRAWIAMVL---AQETAIMLLDEPTTWLDiSHQID-LLELLSELNQQkGYTLAAVLHDLNqACRYATHLIAL- 217
Cdd:PRK00635 809 SLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLH-THDIKaLIYVLQSLTHQ-GHTVVIIEHNMH-VVKVADYVLELg 885
|
90 100
....*....|....*....|.
gi 490237141 218 -----REGKIVAEGAPKEIVS 233
Cdd:PRK00635 886 peggnLGGYLLASCSPEELIH 906
|
|
| ABC_MutS_homologs |
cd03243 |
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair ... |
13-53 |
6.25e-03 |
|
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family also possess a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213210 [Multi-domain] Cd Length: 202 Bit Score: 36.84 E-value: 6.25e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 490237141 13 LTLAYGKKTIaeSLNVTIPDGHFTAIIGPNGCGKSTLLRTL 53
Cdd:cd03243 11 LALTKGETFV--PNDINLGSGRLLLITGPNMGGKSTYLRSI 49
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
16-47 |
8.15e-03 |
|
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: 8.15e-03
10 20 30
....*....|....*....|....*....|..
gi 490237141 16 AYGKKTIAESLNVTIPDGhFTAIIGPNGCGKS 47
Cdd:TIGR02168 7 LAGFKSFADPTTINFDKG-ITGIVGPNGCGKS 37
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