|
Name |
Accession |
Description |
Interval |
E-value |
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
10-262 |
1.49e-124 |
|
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: 354.74 E-value: 1.49e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLGILP 89
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 90 QSPLLPEGLTVYELVSRGRFPWQNFIRQWSDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILL 169
Cdd:COG1120 82 QEPPAPFGLTVRELVALGRYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 170 DEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVVRVLNEGEHCTPELVKAVFDVDVHA 249
Cdd:COG1120 162 DEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVYGVEARV 241
|
250
....*....|...
gi 446863618 250 SINPLTGKPFFMP 262
Cdd:COG1120 242 IEDPVTGRPLVLP 254
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
10-260 |
7.11e-102 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 297.31 E-value: 7.11e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLGILP 89
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 90 QSPLLPEGLTVYELVSRGRFPWQNFIRQWSDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILL 169
Cdd:PRK11231 83 QHHLTPEGITVRELVAYGRSPWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 170 DEPTTWLDLRYQVEILELLHDLtRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVVRVLNEGEHCTPELVKAVFDVDVHA 249
Cdd:PRK11231 163 DEPTTYLDINHQVELMRLMREL-NTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVFDVEAEI 241
|
250
....*....|.
gi 446863618 250 SINPLTGKPFF 260
Cdd:PRK11231 242 HPEPVSGTPMC 252
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
12-264 |
2.10e-90 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 268.10 E-value: 2.10e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 12 LDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLGILPQS 91
Cdd:COG4604 4 IKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 92 PLLPEGLTVYELVSRGRFPWqnfirqwS-----DADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPY 166
Cdd:COG4604 84 NHINSRLTVRELVAFGRFPY-------SkgrltAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 167 ILLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVVRVLNEGEHCTPELVKAVFDVD 246
Cdd:COG4604 157 VLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEVLSDIYDTD 236
|
250
....*....|....*...
gi 446863618 247 VHasINPLTGKPFFMPFR 264
Cdd:COG4604 237 IE--VEEIDGKRICVYFR 252
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
13-263 |
3.32e-83 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 250.29 E-value: 3.32e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 13 DNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLGILPQSP 92
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 93 LLPEGLTVYELVSRGRFPWQNFIRQWSDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEP 172
Cdd:PRK10253 91 TTPGDITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 173 TTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVVRVLNEGEHCTPELVKAVFDVDVHASIN 252
Cdd:PRK10253 171 TTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYGLRCMIIDD 250
|
250
....*....|.
gi 446863618 253 PLTGKPFFMPF 263
Cdd:PRK10253 251 PVAGTPLVVPL 261
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
12-225 |
7.91e-79 |
|
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: 235.79 E-value: 7.91e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 12 LDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLGILPQs 91
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 92 pllpegltvyelvsrgrfpwqnfirqwsdadeqaveeALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDE 171
Cdd:cd03214 81 -------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446863618 172 PTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
10-262 |
7.75e-72 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 220.76 E-value: 7.75e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLGILP 89
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 90 QSPLLPEGLTVYELVSRGRFPWqnfiRQWSDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQ------- 162
Cdd:COG4559 82 QHSSLAFPFTVEEVVALGRAPH----GSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQlwepvdg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 163 KTPYILLDEPTTWLDLRYQVEILELLHDLTRHhGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV------RVLnegehcTP 236
Cdd:COG4559 158 GPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVaqgtpeEVL------TD 230
|
250 260
....*....|....*....|....*.
gi 446863618 237 ELVKAVFDVDVHASINPLTGKPFFMP 262
Cdd:COG4559 231 ELLERVYGADLRVLAHPEGGCPQVLP 256
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
10-262 |
1.98e-69 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 214.64 E-value: 1.98e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLGILP 89
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 90 QSPLLPEGLTVYELVSRGRFPWqnfiRQWSDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQ------K 163
Cdd:PRK13548 83 QHSSLSFPFTVEEVVAMGRAPH----GLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepdgP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 164 TPYILLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVVRVLNEGEHCTPELVKAVF 243
Cdd:PRK13548 159 PRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPETLRRVY 238
|
250
....*....|....*....
gi 446863618 244 DVDVHASINPLTGKPFFMP 262
Cdd:PRK13548 239 GADVLVQPHPETGAPLVLP 257
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
3-225 |
1.07e-65 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 205.41 E-value: 1.07e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 3 HNAKGQGLILDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALS 82
Cdd:PRK10575 5 TNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 83 RRLGILPQSPLLPEGLTVYELVSRGRFPWQNFIRQWSDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQ 162
Cdd:PRK10575 85 RKVAYLPQQLPAAEGMTVRELVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQ 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446863618 163 KTPYILLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:PRK10575 165 DSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMI 227
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
10-248 |
3.27e-65 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 203.40 E-value: 3.27e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPtkalsRRLGILP 89
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRAR-----RRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 90 QSPLLPEG--LTVYELVSRGRFPWQNFIRQWSDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYI 167
Cdd:COG1121 82 QRAEVDWDfpITVRDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 168 LLDEPTTWLDLRYQVEILELLHDLtRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGkVVRVLNEGEHCTPELVKAVFDVDV 247
Cdd:COG1121 162 LLDEPFAGVDAATEEALYELLREL-RREGKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVLTPENLSRAYGGPV 239
|
.
gi 446863618 248 H 248
Cdd:COG1121 240 A 240
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
24-265 |
3.81e-61 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 198.14 E-value: 3.81e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 24 IVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLGILPQSPLLPEGLTVYEL 103
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLSFEFDVRQV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 104 VSRGRFPWQNFIRQWSDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDLRYQVE 183
Cdd:PRK09536 98 VEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 184 ILELLHDLTrHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVVRVLNEGEHCTPELVKAVFDVDVHASINPLTGKPFFMPF 263
Cdd:PRK09536 178 TLELVRRLV-DDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFDARTAVGTDPATGAPTVTPL 256
|
..
gi 446863618 264 RG 265
Cdd:PRK09536 257 PD 258
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
10-225 |
6.79e-58 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 184.88 E-value: 6.79e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYH-KKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALS---RRL 85
Cdd:COG3638 3 LELRNLSKRYPgGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRrlrRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 86 GILPQSPLLPEGLTVYELVSRGRFP----WQNFIRQWSDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLA 161
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNVLAGRLGrtstWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARALV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446863618 162 QKTPYILLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:COG3638 163 QEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVV 226
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
10-225 |
4.78e-57 |
|
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: 182.15 E-value: 4.78e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHK-KIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLGIL 88
Cdd:COG1122 1 IELENLSFSYPGgTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 89 PQSP---LLpeGLTVYELVSrgrFPWQNFirQWSDAD-EQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKT 164
Cdd:COG1122 81 FQNPddqLF--APTVEEDVA---FGPENL--GLPREEiRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446863618 165 PYILLDEPTTWLDLRYQVEILELLHDLtRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRL-NKEGKTVIIVTHDLDLVAELADRVIVLDDGRIV 213
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
12-224 |
6.67e-56 |
|
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: 178.88 E-value: 6.67e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 12 LDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKaiheqPTKALSRRLGILPQS 91
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK-----PLEKERKRIGYVPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 92 PLLPEG--LTVYELVSRGRFPWQNFIRQWSDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILL 169
Cdd:cd03235 77 RSIDRDfpISVRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446863618 170 DEPTTWLDLRYQVEILELLHDLTRhHGRTVVVVLHDLNFAVNYGDTLIFLRQGKV 224
Cdd:cd03235 157 DEPFAGVDPKTQEDIYELLRELRR-EGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
12-225 |
1.33e-54 |
|
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: 176.22 E-value: 1.33e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 12 LDNVSAGY-HKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALS---RRLGI 87
Cdd:cd03256 3 VENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRqlrRQIGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 88 LPQSPLLPEGLTVYELVSRGRFP----WQNFIRQWSDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQK 163
Cdd:cd03256 83 IFQQFNLIERLSVLENVLSGRLGrrstWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQ 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446863618 164 TPYILLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:cd03256 163 PKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
12-223 |
1.56e-53 |
|
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: 172.65 E-value: 1.56e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 12 LDNVSAGY--HKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLGILP 89
Cdd:cd03225 2 LKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 90 QSP---LLpeGLTVYELVSrgrFPWQNfiRQWSDAD-EQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTP 165
Cdd:cd03225 82 QNPddqFF--GPTVEEEVA---FGLEN--LGLPEEEiEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446863618 166 YILLDEPTTWLDLRYQVEILELLHDLtRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGK 223
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKL-KAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
10-246 |
8.73e-52 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 176.25 E-value: 8.73e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHKKI-----IVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIH---EQPTKAL 81
Cdd:COG1123 261 LEVRNLSKRYPVRGkggvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTklsRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 82 SRRLGILPQSPL--LPEGLTVYELVSrgrFPWQNFIRQWSDADEQAVEEALKLTG-TQEFAHLPVEKLSGGQRQRCWIAM 158
Cdd:COG1123 341 RRRVQMVFQDPYssLNPRMTVGDIIA---EPLRLHGLLSRAERRERVAELLERVGlPPDLADRYPHELSGGQRQRVAIAR 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 159 VLAQKTPYILLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV------RVLNEGE 232
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVedgpteEVFANPQ 497
|
250
....*....|....*
gi 446863618 233 H-CTPELVKAVFDVD 246
Cdd:COG1123 498 HpYTRALLAAVPSLD 512
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
10-225 |
4.11e-50 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 164.47 E-value: 4.11e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALsRRLGILP 89
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVR-RRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 90 QSPLLPEGLTVYELVsrgrfpwqNFIRQWSDAD----EQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTP 165
Cdd:COG1131 80 QEPALYPDLTVRENL--------RFFARLYGLPrkeaRERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 166 YILLDEPTTWLDLRYQVEILELLHDLtRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIV 210
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
10-225 |
1.44e-49 |
|
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: 163.49 E-value: 1.44e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALsRRLGILP 89
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREAR-RQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 90 QSPLLPEGLTVYELVsrgRFpwqnFIRQWSDADEQA---VEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPY 166
Cdd:COG4555 81 DERGLYDRLTVRENI---RY----FAELYGLFDEELkkrIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446863618 167 ILLDEPTTWLDLRYQVEILELLHDLtRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVV 211
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
10-224 |
9.49e-47 |
|
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: 155.34 E-value: 9.49e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVS----AGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALS--- 82
Cdd:cd03255 1 IELKNLSktygGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 83 -RRLGILPQSP-LLPEgLTVYE-----LVSRGRFPWQnfirqwsdaDEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCW 155
Cdd:cd03255 81 rRHIGFVFQSFnLLPD-LTALEnvelpLLLAGVPKKE---------RRERAEELLERVGLGDRLNHYPSELSGGQQQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446863618 156 IAMVLAQKTPYILLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAvNYGDTLIFLRQGKV 224
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
10-227 |
1.02e-46 |
|
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: 154.98 E-value: 1.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPtkALSRRLGILP 89
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVP--PERRNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 90 QSPLLPEGLTVYELVsrgRFPWQNfiRQWSDADEQA-VEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYIL 168
Cdd:cd03259 79 QDYALFPHLTVAENI---AFGLKL--RGVPKAEIRArVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446863618 169 LDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVVRV 227
Cdd:cd03259 154 LDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQV 212
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
10-224 |
1.85e-46 |
|
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: 153.32 E-value: 1.85e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALsRRLGILP 89
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVK-RRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 90 QSPLLPEGLTVYELVsrgrfpwqnfirqwsdadeqaveealkltgtqefahlpveKLSGGQRQRCWIAMVLAQKTPYILL 169
Cdd:cd03230 80 EEPSLYENLTVRENL----------------------------------------KLSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446863618 170 DEPTTWLDLRYQVEILELLHDLTRhHGRTVVVVLHDLNFAVNYGDTLIFLRQGKV 224
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKK-EGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
10-244 |
7.15e-46 |
|
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: 154.19 E-value: 7.15e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGY----HKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRL 85
Cdd:COG1124 2 LEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 86 GILPQSPL--LPEGLTVYELVS-----RGRfpwqnfirqwsDADEQAVEEALKLTG-TQEFAHLPVEKLSGGQRQRCWIA 157
Cdd:COG1124 82 QMVFQDPYasLHPRHTVDRILAeplriHGL-----------PDREERIAELLEQVGlPPSFLDRYPHQLSGGQRQRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 158 MVLAQKTPYILLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVVRVLNEGE----H 233
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADllagP 230
|
250
....*....|....
gi 446863618 234 CTP---ELVKAVFD 244
Cdd:COG1124 231 KHPytrELLAASLA 244
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
10-225 |
1.69e-45 |
|
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: 152.84 E-value: 1.69e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGY-HKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALS---RRL 85
Cdd:TIGR02315 2 LEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRklrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 86 GILPQSPLLPEGLTVYELVSRGRFPWQNFIR----QWSDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLA 161
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVLHGRLGYKPTWRsllgRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446863618 162 QKTPYILLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:TIGR02315 162 QQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIV 225
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
10-223 |
1.82e-45 |
|
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: 150.80 E-value: 1.82e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGK--AIHEQPTKALSRRLGI 87
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEdlTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 88 LPQSPLLPEGLTVYELVSRGrfpwqnfirqwsdadeqaveealkltgtqefahlpvekLSGGQRQRCWIAMVLAQKTPYI 167
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG--------------------------------------LSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446863618 168 LLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGK 223
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
18-207 |
5.09e-45 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 150.08 E-value: 5.09e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 18 GYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSIlldgkaiheqpTKALSRRLGILPQSPLLPEG 97
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----------RRAGGARVAYVPQRSEVPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 98 L--TVYELVSRGRFPWQNFIRQWSDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTW 175
Cdd:NF040873 70 LplTVRDLVAMGRWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190
....*....|....*....|....*....|..
gi 446863618 176 LDLRYQVEILELLHDLTRhHGRTVVVVLHDLN 207
Cdd:NF040873 150 LDAESRERIIALLAEEHA-RGATVVVVTHDLE 180
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
10-226 |
1.05e-44 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 150.58 E-value: 1.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVS----AGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALS--- 82
Cdd:COG1136 5 LELRNLTksygTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELArlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 83 -RRLGILPQSP-LLPEgLTVYELVsrgRFPWQnFIRQWSDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVL 160
Cdd:COG1136 85 rRHIGFVFQFFnLLPE-LTALENV---ALPLL-LAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446863618 161 AQKTPYILLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAvNYGDTLIFLRQGKVVR 226
Cdd:COG1136 160 VNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELA-ARADRVIRLRDGRIVS 224
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
12-225 |
3.48e-44 |
|
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: 149.36 E-value: 3.48e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 12 LDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALS---RRLGIL 88
Cdd:COG1127 8 VRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelrRRIGML 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 89 PQSPLLPEGLTVYELVSrgrFPwqnfIRQWSDADE----QAVEEALKLTGTQEFAHL-PVEkLSGGQRQRCWIAMVLAQK 163
Cdd:COG1127 88 FQGGALFDSLTVFENVA---FP----LREHTDLSEaeirELVLEKLELVGLPGAADKmPSE-LSGGMRKRVALARALALD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446863618 164 TPYILLDEPTTWLD---LRyqvEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:COG1127 160 PEILLYDEPTAGLDpitSA---VIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKII 221
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
10-235 |
3.66e-44 |
|
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: 156.84 E-value: 3.66e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHK-KIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLGIL 88
Cdd:COG4988 337 IELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 89 PQSPLLPEGlTVYELVSRGRfpwqnfirqwSDADEQAVEEALKLTGTQEF-AHLPV----------EKLSGGQRQRCWIA 157
Cdd:COG4988 417 PQNPYLFAG-TIRENLRLGR----------PDASDEELEAALEAAGLDEFvAALPDgldtplgeggRGLSGGQAQRLALA 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446863618 158 MVLAQKTPYILLDEPTTWLDLRYQVEILELLHDLTRhhGRTVVVVLHDLNFAVNYgDTLIFLRQGKVVRvlnEGEHCT 235
Cdd:COG4988 486 RALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQA-DRILVLDDGRIVE---QGTHEE 557
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
10-225 |
4.28e-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: 155.83 E-value: 4.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHK--KIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQP---MGGSILLDGKAIHEQPTKALSRR 84
Cdd:COG1123 5 LEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 85 LGILPQSP---LLPegLTVYELVsrgRFPWQNFIRQWSDADEQaVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLA 161
Cdd:COG1123 85 IGMVFQDPmtqLNP--VTVGDQI---AEALENLGLSRAEARAR-VLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446863618 162 QKTPYILLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIV 222
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
12-225 |
3.51e-43 |
|
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: 146.50 E-value: 3.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 12 LDNVSAGYHKKI----IVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIH---EQPTKALSRR 84
Cdd:cd03257 4 VKNLSVSFPTGGgsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLklsRRLRKIRRKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 85 LGILPQSPL--LPEGLTVYELVSRGRFPWQNFIRQWsDADEQAVEEALKLTGTQEFAH-LPVEkLSGGQRQRCWIAMVLA 161
Cdd:cd03257 84 IQMVFQDPMssLNPRMTIGEQIAEPLRIHGKLSKKE-ARKEAVLLLLVGVGLPEEVLNrYPHE-LSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446863618 162 QKTPYILLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
10-205 |
8.19e-43 |
|
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: 144.93 E-value: 8.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTkALSRRLGILP 89
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARE-DYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 90 QSPLLPEGLTVYELVsrgRFpWQNFIRQwsDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILL 169
Cdd:COG4133 82 HADGLKPELTVRENL---RF-WAALYGL--RADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 446863618 170 DEPTTWLDlryqVEILELLHDLTRHH---GRTVVVVLHD 205
Cdd:COG4133 156 DEPFTALD----AAGVALLAELIAAHlarGGAVLLTTHQ 190
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
12-224 |
5.27e-42 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 143.03 E-value: 5.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 12 LDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLGILPQS 91
Cdd:COG4619 3 LEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 92 PLLPEGlTVYELVsrgRFPWQNFIRQWSDADEQAVEEALKLTgtQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDE 171
Cdd:COG4619 83 PALWGG-TVRDNL---PFPFQLRERKFDRERALELLERLGLP--PDILDKPVERLSGGERQRLALIRALLLQPDVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446863618 172 PTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKV 224
Cdd:COG4619 157 PTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
12-254 |
1.56e-41 |
|
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: 142.64 E-value: 1.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 12 LDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIH---EQPTKALSRRLGIL 88
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglsEAELYRLRRRMGML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 89 PQSPLLPEGLTVYELVSrgrFPwqnfIRQWSDADE----QAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKT 164
Cdd:cd03261 83 FQSGALFDSLTVFENVA---FP----LREHTRLSEeeirEIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 165 PYILLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVVRvlnEGehcTPElvkavfd 244
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVA---EG---TPE------- 222
|
250
....*....|
gi 446863618 245 vDVHASINPL 254
Cdd:cd03261 223 -ELRASDDPL 231
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
9-225 |
2.69e-41 |
|
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: 149.15 E-value: 2.69e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 9 GLILDNVSAGY--HKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLG 86
Cdd:COG4987 333 SLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 87 ILPQSPLLPEGlTVYE--LVSRGrfpwqnfirqwsDADEQAVEEALKLTGTQEF-AHLPV----------EKLSGGQRQR 153
Cdd:COG4987 413 VVPQRPHLFDT-TLREnlRLARP------------DATDEELWAALERVGLGDWlAALPDgldtwlgeggRRLSGGERRR 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446863618 154 CWIAMVLAQKTPYILLDEPTTWLDLRYQVEILELLHDLTRhhGRTVVVVLHDLNfAVNYGDTLIFLRQGKVV 225
Cdd:COG4987 480 LALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLA-GLERMDRILVLEDGRIV 548
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
10-228 |
3.65e-41 |
|
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: 141.07 E-value: 3.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYH----KKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQptkalSRRL 85
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP-----GPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 86 GILPQSPLLPEGLTVYELVSrgrFPWQnfIRQWSDADEQA-VEEALKLTGTQEFAHL-PVEkLSGGQRQRCWIAMVLAQK 163
Cdd:cd03293 76 GYVFQQDALLPWLTVLDNVA---LGLE--LQGVPKAEARErAEELLELVGLSGFENAyPHQ-LSGGMRQRVALARALAVD 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446863618 164 TPYILLDEPTTWLD--LRYQVEilELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFL--RQGKVVRVL 228
Cdd:cd03293 150 PDVLLLDEPFSALDalTREQLQ--EELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAEV 216
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
25-241 |
5.32e-41 |
|
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: 141.04 E-value: 5.32e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 25 VDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAI-HEQPTKAlsRRLGILP--QSPLLPEGLTVY 101
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDItGLPPHEI--ARLGIGRtfQIPRLFPELTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 102 E------LVSRGRFPWQNFIRQWSDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTW 175
Cdd:cd03219 94 EnvmvaaQARTGSGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAG 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446863618 176 LDLRYQVEILELLHDLtRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGkvvRVLNEGehcTPELVKA 241
Cdd:cd03219 174 LNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQG---RVIAEG---TPDEVRN 232
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
12-223 |
9.35e-40 |
|
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: 135.45 E-value: 9.35e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 12 LDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLGILPQs 91
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 92 pllpegltvyelvsrgrfpwqnfirqwsdadeqaveealkltgtqefahlpvekLSGGQRQRCWIAMVLAQKTPYILLDE 171
Cdd:cd00267 81 ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446863618 172 PTTWLDLRYQVEILELLHDLTRhHGRTVVVVLHDLNFAVNYGDTLIFLRQGK 223
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAE-EGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
10-225 |
1.07e-39 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 146.13 E-value: 1.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGY--HKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLGI 87
Cdd:COG2274 474 IELENVSFRYpgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 88 LPQSPLLPEGlTVYElvsrgrfpwqNfIRQW-SDADEQAVEEALKLTGTQEF-AHLP----------VEKLSGGQRQRCW 155
Cdd:COG2274 554 VLQDVFLFSG-TIRE----------N-ITLGdPDATDEEIIEAARLAGLHDFiEALPmgydtvvgegGSNLSGGQRQRLA 621
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 156 IAMVLAQKTPYILLDEPTTWLDLRYQVEILELLHDLTRhhGRTVVVVLHDLNFAVNYgDTLIFLRQGKVV 225
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRLA-DRIIVLDKGRIV 688
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
10-226 |
2.58e-38 |
|
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: 133.47 E-value: 2.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHKKIIVDGVSFSVPtEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKaLSRRLGILP 89
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLG-PGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-LRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 90 QSPLLPEGLTVYELVSrgrfpWQNFIRQWSDADE-QAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYIL 168
Cdd:cd03264 79 QEFGVYPNFTVREFLD-----YIAWLKGIPSKEVkARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446863618 169 LDEPTTWLDLRYQVEILELLHDLTRhhGRTVVVVLHDLNFAVNYGDTLIFLRQGKVVR 226
Cdd:cd03264 154 VDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVF 209
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
12-225 |
3.69e-38 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 132.77 E-value: 3.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 12 LDNVSAGYHKKI-IVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEqptKALSRRLGILPQ 90
Cdd:cd03226 2 IENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 91 SP---LLPEglTVYELVSRGRFPwqnfirqwSDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYI 167
Cdd:cd03226 79 DVdyqLFTD--SVREELLLGLKE--------LDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446863618 168 LLDEPTTWLDLRYQVEILELLHDLTRhHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGELIRELAA-QGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
25-174 |
9.94e-38 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 130.08 E-value: 9.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 25 VDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLGILPQSPLLPEGLTVYELV 104
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446863618 105 SRGRFPWQNFirqwSDADEQAVEEALKLTGTQEFAHLPVEK----LSGGQRQRCWIAMVLAQKTPYILLDEPTT 174
Cdd:pfam00005 81 RLGLLLKGLS----KREKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
10-225 |
2.67e-37 |
|
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: 131.09 E-value: 2.67e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHK--KIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALsRRLGI 87
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAAR-QSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 88 LPQSPLLPEGLTVYELVS-----RGRFPWQNfirqwsdadEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQ 162
Cdd:cd03263 80 CPQFDALFDELTVREHLRfyarlKGLPKSEI---------KEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446863618 163 KTPYILLDEPTTWLDLRYQVEILELLHDLTRhhGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:cd03263 151 GPSVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
10-225 |
9.21e-37 |
|
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: 131.42 E-value: 9.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHK-----KIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAI-HEQPT--KAL 81
Cdd:TIGR04521 1 IKLKNVSYIYQPgtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDItAKKKKklKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 82 SRRLGILPQSP---LLPEglTVYELVSRGrfPwQNFirQWSDAD-EQAVEEALKLTGTQE--FAHLPVEkLSGGQRQRCW 155
Cdd:TIGR04521 81 RKKVGLVFQFPehqLFEE--TVYKDIAFG--P-KNL--GLSEEEaEERVKEALELVGLDEeyLERSPFE-LSGGQMRRVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 156 IAMVLAQKTPYILLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:TIGR04521 153 IAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIV 222
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
12-232 |
1.12e-36 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 129.40 E-value: 1.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 12 LDNVSAGYHKKI-IVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALS---RRLGI 87
Cdd:COG2884 4 FENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPylrRRIGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 88 LPQS-PLLPEgLTVYELVSrgrFPWQnfIRQWSDAD-EQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTP 165
Cdd:COG2884 84 VFQDfRLLPD-RTVYENVA---LPLR--VTGKSRKEiRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446863618 166 YILLDEPTTWLDLRYQVEILELLHDLTRhHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVVRVLNEGE 232
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEARGV 223
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
12-246 |
1.23e-36 |
|
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: 130.11 E-value: 1.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 12 LDNVSAGY-HKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLGILPQ 90
Cdd:cd03295 3 FENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 91 S-PLLPEgLTVyelvsrgrfpWQNF-----IRQWSDAD-EQAVEEALKLTG--TQEFAHLPVEKLSGGQRQRCWIAMVLA 161
Cdd:cd03295 83 QiGLFPH-MTV----------EENIalvpkLLKWPKEKiRERADELLALVGldPAEFADRYPHELSGGQQQRVGVARALA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 162 QKTPYILLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVVRVLNEGE---HCTPEL 238
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEilrSPANDF 231
|
....*...
gi 446863618 239 VKAVFDVD 246
Cdd:cd03295 232 VAEFVGAD 239
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
10-225 |
1.25e-36 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 129.48 E-value: 1.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRR-LGIL 88
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 89 PQSPLLPEGLTVYE---LVSRGRFPwqnfirqwsDADEQAVEEAL----KLtgtQEFAHLPVEKLSGGQRQRCWIAMVLA 161
Cdd:cd03224 81 PEGRRIFPELTVEEnllLGAYARRR---------AKRKARLERVYelfpRL---KERRKQLAGTLSGGEQQMLAIARALM 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446863618 162 QKTPYILLDEPTTWLDLRYQVEILELLHDLtRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:cd03224 149 SRPKLLLLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVV 211
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
10-223 |
1.56e-36 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 127.50 E-value: 1.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYH--KKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLGI 87
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 88 LPQSPLLPEGlTVYElvsrgrfpwqNFirqwsdadeqaveealkltgtqefahlpvekLSGGQRQRCWIAMVLAQKTPYI 167
Cdd:cd03228 81 VPQDPFLFSG-TIRE----------NI-------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446863618 168 LLDEPTTWLDLRYQVEILELLHDLTRhhGRTVVVVLHDLNfAVNYGDTLIFLRQGK 223
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLS-TIRDADRIIVLDDGR 171
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
25-241 |
2.97e-36 |
|
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: 129.39 E-value: 2.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 25 VDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRlGILP--QSPLLPEGLTVYE 102
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARL-GIARtfQNPRLFPELTVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 103 ------LVSRGRFPWQNFIRQWSDADEQA-----VEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDE 171
Cdd:COG0411 99 nvlvaaHARLGRGLLAALLRLPRARREERearerAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDE 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 172 PTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGkvvRVLNEGehcTPELVKA 241
Cdd:COG0411 179 PAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFG---RVIAEG---TPAEVRA 242
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
10-229 |
4.77e-36 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 129.05 E-value: 4.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHKK----IIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEqptkaLSRRL 85
Cdd:COG1116 8 LELRGVSKRFPTGgggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----PGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 86 GILPQSPLLpegltvyelvsrgrFPW----QN--F---IRQWSDAD-EQAVEEALKLTGTQEFA-HLPVEkLSGGQRQRC 154
Cdd:COG1116 83 GVVFQEPAL--------------LPWltvlDNvaLgleLRGVPKAErRERARELLELVGLAGFEdAYPHQ-LSGGMRQRV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446863618 155 WIAMVLAQKTPYILLDEPTTWLD--LRYQVEilELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFL--RQGKVVRVLN 229
Cdd:COG1116 148 AIARALANDPEVLLMDEPFGALDalTRERLQ--DELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLsaRPGRIVEEID 224
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
12-227 |
8.31e-36 |
|
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: 127.74 E-value: 8.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 12 LDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPtkALSRRLGILPQS 91
Cdd:cd03300 3 LENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLP--PHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 92 PLLPEGLTVYELVSrgrFPWQnfIRQWSDAD-EQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLD 170
Cdd:cd03300 81 YALFPHLTVFENIA---FGLR--LKKLPKAEiKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446863618 171 EPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVVRV 227
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQI 212
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
12-227 |
1.24e-35 |
|
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: 126.91 E-value: 1.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 12 LDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARIL-----QPMGGSILLDGKAIHEQPTK--ALSRR 84
Cdd:cd03260 3 LRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVDvlELRRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 85 LGILPQSP-LLPegLTVYELVSRGrfPWQNFIRqWSDADEQAVEEALKLTG-TQEFA-HLPVEKLSGGQRQRCWIAMVLA 161
Cdd:cd03260 83 VGMVFQKPnPFP--GSIYDNVAYG--LRLHGIK-LKEELDERVEEALRKAAlWDEVKdRLHALGLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446863618 162 QKTPYILLDEPTTWLDLRYQVEILELLHDLtrHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVVRV 227
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAEL--KKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEF 221
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
10-225 |
2.63e-35 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 129.45 E-value: 2.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKAlsRRLGILP 89
Cdd:COG3842 6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK--RNVGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 90 QSPLL-PEgLTVYELVsrgRFPWQnfIRQWSDAD-EQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYI 167
Cdd:COG3842 84 QDYALfPH-LTVAENV---AFGLR--MRGVPKAEiRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446863618 168 LLDEPTTWLD--LRY--QVEILELLHDLtrhhGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:COG3842 158 LLDEPLSALDakLREemREELRRLQREL----GITFIYVTHDQEEALALADRIAVMNDGRIE 215
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
10-225 |
3.16e-35 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 126.02 E-value: 3.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHKKIIvdGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKAlsRRLGILP 89
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--RPVSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 90 QSPLLPEGLTVYELVSRGRFPWQNFirqwSDADEQAVEEALKLTGTQEF-AHLPvEKLSGGQRQRCWIAMVLAQKTPYIL 168
Cdd:COG3840 78 QENNLFPHLTVAQNIGLGLRPGLKL----TAEQRAQVEQALERVGLAGLlDRLP-GQLSGGQRQRVALARCLVRKRPILL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446863618 169 LDEPTTWLD--LRYqvEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:COG3840 153 LDEPFSALDpaLRQ--EMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIA 209
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
12-225 |
9.16e-35 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 131.44 E-value: 9.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 12 LDNVSAGYHK-KIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLGILPQ 90
Cdd:COG1132 342 FENVSFSYPGdRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 91 SPLLPEGlTVYELVSRGRfpwqnfirqwSDADEQAVEEALKLTGTQEF-AHLP------VE----KLSGGQRQRCWIAMV 159
Cdd:COG1132 422 DTFLFSG-TIRENIRYGR----------PDATDEEVEEAAKAAQAHEFiEALPdgydtvVGergvNLSGGQRQRIAIARA 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446863618 160 LAQKTPYILLDEPTTWLDLRYQVEILELLHDLTRhhGRTVVVVLHDLNFAVNYgDTLIFLRQGKVV 225
Cdd:COG1132 491 LLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRNA-DRILVLDDGRIV 553
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
22-249 |
1.34e-34 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 125.71 E-value: 1.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 22 KIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARIL----QPMG----GSILLDGKAIHEQPTKALSRRLGILPQSPL 93
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggAPRGarvtGDVTLNGEPLAAIDAPRLARLRAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 94 LPEGLTVYELVSRGRFPWQNFIRQWSDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTP-------- 165
Cdd:PRK13547 94 PAFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQLWPphdaaqpp 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 166 -YILLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVVRVLNEGEHCTPELVKAVFD 244
Cdd:PRK13547 174 rYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLTPAHIARCYG 253
|
....*
gi 446863618 245 VDVHA 249
Cdd:PRK13547 254 FAVRL 258
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
10-219 |
1.70e-34 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 130.10 E-value: 1.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYH-KKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLGIL 88
Cdd:TIGR02857 322 LEFSGVSVAYPgRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 89 PQSPLLPEGlTVYELVSRGRfpwqnfirqwSDADEQAVEEALKLTGTQEFA-------HLPV----EKLSGGQRQRCWIA 157
Cdd:TIGR02857 402 PQHPFLFAG-TIAENIRLAR----------PDASDAEIREALERAGLDEFVaalpqglDTPIgeggAGLSGGQAQRLALA 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446863618 158 MVLAQKTPYILLDEPTTWLDLRYQVEILELLHDLTRhhGRTVVVVLHDLNFAVNYgDTLIFL 219
Cdd:TIGR02857 471 RAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALA-DRIVVL 529
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
10-233 |
3.17e-34 |
|
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: 123.49 E-value: 3.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYH-KKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLGIL 88
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 89 PQ-SPLLPEglTVYELVSRGRFpwqnfirqwsDADEQAVEEALKLTGTQEF-AHLPVE----------KLSGGQRQRCWI 156
Cdd:cd03253 81 PQdTVLFND--TIGYNIRYGRP----------DATDEEVIEAAKAAQIHDKiMRFPDGydtivgerglKLSGGEKQRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446863618 157 AMVLAQKTPYILLDEPTTWLDLRYQVEILELLHDLTRhhGRTVVVVLHDLNFAVNyGDTLIFLRQGKVVRvlnEGEH 233
Cdd:cd03253 149 ARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVE---RGTH 219
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
25-248 |
4.28e-34 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 123.41 E-value: 4.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 25 VDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILqPMGGSILLDGKAIHEQPTKALSRRLGILPQSPLLPEGLTVYELV 104
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 105 SRGRFPWQNfirqwSDADEQAVE---EALKLTgtqEFAHLPVEKLSGGQRQRCWIAMVLAQKTP-------YILLDEPTT 174
Cdd:COG4138 91 ALHQPAGAS-----SEAVEQLLAqlaEALGLE---DKLSRPLTQLSGGEWQRVRLAAVLLQVWPtinpegqLLLLDEPMN 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446863618 175 WLDLRYQVEILELLHDLTrHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVVRVLNEGEHCTPELVKAVFDVDVH 248
Cdd:COG4138 163 SLDVAQQAALDRLLRELC-QQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVFGVKFR 235
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
25-231 |
8.86e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 123.31 E-value: 8.86e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 25 VDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLGILPQSP---LLpeGLTVY 101
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDPddqVF--SSTVW 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 102 ELVSRGrfPwqnfIRQWSDADE--QAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDLR 179
Cdd:PRK13647 99 DDVAFG--P----VNMGLDKDEveRRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPR 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446863618 180 YQVEILELLHDLTRhHGRTVVVVLHDLNFAVNYGDTLIFLRQGkvvRVLNEG 231
Cdd:PRK13647 173 GQETLMEILDRLHN-QGKTVIVATHDVDLAAEWADQVIVLKEG---RVLAEG 220
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
12-224 |
8.99e-34 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 121.87 E-value: 8.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 12 LDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAI--HEQPTKALSRRLGILP 89
Cdd:cd03262 3 IKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 90 QSPLLPEGLTVYELVSRGrfPWQNFIRQWSDADEQAvEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILL 169
Cdd:cd03262 83 QQFNLFPHLTVLENITLA--PIKVKGMSKAEAEERA-LELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446863618 170 DEPTTWLDLRYQVEILELLHDLTrHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKV 224
Cdd:cd03262 160 DEPTSALDPELVGEVLDVMKDLA-EEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
12-225 |
3.37e-33 |
|
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: 121.11 E-value: 3.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 12 LDNVSAGYHKK---IIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLGIL 88
Cdd:cd03249 3 FKNVSFRYPSRpdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 89 PQSPLLPEGlTVYELVSRGRFpwqnfirqwsDADEQAVEEALKLTGTQEF-AHLPVE----------KLSGGQRQRCWIA 157
Cdd:cd03249 83 SQEPVLFDG-TIAENIRYGKP----------DATDEEVEEAAKKANIHDFiMSLPDGydtlvgergsQLSGGQKQRIAIA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446863618 158 MVLAQKTPYILLDEPTTWLDLRYQVEILELLHDLTRhhGRTVVVVLHDLNfAVNYGDTLIFLRQGKVV 225
Cdd:cd03249 152 RALLRNPKILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLS-TIRNADLIAVLQNGQVV 216
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
10-225 |
3.98e-33 |
|
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: 120.47 E-value: 3.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRlGILp 89
Cdd:COG0410 4 LEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARL-GIG- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 90 qspLLPEG------LTVYElvsrgrfpwqN-----FIRQWSDADEQAVEEAL----KLtgtQEFAHLPVEKLSGGQRQRC 154
Cdd:COG0410 82 ---YVPEGrrifpsLTVEE----------NlllgaYARRDRAEVRADLERVYelfpRL---KERRRQRAGTLSGGEQQML 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446863618 155 WIAMVLAQKTPYILLDEPTTWLDLRYQVEILELLHDLtRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:COG0410 146 AIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLERGRIV 215
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
12-233 |
6.01e-33 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 120.03 E-value: 6.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 12 LDNVSAGY--HKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLGILP 89
Cdd:cd03251 3 FKNVTFRYpgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 90 QSPLLPEGlTVYELVSRGRFpwqnfirqwsDADEQAVEEALKLTGTQEFA-------HLPVE----KLSGGQRQRCWIAM 158
Cdd:cd03251 83 QDVFLFND-TVAENIAYGRP----------GATREEVEEAARAANAHEFImelpegyDTVIGergvKLSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446863618 159 VLAQKTPYILLDEPTTWLDLRYQVEILELLHDLTRhhGRTVVVVLHDLNfAVNYGDTLIFLRQGKVVRvlnEGEH 233
Cdd:cd03251 152 ALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLS-TIENADRIVVLEDGKIVE---RGTH 220
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
10-225 |
1.01e-32 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 122.49 E-value: 1.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKAlsRRLGILP 89
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD--RNIAMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 90 QSP-LLPeGLTVYELVSrgrFPWQnfIRQWSDAD-EQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYI 167
Cdd:COG3839 82 QSYaLYP-HMTVYENIA---FPLK--LRKVPKAEiDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVF 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446863618 168 LLDEPTTWLD--LRYQ--VEILELLHDLtrhhGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:COG3839 156 LLDEPLSNLDakLRVEmrAEIKRLHRRL----GTTTIYVTHDQVEAMTLADRIAVMNDGRIQ 213
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
25-227 |
1.41e-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: 120.06 E-value: 1.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 25 VDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKAL----SRRLGILPQS-PLLPEgLT 99
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSfALLPH-RT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 100 VYELVSRGrFPWQNFIRQwsdADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDLR 179
Cdd:cd03294 119 VLENVAFG-LEVQGVPRA---EREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPL 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446863618 180 YQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVVRV 227
Cdd:cd03294 195 IRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQV 242
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
14-233 |
1.54e-32 |
|
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: 118.87 E-value: 1.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 14 NVSAGY-HKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLGILPQSP 92
Cdd:cd03254 7 NVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 93 LLPEGlTVYELVSRGRfpwqnfirqwSDADEQAVEEALKLTGTQEF-AHLP-------VEK---LSGGQRQRCWIAMVLA 161
Cdd:cd03254 87 FLFSG-TIMENIRLGR----------PNATDEEVIEAAKEAGAHDFiMKLPngydtvlGENggnLSQGERQLLAIARAML 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446863618 162 QKTPYILLDEPTTWLDLRYQVEILELLHDLTrhHGRTVVVVLHDLNFAVNyGDTLIFLRQGKVVRvlnEGEH 233
Cdd:cd03254 156 RDPKILILDEATSNIDTETEKLIQEALEKLM--KGRTSIIIAHRLSTIKN-ADKILVLDDGKIIE---EGTH 221
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
25-206 |
1.77e-32 |
|
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: 120.93 E-value: 1.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 25 VDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMG---GSILLDGKAIHEQPTKAL----SRRLGILPQSPL---- 93
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLLKLSEKELrkirGREIQMIFQDPMtsln 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 94 --------LPEGLTVYELVSRgrfpwqnfirqwSDADEQAVE--EALKLTGTQEFAHL-PVEkLSGGQRQRCWIAMVLAQ 162
Cdd:COG0444 101 pvmtvgdqIAEPLRIHGGLSK------------AEARERAIEllERVGLPDPERRLDRyPHE-LSGGMRQRVMIARALAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446863618 163 KtPYILL-DEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDL 206
Cdd:COG0444 168 E-PKLLIaDEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDL 211
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
10-244 |
6.54e-32 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 117.40 E-value: 6.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTK--ALSRRLGI 87
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDinKLRRKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 88 LPQSP-LLPEgLTVYELVSRGrfPWQnfIRQWS--DADEQAvEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKT 164
Cdd:COG1126 82 VFQQFnLFPH-LTVLENVTLA--PIK--VKKMSkaEAEERA-MELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 165 PYILLDEPTTWLDLRYQVEILELLHDLtRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVVrvlnegEHCTPElvkAVFD 244
Cdd:COG1126 156 KVMLFDEPTSALDPELVGEVLDVMRDL-AKEGMTMVVVTHEMGFAREVADRVVFMDGGRIV------EEGPPE---EFFE 225
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
12-225 |
6.88e-32 |
|
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: 116.92 E-value: 6.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 12 LDNVSAGY--HKKIIVDGVSFSV-PTEKMTVLvGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLGIL 88
Cdd:cd03245 5 FRNVSFSYpnQEIPALDNVSLTIrAGEKVAII-GRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 89 PQSPLLPEGlTVYELVSRGRfpwqnfirqwSDADEQAVEEALKLTGTQEFA--H-----LPV----EKLSGGQRQRCWIA 157
Cdd:cd03245 84 PQDVTLFYG-TLRDNITLGA----------PLADDERILRAAELAGVTDFVnkHpngldLQIgergRGLSGGQRQAVALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446863618 158 MVLAQKTPYILLDEPTTWLDLRYQVEILELLHDLTRHhgRTVVVVLHDLNFaVNYGDTLIFLRQGKVV 225
Cdd:cd03245 153 RALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGD--KTLIIITHRPSL-LDLVDRIIVMDSGRIV 217
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
10-227 |
9.36e-32 |
|
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: 116.59 E-value: 9.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKalSRRLGILP 89
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK--DRDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 90 QSPLLPEGLTVYE-----LVSRGRFPwqnfirqwsDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKT 164
Cdd:cd03301 79 QNYALYPHMTVYDniafgLKLRKVPK---------DEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446863618 165 PYILLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVVRV 227
Cdd:cd03301 150 KVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQI 212
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
10-229 |
4.03e-31 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 116.11 E-value: 4.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHK----KIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIheqpTKALSRRL 85
Cdd:COG4525 4 LTVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV----TGPGADRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 86 GILPQSPLLPeGLTVYELVSrgrFPWQnfIRQWSDADEQAV-EEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKT 164
Cdd:COG4525 80 VVFQKDALLP-WLNVLDNVA---FGLR--LRGVPKAERRARaEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446863618 165 PYILLDEPTTWLDL--RYQVEilELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFL--RQGKVVRVLN 229
Cdd:COG4525 154 RFLLMDEPFGALDAltREQMQ--ELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRIVERLE 220
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
25-225 |
1.05e-30 |
|
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: 114.00 E-value: 1.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 25 VDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALsRRLGILPQSPLLPEGLTVYELV 104
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEAR-RRLGFVSDSTGLYDRLTARENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 105 srgrfpwQNFIRQWS---DADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDLRYQ 181
Cdd:cd03266 100 -------EYFAGLYGlkgDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMAT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446863618 182 VEILELLHDLtRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:cd03266 173 RALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
5-206 |
1.29e-30 |
|
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: 119.39 E-value: 1.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 5 AKGQGLILDNVSAGY-HKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSR 83
Cdd:TIGR02868 330 LGKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 84 RLGILPQSPLLpEGLTVYELVSRGRfpwqnfirqwSDADEQAVEEALK-------LTGTQEFAHLPV----EKLSGGQRQ 152
Cdd:TIGR02868 410 RVSVCAQDAHL-FDTTVRENLRLAR----------PDATDEELWAALErvgladwLRALPDGLDTVLgeggARLSGGERQ 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446863618 153 RCWIAMVLAQKTPYILLDEPTTWLDLRYQVEILELLHDLTRhhGRTVVVVLHDL 206
Cdd:TIGR02868 479 RLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALS--GRTVVLITHHL 530
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
25-237 |
5.19e-30 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 113.57 E-value: 5.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 25 VDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLGILPQSP---LLpeGLTVY 101
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVFQNPdnqFV--GATVQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 102 ELVSrgrFPWQNfirQWSDADE--QAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDLR 179
Cdd:PRK13635 101 DDVA---FGLEN---IGVPREEmvERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPR 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446863618 180 YQVEILELLHDLTRHHGRTVVVVLHDLNFAVNyGDTLIFLRQGKvvrVLNEGehcTPE 237
Cdd:PRK13635 175 GRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGE---ILEEG---TPE 225
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
10-248 |
7.45e-30 |
|
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: 112.49 E-value: 7.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHKKIIVDGVSFSV-PTEKmTVLVGANGCGKSTLLSTIARILQPM-GGSILLDGK-----AIHEqptkaLS 82
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVkPGEH-WAILGPNGAGKSTLLSLITGDLPPTyGNDVRLFGErrggeDVWE-----LR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 83 RRLGILpqSPLL----PEGLTVYELV------SRGRFpwqnfiRQWSDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQ 152
Cdd:COG1119 78 KRIGLV--SPALqlrfPRDETVLDVVlsgffdSIGLY------REPTDEQRERARELLELLGLAHLADRPFGTLSQGEQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 153 RCWIAMVLAQKTPYILLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVVR------ 226
Cdd:COG1119 150 RVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAagpkee 229
|
250 260
....*....|....*....|..
gi 446863618 227 VLnegehcTPELVKAVFDVDVH 248
Cdd:COG1119 230 VL------TSENLSEAFGLPVE 245
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
17-246 |
1.86e-29 |
|
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: 115.94 E-value: 1.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 17 AGYHKkiIVDGVSFSVPtEKMTV-LVGANGCGKSTLLSTIARiLQPMGGSILLDGKAIHEQPTKA---LSRRLGILPQSP 92
Cdd:COG4172 296 VGHVK--AVDGVSLTLR-RGETLgLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQDLDGLSRRAlrpLRRRMQVVFQDP 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 93 ---LLP---------EGLTVYElvsrgrfpwqnfiRQWSDAD-EQAVEEALKLTG-TQEFAH-LPVEkLSGGQRQRCWIA 157
Cdd:COG4172 372 fgsLSPrmtvgqiiaEGLRVHG-------------PGLSAAErRARVAEALEEVGlDPAARHrYPHE-FSGGQRQRIAIA 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 158 MVLAQKTPYILLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNfAVNY-GDTLIFLRQGKVV------RVLNE 230
Cdd:COG4172 438 RALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLA-VVRAlAHRVMVMKDGKVVeqgpteQVFDA 516
|
250
....*....|....*..
gi 446863618 231 GEH-CTPELVKAVFDVD 246
Cdd:COG4172 517 PQHpYTRALLAAAPLLE 533
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
9-225 |
1.91e-29 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 113.70 E-value: 1.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 9 GLILDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGK--AIHEQPTKalsRRLG 86
Cdd:COG1118 2 SIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRdlFTNLPPRE---RRVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 87 ILPQSPLLPEGLTVYELVSRG-RfpwqnfIRQWSDADEQA-VEEALKLTGTQEFAH-LPVEkLSGGQRQRCWIAMVLAQK 163
Cdd:COG1118 79 FVFQHYALFPHMTVAENIAFGlR------VRPPSKAEIRArVEELLELVQLEGLADrYPSQ-LSGGQRQRVALARALAVE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446863618 164 TPYILLDEPTTWLD--LRYQVEilELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:COG1118 152 PEVLLLDEPFGALDakVRKELR--RWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIE 213
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
10-225 |
4.17e-29 |
|
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: 108.55 E-value: 4.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGY--HKKIIVDGVSFSV-PTEKMTVLvGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQpTKALSRRLG 86
Cdd:cd03247 1 LSINNVSFSYpeQEQQVLKNLSLELkQGEKIALL-GRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL-EKALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 87 ILPQSPLLPEGlTVYELVSRgrfpwqnfirqwsdadeqaveealkltgtqefahlpveKLSGGQRQRCWIAMVLAQKTPY 166
Cdd:cd03247 79 VLNQRPYLFDT-TLRNNLGR--------------------------------------RFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446863618 167 ILLDEPTTWLDLRYQVEILELLHDLTRhhGRTVVVVLHDLNfAVNYGDTLIFLRQGKVV 225
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLT-GIEHMDKILFLENGKII 175
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
4-220 |
5.84e-29 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 110.74 E-value: 5.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 4 NAKGQGLILDNVSAGYHK-KIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSIlldgkAIHEQPT-KAL 81
Cdd:PRK15056 1 MMQQAGIVVNDVTVTWRNgHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKI-----SILGQPTrQAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 82 SRRL-GILPQS-------PLLPEgltvyELVSRGRFPWQNFIRQWSDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQR 153
Cdd:PRK15056 76 QKNLvAYVPQSeevdwsfPVLVE-----DVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446863618 154 CWIAMVLAQKTPYILLDEPTTWLDLRYQVEILELLHDLtRHHGRTVVVVLHDLNFAVNYGDTLIFLR 220
Cdd:PRK15056 151 VFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDYTVMVK 216
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
9-207 |
8.38e-29 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 108.72 E-value: 8.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 9 GLILDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQP---MGGSILLDGKAIHEQPTKAlsRRL 85
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQ--RRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 86 GILPQSPLLPEGLTVyelvsrgrfpWQNFI----RQWSDADEQA-VEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVL 160
Cdd:COG4136 79 GILFQDDLLFPHLSV----------GENLAfalpPTIGRAQRRArVEQALEEAGLAGFADRDPATLSGGQRARVALLRAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446863618 161 AQKTPYILLDEPTTWLD--LRYQVeiLELLHDLTRHHGRTVVVVLHDLN 207
Cdd:COG4136 149 LAEPRALLLDEPFSKLDaaLRAQF--REFVFEQIRQRGIPALLVTHDEE 195
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-232 |
1.15e-28 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 110.10 E-value: 1.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 19 YHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIH--EQPTKALSRRLGILPQSPllPE 96
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDysKRGLLALRQQVATVFQDP--EQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 97 GLTVYELVSRGRFPWQNfIRQWSDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTWL 176
Cdd:PRK13638 89 QIFYTDIDSDIAFSLRN-LGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446863618 177 DLRYQVEILELLHDLTRhHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVVRVLNEGE 232
Cdd:PRK13638 168 DPAGRTQMIAIIRRIVA-QGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGE 222
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
25-232 |
1.25e-28 |
|
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: 108.61 E-value: 1.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 25 VDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKaLSRRLGILPQSPLLPEGLTVYE-L 103
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE-VRRRIGIVFQDLSVDDELTGWEnL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 104 VSRGRFpwqnFIRQWSDADEQaVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDLRYQVE 183
Cdd:cd03265 95 YIHARL----YGVPGAERRER-IDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAH 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446863618 184 ILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVVRVLNEGE 232
Cdd:cd03265 170 VWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
29-225 |
1.28e-28 |
|
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: 108.35 E-value: 1.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 29 SFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKAlsRRLGILPQSPLLPEGLTVYELVSRGR 108
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSMLFQENNLFAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 109 FPWQNFIRQwsdaDEQAVEEALKLTGTQEF-AHLPvEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDLRYQVEILEL 187
Cdd:cd03298 96 SPGLKLTAE----DRQAIEVALARVGLAGLeKRLP-GELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 446863618 188 LHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:cd03298 171 VLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
8-225 |
1.37e-28 |
|
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: 114.19 E-value: 1.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 8 QGLI-LDNVSAGY--HKKIIVDGVSFSV-PTEKMTVLvGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSR 83
Cdd:TIGR03375 461 QGEIeFRNVSFAYpgQETPALDNVSLTIrPGEKVAII-GRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRR 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 84 RLGILPQSPLLPEGlTVYE-LVSRGRFpwqnfirqwsdADEQAVEEALKLTGTQEFA--H-----LPV----EKLSGGQR 151
Cdd:TIGR03375 540 NIGYVPQDPRLFYG-TLRDnIALGAPY-----------ADDEEILRAAELAGVTEFVrrHpdgldMQIgergRSLSGGQR 607
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446863618 152 QRCWIAMVLAQKTPYILLDEPTTWLDLRYQVEILELLHDLTrhHGRTVVVVLHDLNFaVNYGDTLIFLRQGKVV 225
Cdd:TIGR03375 608 QAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWL--AGKTLVLVTHRTSL-LDLVDRIIVMDNGRIV 678
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
26-226 |
1.37e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 109.78 E-value: 1.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 26 DGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRR--LGILPQSP----LLPeglT 99
Cdd:PRK13639 19 KGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVRktVGIVFQNPddqlFAP---T 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 100 VYELVSRG----RFPwqnfirqwSDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTW 175
Cdd:PRK13639 96 VEEDVAFGplnlGLS--------KEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446863618 176 LDLRYQVEILELLHDLTRhHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVVR 226
Cdd:PRK13639 168 LDPMGASQIMKLLYDLNK-EGITIIISTHDVDLVPVYADKVYVMSDGKIIK 217
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
12-224 |
1.46e-28 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 109.33 E-value: 1.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 12 LDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARIL---QPMGGSILLDGKAIHEQPTKALSRR---- 84
Cdd:PRK09984 7 VEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQREGRLARDIRksra 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 85 -LGILPQSPLLPEGLTVYELV---SRGRFP-WQNFIRQWSDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMV 159
Cdd:PRK09984 87 nTGYIFQQFNLVNRLSVLENVligALGSTPfWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446863618 160 LAQKTPYILLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKV 224
Cdd:PRK09984 167 LMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
25-227 |
1.48e-28 |
|
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: 108.58 E-value: 1.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 25 VDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKalSRRLGILPQSPLLPEGLTVYELV 104
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFPHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 105 SRGrfpwqnFIRQWSD--ADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDLRYQV 182
Cdd:cd03299 93 AYG------LKKRKVDkkEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446863618 183 EILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVVRV 227
Cdd:cd03299 167 KLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQV 211
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-225 |
6.19e-28 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 107.43 E-value: 6.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 1 MAHNAKGQGLILD--NVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARI--LQP---MGGSILLDGKAI 73
Cdd:COG1117 1 MTAPASTLEPKIEvrNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPgarVEGEILLDGEDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 74 H--EQPTKALSRRLGILPQSP-LLPegLTVYELVSRGrfPWQNFIRQWSDADEqAVEEALKLtgtqefAHLPVE------ 144
Cdd:COG1117 81 YdpDVDVVELRRRVGMVFQKPnPFP--KSIYDNVAYG--LRLHGIKSKSELDE-IVEESLRK------AALWDEvkdrlk 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 145 ----KLSGGQRQR-CwIAMVLAQKTPYILLDEPTTWLD----LRyqVEilELLHDLTRHHgrTVVVVLHDLNFAVNYGDT 215
Cdd:COG1117 150 ksalGLSGGQQQRlC-IARALAVEPEVLLMDEPTSALDpistAK--IE--ELILELKKDY--TIVIVTHNMQQAARVSDY 222
|
250
....*....|
gi 446863618 216 LIFLRQGKVV 225
Cdd:COG1117 223 TAFFYLGELV 232
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
25-207 |
6.20e-28 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 109.05 E-value: 6.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 25 VDGVSFSVPtEKMTV-LVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPT---KALSRRLGIL---PQSPLLPEg 97
Cdd:COG4608 34 VDGVSFDIR-RGETLgLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGrelRPLRRRMQMVfqdPYASLNPR- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 98 LTVYELVSrgrFPWQNFiRQWSDAD-EQAVEEALKLTG-TQEFAH-LPVEkLSGGQRQRCWIAMVLAQKTPYILLDEPTT 174
Cdd:COG4608 112 MTVGDIIA---EPLRIH-GLASKAErRERVAELLELVGlRPEHADrYPHE-FSGGQRQRIGIARALALNPKLIVCDEPVS 186
|
170 180 190
....*....|....*....|....*....|...
gi 446863618 175 WLDLRYQVEILELLHDLTRHHGRTVVVVLHDLN 207
Cdd:COG4608 187 ALDVSIQAQVLNLLEDLQDELGLTYLFISHDLS 219
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
25-225 |
6.36e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 108.40 E-value: 6.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 25 VDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRR--LGILPQSP---LLPEglT 99
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKLResVGMVFQDPdnqLFSA--S 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 100 VYELVSRG----RFPwqnfirqwSDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTW 175
Cdd:PRK13636 100 VYQDVSFGavnlKLP--------EDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAG 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446863618 176 LDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:PRK13636 172 LDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVI 221
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
28-226 |
7.85e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 108.18 E-value: 7.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 28 VSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAI----HEQPTKALSRRLGIL---PQSPLLPEglTV 100
Cdd:PRK13634 26 VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLKPLRKKVGIVfqfPEHQLFEE--TV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 101 YELVSRGrfPwQNFIRQWSDADEQAvEEALKLTGTQE--FAHLPVEkLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDL 178
Cdd:PRK13634 104 EKDICFG--P-MNFGVSEEDAKQKA-REMIELVGLPEelLARSPFE-LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446863618 179 RYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVVR 226
Cdd:PRK13634 179 KGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFL 226
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
12-225 |
1.02e-27 |
|
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: 106.51 E-value: 1.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 12 LDNVSAGYH----KKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKAL---SRR 84
Cdd:cd03258 4 LKNVSKVFGdtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 85 LGILPQSPLLPEGLTVYELVSrgrFPWQnfIRQWSDAD-EQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQK 163
Cdd:cd03258 84 IGMIFQHFNLLSSRTVFENVA---LPLE--IAGVPKAEiEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446863618 164 tPYILL-DEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:cd03258 159 -PKVLLcDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVV 220
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
14-224 |
1.04e-27 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 106.72 E-value: 1.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 14 NVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLG---ILPQ 90
Cdd:PRK09493 6 NVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEagmVFQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 91 SPLLPEgLTVYELVSRGrfPWQnfIRQWS--DADEQAvEEALKLTGTQEFA-HLPVEkLSGGQRQRCWIAMVLAQKTPYI 167
Cdd:PRK09493 86 FYLFPH-LTALENVMFG--PLR--VRGASkeEAEKQA-RELLAKVGLAERAhHYPSE-LSGGQQQRVAIARALAVKPKLM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446863618 168 LLDEPTTWLDLRYQVEILELLHDLTrHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKV 224
Cdd:PRK09493 159 LFDEPTSALDPELRHEVLKVMQDLA-EEGMTMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
26-224 |
1.15e-27 |
|
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: 105.95 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 26 DGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKA---LSRRLGILPQSPLLPEGLTVYE 102
Cdd:cd03292 18 DGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRRKIGVVFQDFRLLPDRNVYE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 103 LVSrgrFPWQNFIRQWSDADEQaVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDLRYQV 182
Cdd:cd03292 98 NVA---FALEVTGVPPREIRKR-VPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTW 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446863618 183 EILELLHDLTRhHGRTVVVVLHDLNFAVNYGDTLIFLRQGKV 224
Cdd:cd03292 174 EIMNLLKKINK-AGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
10-225 |
1.69e-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: 105.68 E-value: 1.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRR-LGIL 88
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAgIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 89 PQSPLLPEGLTVYE--LVSRGRFPwqnfirqwsDADEQAVEEALKLTGT-QEFAHLPVEKLSGGQRQRCWIAMVLAQKTP 165
Cdd:TIGR03410 81 PQGREIFPRLTVEEnlLTGLAALP---------RRSRKIPDEIYELFPVlKEMLGRRGGDLSGGQQQQLAIARALVTRPK 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 166 YILLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:TIGR03410 152 LLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVV 211
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
12-224 |
1.99e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 106.76 E-value: 1.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 12 LDNVSAGYH--KKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLGILP 89
Cdd:PRK13648 10 FKNVSFQYQsdASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 90 QSPllpEGLTVYELVSRG-RFPWQNFIRQWSDADEQaVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYIL 168
Cdd:PRK13648 90 QNP---DNQFVGSIVKYDvAFGLENHAVPYDEMHRR-VSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVII 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446863618 169 LDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNyGDTLIFLRQGKV 224
Cdd:PRK13648 166 LDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTV 220
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
14-225 |
2.91e-27 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 104.61 E-value: 2.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 14 NVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIheQPTKALSRRLGILPQSPL 93
Cdd:cd03268 5 DLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY--QKNIEALRRIGALIEAPG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 94 LPEGLTVYE-LVSRGRFPwqnfirqwsDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEP 172
Cdd:cd03268 83 FYPNLTAREnLRLLARLL---------GIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446863618 173 TTWLDLRYQVEILELLHDLtRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:cd03268 154 TNGLDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
30-245 |
3.92e-27 |
|
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: 104.55 E-value: 3.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 30 FSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKaiheqPTKALSRRLGILPQS-------PLlpeglTVYE 102
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGA-----SPGKGWRHIGYVPQRhefawdfPI-----SVAH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 103 LVSRGRFPWQNFIRQWSDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDLRYQV 182
Cdd:TIGR03771 71 TVMSGRTGHIGWLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQE 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446863618 183 EILELLHDLTRhHGRTVVVVLHDLNFAVNYGDTLIFLrQGKVVRVLNEGEHCTPELVKAVFDV 245
Cdd:TIGR03771 151 LLTELFIELAG-AGTAILMTTHDLAQAMATCDRVVLL-NGRVIADGTPQQLQDPAPWMTTFGV 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
26-241 |
4.46e-27 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 108.95 E-value: 4.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 26 DGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQ-PTKALSRRLGILPQSPLLPEGLTVYELV 104
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRsPRDAQAAGIAIIHQELNLVPNLSVAENI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 105 SRGRFPWQNFIRQWSDADEQAvEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDLRyQVEI 184
Cdd:COG1129 101 FLGREPRRGGLIDWRAMRRRA-RELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTER-EVER 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 185 L-ELLHDLtRHHGRTVVVVLHDLN--FAVnyGDTLIFLRQGKVVRVLNEGEHCTPELVKA 241
Cdd:COG1129 179 LfRIIRRL-KAQGVAIIYISHRLDevFEI--ADRVTVLRDGRLVGTGPVAELTEDELVRL 235
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
14-227 |
5.21e-27 |
|
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: 104.73 E-value: 5.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 14 NVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKalSRRLGILPQSPL 93
Cdd:cd03296 7 NVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFVFQHYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 94 LPEGLTVYELVSRGRFPWQNFIRQWSDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPT 173
Cdd:cd03296 85 LFRHMTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPF 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446863618 174 TWLDLRYQVEI---LELLHDLTRHhgrTVVVVLHDLNFAVNYGDTLIFLRQGKVVRV 227
Cdd:cd03296 165 GALDAKVRKELrrwLRRLHDELHV---TTVFVTHDQEEALEVADRVVVMNKGRIEQV 218
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
12-232 |
6.78e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 105.07 E-value: 6.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 12 LDNVSAGYH--KKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLGILP 89
Cdd:PRK13632 10 VENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 90 QSP---LLpeGLTVYELVSrgrFPWQNfiRQWSDADEQA-VEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTP 165
Cdd:PRK13632 90 QNPdnqFI--GATVEDDIA---FGLEN--KKVPPKKMKDiIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446863618 166 YILLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNyGDTLIFLRQGKVVR------VLNEGE 232
Cdd:PRK13632 163 IIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAqgkpkeILNNKE 234
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
10-225 |
7.54e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 108.61 E-value: 7.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHKKIIVDGVSFSV-PTEKmTVLVGANGCGKSTLLSTIARILQPMGGSILLdGKAIheqptkalsrRLGIL 88
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIdRGDR-IGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------KIGYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 89 PQSP-LLPEGLTVYELVSRGRfpwqnfirqwSDADEQAVEEALK---LTGTQefAHLPVEKLSGGQRQRCWIAMVLAQKT 164
Cdd:COG0488 384 DQHQeELDPDKTVLDELRDGA----------PGGTEQEVRGYLGrflFSGDD--AFKPVGVLSGGEKARLALAKLLLSPP 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446863618 165 PYILLDEPTTWLDLryqvEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:COG0488 452 NVLLLDEPTNHLDI----ETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
22-204 |
8.44e-27 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 103.42 E-value: 8.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 22 KIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLGilPQSPLLPEgLTVY 101
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG--HRNAMKPA-LTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 102 ELVsrgRFpWQNFIrqwsDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDLRYQ 181
Cdd:PRK13539 92 ENL---EF-WAAFL----GGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAV 163
|
170 180
....*....|....*....|....*.
gi 446863618 182 veilELLHDLTRHH---GRTVVVVLH 204
Cdd:PRK13539 164 ----ALFAELIRAHlaqGGIVIAATH 185
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
12-205 |
1.21e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 107.84 E-value: 1.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 12 LDNVSAGYHKKIIVDGVSFSVPT-EKmtV-LVGANGCGKSTLLSTIARILQPMGGSILLDGKAiheqptkalsrRLGILP 89
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPgDR--IgLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL-----------RIGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 90 QSPLLPEGLTVYELVSRGRFPWQNFIRQW---------SDAD-------------------EQAVEEALKLTG-TQEFAH 140
Cdd:COG0488 68 QEPPLDDDLTVLDTVLDGDAELRALEAELeeleaklaePDEDlerlaelqeefealggweaEARAEEILSGLGfPEEDLD 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446863618 141 LPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDLryqvEILELLHDLTRHHGRTVVVVLHD 205
Cdd:COG0488 148 RPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL----ESIEWLEEFLKNYPGTVLVVSHD 208
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
21-225 |
2.07e-26 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 102.73 E-value: 2.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 21 KKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMG---GSILLDGKAIHEQPTKalsRRLGILPQSPLLPEG 97
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKPDQFQ---KCVAYVRQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 98 LTVYE-----LVSRGRFPWQNFIRQWSDADEqaveeALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEP 172
Cdd:cd03234 96 LTVREtltytAILRLPRKSSDAIRKKRVEDV-----LLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446863618 173 TTWLDLRYQVEILELLHDLTRhHGRTVVVVLH----DLnfaVNYGDTLIFLRQGKVV 225
Cdd:cd03234 171 TSGLDSFTALNLVSTLSQLAR-RNRIVILTIHqprsDL---FRLFDRILLLSSGEIV 223
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
25-225 |
2.48e-26 |
|
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: 107.49 E-value: 2.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 25 VDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLGILPQSPLLPEGlTVYELV 104
Cdd:TIGR02203 348 LDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFND-TIANNI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 105 SRGRFpwqnfirqwSDADEQAVEEALKLTGTQEFA-------HLPV----EKLSGGQRQRCWIAMVLAQKTPYILLDEPT 173
Cdd:TIGR02203 427 AYGRT---------EQADRAEIERALAAAYAQDFVdklplglDTPIgengVLLSGGQRQRLAIARALLKDAPILILDEAT 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446863618 174 TWLDLRYQVEILELLHDLTRhhGRTVVVVLHDLNfAVNYGDTLIFLRQGKVV 225
Cdd:TIGR02203 498 SALDNESERLVQAALERLMQ--GRTTLVIAHRLS-TIEKADRIVVMDDGRIV 546
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
14-227 |
2.54e-26 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 105.69 E-value: 2.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 14 NVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPtkALSRRLGILPQSPL 93
Cdd:PRK11607 24 NLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP--PYQRPINMMFQSYA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 94 LPEGLTVYELVSRG----RFPwqnfirqwSDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILL 169
Cdd:PRK11607 102 LFPHMTVEQNIAFGlkqdKLP--------KAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446863618 170 DEPTTWLDL----RYQVEILELLHDLtrhhGRTVVVVLHDLNFAVNYGDTLIFLRQGKVVRV 227
Cdd:PRK11607 174 DEPMGALDKklrdRMQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQI 231
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
13-225 |
2.74e-26 |
|
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: 107.21 E-value: 2.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 13 DNVSAGYH-KKIIVDGVSFSVPTEKMTVLVGANGCGKstllSTIARIL----QPMGGSILLDGKAIHEQPTKALSRRLGI 87
Cdd:COG5265 361 ENVSFGYDpERPILKGVSFEVPAGKTVAIVGPSGAGK----STLARLLfrfyDVTSGRILIDGQDIRDVTQASLRAAIGI 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 88 LPQSPLLPEGlTVYELVSRGRfPwqnfirqwsDADEQAVEEALKLTGTQEF-AHLP------V-E---KLSGGQRQRCWI 156
Cdd:COG5265 437 VPQDTVLFND-TIAYNIAYGR-P---------DASEEEVEAAARAAQIHDFiESLPdgydtrVgErglKLSGGEKQRVAI 505
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446863618 157 AMVLAQKTPYILLDEPTTWLDLRYQVEILELLHDLTRhhGRTVVVVLHDLNFAVNyGDTLIFLRQGKVV 225
Cdd:COG5265 506 ARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTIVD-ADEILVLEAGRIV 571
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
28-248 |
2.78e-26 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 103.09 E-value: 2.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 28 VSFSVPTEKMTVLVGANGCGKSTLLSTIARILqPMGGSILLDGKAIHEQPTKALSRRLGILPQSPLLPEGLTVYELVSRG 107
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 108 RFPWQNfirqwSDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYI-------LLDEPTTWLDLRY 180
Cdd:PRK03695 94 QPDKTR-----TEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQVWPDInpagqllLLDEPMNSLDVAQ 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446863618 181 QVEILELLHDLTRhHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVVRVLNEGEHCTPELVKAVFDVDVH 248
Cdd:PRK03695 169 QAALDRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVFGVNFR 235
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
28-225 |
3.43e-26 |
|
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: 101.99 E-value: 3.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 28 VSFSVPTEkMTVLVGANGCGKSTLLSTIARILQPMGGSILLDG-------KAIHEQPTKalsRRLGILPQSPLLPEGLTV 100
Cdd:cd03297 17 IDFDLNEE-VTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrKKINLPPQQ---RKIGLVFQQYALFPHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 101 YELVSRGrfpwqnFIRQWSDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLD--L 178
Cdd:cd03297 93 RENLAFG------LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDraL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446863618 179 RYQveILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:cd03297 167 RLQ--LLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
18-225 |
3.49e-26 |
|
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: 101.47 E-value: 3.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 18 GYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIA--RILQPMGGSILLDGKAIHEQptkALSRRLGILPQSPLLP 95
Cdd:cd03213 18 SKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLDKR---SFRKIIGYVPQDDILH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 96 EGLTVYElvsrgrfpwqnfirqwsdadeqAVEEALKLTGtqefahlpvekLSGGQRQRCWIAMVLAQKTPYILLDEPTTW 175
Cdd:cd03213 95 PTLTVRE----------------------TLMFAAKLRG-----------LSGGERKRVSIALELVSNPSLLFLDEPTSG 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446863618 176 LDLRYQVEILELLHDLtRHHGRTVVVVLHDL-NFAVNYGDTLIFLRQGKVV 225
Cdd:cd03213 142 LDSSSALQVMSLLRRL-ADTGRTIICSIHQPsSEIFELFDKLLLLSQGRVI 191
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
40-227 |
5.45e-26 |
|
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: 104.11 E-value: 5.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 40 LVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPtkALSRRLGILPQSPLLPEGLTVYELVSrgrFPWQnfiRQWS 119
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVP--PHLRHINMVFQSYALFPHMTVEENVA---FGLK---MRKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 120 DADEQA--VEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLD--LRYQVEiLElLHDLTRHH 195
Cdd:TIGR01187 73 PRAEIKprVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDkkLRDQMQ-LE-LKTIQEQL 150
|
170 180 190
....*....|....*....|....*....|..
gi 446863618 196 GRTVVVVLHDLNFAVNYGDTLIFLRQGKVVRV 227
Cdd:TIGR01187 151 GITFVFVTHDQEEAMTMSDRIAIMRKGKIAQI 182
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
24-209 |
9.72e-26 |
|
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: 100.97 E-value: 9.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 24 IVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIH----EQPTKALSRRLGILPQS-PLLPeGL 98
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFaldeDARARLRARHVGFVFQSfQLLP-TL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 99 TVYELVS-----RGRfpwqnfirqwSDADEQAvEEALKLTGTQE-FAHLPVEkLSGGQRQRCWIAMVLAQKTPYILLDEP 172
Cdd:COG4181 106 TALENVMlplelAGR----------RDARARA-RALLERVGLGHrLDHYPAQ-LSGGEQQRVALARAFATEPAILFADEP 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 446863618 173 TTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFA 209
Cdd:COG4181 174 TGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA 210
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
24-225 |
1.59e-25 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 104.77 E-value: 1.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 24 IVDGVSFSVPTEKMTVLVGANGCGKS-TLLStIARILQP----MGGSILLDGKAIHEQPTKALSR----RLGILPQSPL- 93
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSvTALS-ILRLLPDpaahPSGSILFDGQDLLGLSERELRRirgnRIAMIFQEPMt 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 94 -----------LPEGLTVYELVSRgrfpwqnfirqwsDADEQAVEEALKLTGTQE-------FAHlpveKLSGGQRQRCW 155
Cdd:COG4172 104 slnplhtigkqIAEVLRLHRGLSG-------------AAARARALELLERVGIPDperrldaYPH----QLSGGQRQRVM 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446863618 156 IAMVLAQKtPYILL-DEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:COG4172 167 IAMALANE-PDLLIaDEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIV 236
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
12-225 |
2.22e-25 |
|
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: 98.27 E-value: 2.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 12 LDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIH-EQPTKAlsRRLGIlpq 90
Cdd:cd03216 3 LRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSfASPRDA--RRAGI--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 91 spllpegLTVYElvsrgrfpwqnfirqwsdadeqaveealkltgtqefahlpvekLSGGQRQRCWIAMVLAQKTPYILLD 170
Cdd:cd03216 78 -------AMVYQ-------------------------------------------LSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446863618 171 EPTTWLDLRYQVEILELLHDLTRhHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:cd03216 108 EPTAALTPAEVERLFKVIRRLRA-QGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
25-222 |
2.52e-25 |
|
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: 100.23 E-value: 2.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 25 VDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIheqpTKALSRRLGILPQSPLLPeGLTVYELV 104
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI----TEPGPDRMVVFQNYSLLP-WLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 105 SrgrFPWQNFIRQWSDADEQA-VEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDLRYQVE 183
Cdd:TIGR01184 76 A---LAVDRVLPDLSKSERRAiVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 446863618 184 ILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQG 222
Cdd:TIGR01184 153 LQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
10-219 |
4.93e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 99.02 E-value: 4.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLGILP 89
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 90 QSPLLpEGLTVYE-LVsrgrFPWQnfIRQwsdadeQAVEEALKLTGTQEFAhLP-------VEKLSGGQRQRcwIAMVL- 160
Cdd:PRK10247 88 QTPTL-FGDTVYDnLI----FPWQ--IRN------QQPDPAIFLDDLERFA-LPdtiltknIAELSGGEKQR--ISLIRn 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 161 AQKTPYI-LLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNfAVNYGDTLIFL 219
Cdd:PRK10247 152 LQFMPKVlLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKD-EINHADKVITL 210
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-227 |
8.11e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 99.22 E-value: 8.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 24 IVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQ-----PMGGSILLDGKAIHEQPTKALSRRLGILPQSPLLPEGL 98
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPIPNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 99 TVYELVSRGrfPWQNFIRQWSDADEQAVEEALkltgtqEFAHL----------PVEKLSGGQRQRCWIAMVLAQKTPYIL 168
Cdd:PRK14247 98 SIFENVALG--LKLNRLVKSKKELQERVRWAL------EKAQLwdevkdrldaPAGKLSGGQQQRLCIARALAFQPEVLL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446863618 169 LDEPTTWLDLRYQVEILELLHDLTRHhgRTVVVVLHDLNFAVNYGDTLIFLRQGKVVRV 227
Cdd:PRK14247 170 ADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEW 226
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
6-226 |
1.12e-24 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 102.52 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 6 KGQgLILDNVSAGY--HKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSR 83
Cdd:COG4618 328 KGR-LSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 84 RLGILPQSPLLPEGlTVYELVSrgRFPwqnfirqwsDADEQAVEEALKLTGTQEF-AHLP----------VEKLSGGQRQ 152
Cdd:COG4618 407 HIGYLPQDVELFDG-TIAENIA--RFG---------DADPEKVVAAAKLAGVHEMiLRLPdgydtrigegGARLSGGQRQ 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 153 RCWIAMVLAQKTPYILLDEPTTWLD------LRYQVEILellhdltRHHGRTVVVVLHDLNfAVNYGDTLIFLRQGKVVR 226
Cdd:COG4618 475 RIGLARALYGDPRLVVLDEPNSNLDdegeaaLAAAIRAL-------KARGATVVVITHRPS-LLAAVDKLLVLRDGRVQA 546
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
12-224 |
1.42e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 99.04 E-value: 1.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 12 LDNVSAGYHK---KIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLGIL 88
Cdd:PRK13650 7 VKNLTFKYKEdqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 89 PQSP----------------LLPEGLTVYELVSRgrfpwqnfirqwsdadeqaVEEALKLTGTQEFAHLPVEKLSGGQRQ 152
Cdd:PRK13650 87 FQNPdnqfvgatveddvafgLENKGIPHEEMKER-------------------VNEALELVGMQDFKEREPARLSGGQKQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446863618 153 RCWIAMVLAQKTPYILLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNfAVNYGDTLIFLRQGKV 224
Cdd:PRK13650 148 RVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLD-EVALSDRVLVMKNGQV 218
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
10-232 |
2.69e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 98.23 E-value: 2.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHK-----KIIVDGVSFSVPT-EKMTVlVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSR 83
Cdd:COG1101 2 LELKNLSKTFNPgtvneKRALDGLNLTIEEgDFVTV-IGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 84 RLGILPQSPLL--PEGLTVYELVS----RGRFPwqNFIRQWSDADEQAVEEALKLTGTQEFAHL--PVEKLSGGQRQRcw 155
Cdd:COG1101 81 YIGRVFQDPMMgtAPSMTIEENLAlayrRGKRR--GLRRGLTKKRRELFRELLATLGLGLENRLdtKVGLLSGGQRQA-- 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446863618 156 IAMVLAQ-KTPYIL-LDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVVRVLNEGE 232
Cdd:COG1101 157 LSLLMATlTKPKLLlLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIILDVSGEE 235
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
10-222 |
3.06e-24 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 97.85 E-value: 3.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKaiheqPTKALSRRLGILP 89
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK-----PVEGPGAERGVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 90 QSpllpEGLtvyelvsrgrFPWQN------FIRQWSDAD----EQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMV 159
Cdd:PRK11248 77 QN----EGL----------LPWRNvqdnvaFGLQLAGVEkmqrLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446863618 160 LAQKTPYILLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQG 222
Cdd:PRK11248 143 LAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-224 |
3.51e-24 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 97.83 E-value: 3.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 6 KGQGLILDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSiLLDGKAiheqPTKALSRRL 85
Cdd:PRK11247 9 QGTPLLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-LLAGTA----PLAEAREDT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 86 GILPQSPLLpegltvyelvsrgrFPWQNFIR--------QWSDADEQAVEEalklTGTQEFAHLPVEKLSGGQRQRCWIA 157
Cdd:PRK11247 84 RLMFQDARL--------------LPWKKVIDnvglglkgQWRDAALQALAA----VGLADRANEWPAALSGGQKQRVALA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446863618 158 MVLAQKTPYILLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKV 224
Cdd:PRK11247 146 RALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
14-224 |
6.83e-24 |
|
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: 96.00 E-value: 6.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 14 NVSAGYHKK---IIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLGILPQ 90
Cdd:cd03248 16 NVTFAYPTRpdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 91 SPLLPEGlTVYELVSRGrfpwqnfirqWSDADEQAVEEALKLTGT----QEFAHLPVE-------KLSGGQRQRCWIAMV 159
Cdd:cd03248 96 EPVLFAR-SLQDNIAYG----------LQSCSFECVKEAAQKAHAhsfiSELASGYDTevgekgsQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446863618 160 LAQKTPYILLDEPTTWLDLRYQVEILELLHDltRHHGRTVVVVLHDLNfAVNYGDTLIFLRQGKV 224
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALYD--WPERRTVLVIAHRLS-TVERADQILVLDGGRI 226
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
13-225 |
7.51e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 97.08 E-value: 7.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 13 DNVSAGYHK------KIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDG-KAIHEQPTKALSRRL 85
Cdd:PRK13633 8 KNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGlDTSDEENLWDIRNKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 86 GILPQSP--------------LLPEGLTVYELVSRGRfpwqnfirqwsdadeqaVEEALKLTGTQEFAHLPVEKLSGGQR 151
Cdd:PRK13633 88 GMVFQNPdnqivativeedvaFGPENLGIPPEEIRER-----------------VDESLKKVGMYEYRRHAPHLLSGGQK 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446863618 152 QRCWIAMVLAQKTPYILLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNyGDTLIFLRQGKVV 225
Cdd:PRK13633 151 QRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVV 223
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
21-243 |
8.97e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 97.21 E-value: 8.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 21 KKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPT----KALSRRLGIL---PQSPL 93
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGnknlKKLRKKVSLVfqfPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 94 LPEglTVYELVSRGrfPwQNFIRQWSDADEQAVEeALKLTGTQE--FAHLPVEkLSGGQRQRCWIAMVLAQKTPYILLDE 171
Cdd:PRK13641 99 FEN--TVLKDVEFG--P-KNFGFSEDEAKEKALK-WLKKVGLSEdlISKSPFE-LSGGQMRRVAIAGVMAYEPEILCLDE 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446863618 172 PTTWLDLRYQVEILELLHDLTRhHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVVRvlnegeHCTPelvKAVF 243
Cdd:PRK13641 172 PAAGLDPEGRKEMMQLFKDYQK-AGHTVILVTHNMDDVAEYADDVLVLEHGKLIK------HASP---KEIF 233
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
9-225 |
1.17e-23 |
|
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: 95.25 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 9 GLI-LDNVSAGY--HKKIIVDGVSFSV-PTEKMTVlVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRR 84
Cdd:cd03244 1 GDIeFKNVSLRYrpNLPPVLKNISFSIkPGEKVGI-VGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 85 LGILPQSPLLPEGlTVyelvsrgRF---PWQnfirQWSDADeqaVEEALKLTGTQEFAHLPVEKL-----------SGGQ 150
Cdd:cd03244 80 ISIIPQDPVLFSG-TI-------RSnldPFG----EYSDEE---LWQALERVGLKEFVESLPGGLdtvveeggenlSVGQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446863618 151 RQRCWIAMVLAQKTPYILLDEPTTWLDlryqVEILELLHDLTRHH--GRTVVVVLHDLNFAVNYgDTLIFLRQGKVV 225
Cdd:cd03244 145 RQLLCLARALLRKSKILVLDEATASVD----PETDALIQKTIREAfkDCTVLTIAHRLDTIIDS-DRILVLDKGRVV 216
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
8-225 |
1.51e-23 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 95.92 E-value: 1.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 8 QGLILDNVSAGYHKkIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQP----MGGSILLDGKAIHeqPTKALSR 83
Cdd:PRK10418 3 QQIELRNIALQAAQ-PLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVA--PCALRGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 84 RLGIL---PQSPLLPegltVYELVSRGRFPWQNFIRQWSDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVL 160
Cdd:PRK10418 80 KIATImqnPRSAFNP----LHTMHTHARETCLALGKPADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRMMIALAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446863618 161 AQKTPYILLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:PRK10418 156 LCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIV 220
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
10-207 |
1.77e-23 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 94.35 E-value: 1.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQpTKALSRRLGILP 89
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQ-RDEPHENILYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 90 QSPLLPEGLTVYELVSrgrfpwqnFIRQWSDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILL 169
Cdd:TIGR01189 80 HLPGLKPELSALENLH--------FWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWIL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446863618 170 DEPTTWLDlRYQVEILEllHDLTRHHGRTVVVVL---HDLN 207
Cdd:TIGR01189 152 DEPTTALD-KAGVALLA--GLLRAHLARGGIVLLtthQDLG 189
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
21-225 |
2.23e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 96.02 E-value: 2.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 21 KKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQP---MGGSILLDGKAIHEQPTKALSRRLGILPQSPLLP-E 96
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIREKVGIVFQNPDNQfV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 97 GLTVYELVSRG----RFPWQNFIRqwsdadeqAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEP 172
Cdd:PRK13640 99 GATVGDDVAFGlenrAVPRPEMIK--------IVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDES 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446863618 173 TTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAvNYGDTLIFLRQGKVV 225
Cdd:PRK13640 171 TSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLL 222
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
10-227 |
5.06e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 94.46 E-value: 5.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARI--LQP---MGGSILLDGKAIHEQPTKA--LS 82
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPevtITGSIVYNGHNIYSPRTDTvdLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 83 RRLGILPQSPLlPEGLTVYELVSRG-RFpwqNFIRQWSDADEqAVEEALKLTG----TQEFAHLPVEKLSGGQRQRCWIA 157
Cdd:PRK14239 86 KEIGMVFQQPN-PFPMSIYENVVYGlRL---KGIKDKQVLDE-AVEKSLKGASiwdeVKDRLHDSALGLSGGQQQRVCIA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 158 MVLAQKTPYILLDEPTTWLDLRYQVEILELLHDLTRHHgrTVVVVLHDLNFAVNYGDTLIFLRQGKVVRV 227
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEY 228
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
10-224 |
5.62e-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: 5.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGY--HKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLGI 87
Cdd:cd03246 1 LEVENVSFRYpgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 88 LPQSPLLPEGlTVYELVsrgrfpwqnfirqwsdadeqaveealkltgtqefahlpvekLSGGQRQRCWIAMVLAQKTPYI 167
Cdd:cd03246 81 LPQDDELFSG-SIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446863618 168 LLDEPTTWLDLRYQVEILELLHDLtRHHGRTVVVVLHDLNfAVNYGDTLIFLRQGKV 224
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPE-TLASADRILVLEDGRV 173
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
19-206 |
7.17e-23 |
|
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: 93.55 E-value: 7.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 19 YHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLGILPQSPLLPEGL 98
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKTQLWWDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 99 TV---YELVSRgrfpwqnfIRQWSDADEQA-VEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTT 174
Cdd:cd03267 111 PVidsFYLLAA--------IYDLPPARFKKrLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTI 182
|
170 180 190
....*....|....*....|....*....|..
gi 446863618 175 WLDLRYQVEILELLHDLTRHHGRTVVVVLHDL 206
Cdd:cd03267 183 GLDVVAQENIRNFLKEYNRERGTTVLLTSHYM 214
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
22-225 |
9.03e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 94.34 E-value: 9.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 22 KIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKA--LSRRLGILPQSP---LLPE 96
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLsdIRKKVGLVFQYPeyqLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 97 glTVYELVSRGrfPwQNfiRQWSDAD-EQAVEEALKLTGtqefahLPVEK--------LSGGQRQRCWIAMVLAQKTPYI 167
Cdd:PRK13637 100 --TIEKDIAFG--P-IN--LGLSEEEiENRVKRAMNIVG------LDYEDykdkspfeLSGGQKRRVAIAGVVAMEPKIL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446863618 168 LLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:PRK13637 167 ILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
10-233 |
9.11e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 97.20 E-value: 9.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHKK--IIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLGI 87
Cdd:PRK11160 339 LTLNNVSFTYPDQpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 88 LPQSpllpegltVYELVSRGRfpwQNFIRQWSDADEQAVEEALKLTGTQefAHLPVEK------------LSGGQRQRCW 155
Cdd:PRK11160 419 VSQR--------VHLFSATLR---DNLLLAAPNASDEALIEVLQQVGLE--KLLEDDKglnawlgeggrqLSGGEQRRLG 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446863618 156 IAMVLAQKTPYILLDEPTTWLDLRYQVEILELLHDLTRHhgRTVVVVLHDLNfAVNYGDTLIFLRQGKVVrvlNEGEH 233
Cdd:PRK11160 486 IARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQN--KTVLMITHRLT-GLEQFDRICVMDNGQII---EQGTH 557
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
10-224 |
1.24e-22 |
|
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: 92.62 E-value: 1.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHKKIIVdgVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKaihEQPTKALSRR-LGIL 88
Cdd:TIGR01277 1 LALDKVRYEYEHLPME--FDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQ---SHTGLAPYQRpVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 89 PQSPLLPEGLTVYELVSRGRFPWQNFirqwSDADEQAVEEALKLTGTQEF-AHLPvEKLSGGQRQRCWIAMVLAQKTPYI 167
Cdd:TIGR01277 76 FQENNLFAHLTVRQNIGLGLHPGLKL----NAEQQEKVVDAAQQVGIADYlDRLP-EQLSGGQRQRVALARCLVRPNPIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446863618 168 LLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKV 224
Cdd:TIGR01277 151 LLDEPFSALDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
8-239 |
1.25e-22 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 97.10 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 8 QGLI-LDNVSAGY---HKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSR 83
Cdd:TIGR00958 476 EGLIeFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHR 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 84 RLGILPQSPLLPEGlTVYELVSRGrfpwqnfirqWSDADEQAVEEALKLTGTQEF-AHLPV-------EK---LSGGQRQ 152
Cdd:TIGR00958 556 QVALVGQEPVLFSG-SVRENIAYG----------LTDTPDEEIMAAAKAANAHDFiMEFPNgydtevgEKgsqLSGGQKQ 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 153 RCWIAMVLAQKTPYILLDEPTTWLDlryqVEILELLHDLTRHHGRTVVVVLHDLNFAVNyGDTLIFLRQGKVVRV----- 227
Cdd:TIGR00958 625 RIAIARALVRKPRVLILDEATSALD----AECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMgthkq 699
|
250
....*....|..
gi 446863618 228 LNEGEHCTPELV 239
Cdd:TIGR00958 700 LMEDQGCYKHLV 711
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
23-209 |
1.46e-22 |
|
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: 92.41 E-value: 1.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 23 IIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALS----RRLGILPQ-SPLLPEg 97
Cdd:TIGR02211 19 RVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAklrnKKLGFIYQfHHLLPD- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 98 LTVYELVSrgrFPWqnFIRQWS--DADEQAVEEALKLTGTQEFAHLPVEkLSGGQRQRCWIAMVLAQKTPYILLDEPTTW 175
Cdd:TIGR02211 98 FTALENVA---MPL--LIGKKSvkEAKERAYEMLEKVGLEHRINHRPSE-LSGGERQRVAIARALVNQPSLVLADEPTGN 171
|
170 180 190
....*....|....*....|....*....|....
gi 446863618 176 LDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFA 209
Cdd:TIGR02211 172 LDNNNAKIIFDLMLELNRELNTSFLVVTHDLELA 205
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-224 |
1.70e-22 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 95.01 E-value: 1.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 1 MAHNAKGQGLI-LDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPtk 79
Cdd:PRK09452 5 NKQPSSLSPLVeLRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 80 ALSRRLGILPQSPLLPEGLTVYELVSRGrfpwqnfIR-QWSDADEQA--VEEALKLTGTQEFAHLPVEKLSGGQRQRCWI 156
Cdd:PRK09452 83 AENRHVNTVFQSYALFPHMTVFENVAFG-------LRmQKTPAAEITprVMEALRMVQLEEFAQRKPHQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 157 AMVLAQKTPYILLDEPTTWLD--LRYQVEiLELLHdLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKV 224
Cdd:PRK09452 156 ARAVVNKPKVLLLDESLSALDykLRKQMQ-NELKA-LQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRI 223
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-225 |
1.76e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 96.45 E-value: 1.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 22 KIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILqPMGGSILLDGKAIHEQPTKALSRRLGILPQSPLLPEGlTVY 101
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHG-TLR 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 102 ELVSRGRfpwqnfirqwSDADEQAVEEALKLTGTQEF-AHLPV----------EKLSGGQRQRCWIAMVLAQKTPYILLD 170
Cdd:PRK11174 441 DNVLLGN----------PDASDEQLQQALENAWVSEFlPLLPQgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLD 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446863618 171 EPTTWLDLRYQVEILELLHDLTRHHgrTVVVVLHDLNFAVNYgDTLIFLRQGKVV 225
Cdd:PRK11174 511 EPTASLDAHSEQLVMQALNAASRRQ--TTLMVTHQLEDLAQW-DQIWVMQDGQIV 562
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
10-226 |
2.26e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 93.23 E-value: 2.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHKKIIVD---GVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLG 86
Cdd:PRK13642 5 LEVENLVFKYEKESDVNqlnGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 87 ILPQSPLLP-EGLTVYELVSRGR----FPWQNFIRQwsdadeqaVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLA 161
Cdd:PRK13642 85 MVFQNPDNQfVGATVEDDVAFGMenqgIPREEMIKR--------VDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446863618 162 QKTPYILLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNyGDTLIFLRQGKVVR 226
Cdd:PRK13642 157 LRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIK 220
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
19-224 |
2.26e-22 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 92.72 E-value: 2.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 19 YHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIH-------------EQPTKALSRRL 85
Cdd:PRK10619 15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadKNQLRLLRTRL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 86 GILPQSPLLPEGLTVYELVSRGrfPWQNFIRQWSDADEQAVEEALKLtGTQEFAH--LPVEkLSGGQRQRCWIAMVLAQK 163
Cdd:PRK10619 95 TMVFQHFNLWSHMTVLENVMEA--PIQVLGLSKQEARERAVKYLAKV-GIDERAQgkYPVH-LSGGQQQRVSIARALAME 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446863618 164 TPYILLDEPTTWLDLRYQVEILELLHDLTrHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKV 224
Cdd:PRK10619 171 PEVLLFDEPTSALDPELVGEVLRIMQQLA-EEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
10-226 |
2.59e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 94.40 E-value: 2.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKalSRRLGILP 89
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 90 QSPLLPEGLTVYELVSRGrfpwQNFIRQWSDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILL 169
Cdd:PRK11432 85 QSYALFPHMSLGENVGYG----LKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446863618 170 DEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLN--FAVNygDTLIFLRQGKVVR 226
Cdd:PRK11432 161 DEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSeaFAVS--DTVIVMNKGKIMQ 217
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-227 |
2.90e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 92.60 E-value: 2.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 14 NVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQ-----PMGGSILLDGKAIHEQPTKALS--RRLG 86
Cdd:PRK14267 9 NLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDPIEvrREVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 87 ILPQSPLLPEGLTVYELVSRGrFPWQNFIRQWSDADEQaVEEALKLTGTQE-----FAHLPvEKLSGGQRQRCWIAMVLA 161
Cdd:PRK14267 89 MVFQYPNPFPHLTIYDNVAIG-VKLNGLVKSKKELDER-VEWALKKAALWDevkdrLNDYP-SNLSGGQRQRLVIARALA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446863618 162 QKTPYILLDEPTTWLDLRYQVEILELLHDLTRHHgrTVVVVLHDLNFAVNYGDTLIFLRQGKVVRV 227
Cdd:PRK14267 166 MKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEV 229
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
12-225 |
3.35e-22 |
|
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: 91.32 E-value: 3.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 12 LDNVSAGY--HKKIIVDGVSFSV-PTEKMTVlVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLGIL 88
Cdd:cd03369 9 VENLSVRYapDLPPVLKNVSFKVkAGEKIGI-VGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTII 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 89 PQSPLLPEGLTVYELVSRGRFpwqnfirqwsdADEQaVEEALKLTGTQefahlpvEKLSGGQRQRCWIAMVLAQKTPYIL 168
Cdd:cd03369 88 PQDPTLFSGTIRSNLDPFDEY-----------SDEE-IYGALRVSEGG-------LNLSQGQRQLLCLARALLKRPRVLV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446863618 169 LDEPTTWLDLRYQVEILELLHDLTRhhGRTVVVVLHDLNFAVNYgDTLIFLRQGKVV 225
Cdd:cd03369 149 LDEATASIDYATDALIQKTIREEFT--NSTILTIAHRLRTIIDY-DKILVMDAGEVK 202
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
28-209 |
3.36e-22 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 91.80 E-value: 3.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 28 VSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALS----RRLGILPQ-SPLLPEgLTVYE 102
Cdd:PRK11629 28 VSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAelrnQKLGFIYQfHHLLPD-FTALE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 103 LVSrgrFPWQNFIRQWSDADEQAVEeALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDLRYQV 182
Cdd:PRK11629 107 NVA---MPLLIGKKKPAEINSRALE-MLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNAD 182
|
170 180
....*....|....*....|....*..
gi 446863618 183 EILELLHDLTRHHGRTVVVVLHDLNFA 209
Cdd:PRK11629 183 SIFQLLGELNRLQGTAFLVVTHDLQLA 209
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
10-225 |
4.09e-22 |
|
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: 90.80 E-value: 4.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIheqpTKALSRRLGILP 89
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL----DIAARNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 90 QSPLLPEGLTVYE-LVSRGRFPWQNFirqwSDADEQaVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYIL 168
Cdd:cd03269 77 EERGLYPKMKVIDqLVYLAQLKGLKK----EEARRR-IDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446863618 169 LDEPTTWLDLRYQVEILELLHDLTRhHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRELAR-AGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
26-258 |
4.74e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 94.71 E-value: 4.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 26 DGVSFSVptEKMTV--LVGANGCGKSTLLSTIARILQPMGGSILLDGKAIH-EQPTKALSRRLGILPQSPLLPEGLTVYE 102
Cdd:COG3845 22 DDVSLTV--RPGEIhaLLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRiRSPRDAIALGIGMVHQHFMLVPNLTVAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 103 LVSRGRFPWQNFIRQWSDAdEQAVEEALKLTGtqeFA---HLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDLR 179
Cdd:COG3845 100 NIVLGLEPTKGGRLDRKAA-RARIRELSERYG---LDvdpDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 180 yQVEIL-ELLHDLTRhHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVVRVLNEGEHCTPELVKAVFDVDVHASINPLTGKP 258
Cdd:COG3845 176 -EADELfEILRRLAA-EGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELAELMVGREVLLRVEKAPAEP 253
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
24-233 |
5.15e-22 |
|
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: 91.39 E-value: 5.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 24 IVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLGILPQSPLLPEGlTVYEL 103
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQENVLFNR-SIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 104 VSRGRfpwqnfirqwSDADEQAVEEALKLTGTQEF-AHLPV-------EK---LSGGQRQRCWIAMVLAQKTPYILLDEP 172
Cdd:cd03252 96 IALAD----------PGMSMERVIEAAKLAGAHDFiSELPEgydtivgEQgagLSGGQRQRIAIARALIHNPRILIFDEA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446863618 173 TTWLDLRYQVEILELLHDLTRhhGRTVVVVLHDLNfAVNYGDTLIFLRQGKVVRvlnEGEH 233
Cdd:cd03252 166 TSALDYESEHAIMRNMHDICA--GRTVIIIAHRLS-TVKNADRIIVMEKGRIVE---QGSH 220
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
9-226 |
8.49e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 91.73 E-value: 8.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 9 GLILDNVSAGYHKKIIVDG-----VSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPT----K 79
Cdd:PRK13649 2 GINLQNVSYTYQAGTPFEGralfdVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdiK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 80 ALSRRLGIL---PQSPLLPEglTVYELVSrgrFPWQNFIRQWSDAdEQAVEEALKLTGTQE--FAHLPVEkLSGGQRQRC 154
Cdd:PRK13649 82 QIRKKVGLVfqfPESQLFEE--TVLKDVA---FGPQNFGVSQEEA-EALAREKLALVGISEslFEKNPFE-LSGGQMRRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446863618 155 WIAMVLAQKTPYILLDEPTTWLDLRYQVEILELLHDLtRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVVR 226
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKL-HQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVL 225
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
10-172 |
1.21e-21 |
|
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: 90.29 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRR-LGIL 88
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 89 PQSPLLPEGLTVYE---LVSRgrfpwqnfIRQWSDAD-EQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKT 164
Cdd:cd03218 81 PQEASIFRKLTVEEnilAVLE--------IRGLSKKErEEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNP 152
|
....*...
gi 446863618 165 PYILLDEP 172
Cdd:cd03218 153 KFLLLDEP 160
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
28-224 |
1.53e-21 |
|
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: 92.10 E-value: 1.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 28 VSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDG-------KAIHEQPTKalsRRLGILPQSPLLPEGLTV 100
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfdsrKGIFLPPEK---RRIGYVFQEARLFPHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 101 YELVSRGRfpwqnfirQWSDADEQAV--EEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDL 178
Cdd:TIGR02142 93 RGNLRYGM--------KRARPSERRIsfERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446863618 179 RYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKV 224
Cdd:TIGR02142 165 PRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRV 210
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
28-226 |
1.55e-21 |
|
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: 92.09 E-value: 1.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 28 VSFSVPTEKMTVLVGANGCGKSTLLSTIARILQP------MGGSILLDGKAIHEQPTKAlsRRLGILPQSPLLPEGLTVy 101
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPdsgrirLGGEVLQDSARGIFLPPHR--RRIGYVFQEARLFPHLSV- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 102 elvsRG--RFPWQnfiRQWSDADEQAVEEALKLTGtqeFAHL---PVEKLSGGQRQRCWIAMVLAQKtPYILL-DEPTTW 175
Cdd:COG4148 95 ----RGnlLYGRK---RAPRAERRISFDEVVELLG---IGHLldrRPATLSGGERQRVAIGRALLSS-PRLLLmDEPLAA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446863618 176 LDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVVR 226
Cdd:COG4148 164 LDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVA 214
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
28-225 |
1.68e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 90.95 E-value: 1.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 28 VSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAI----HEQPTKALSRRLGIL---PQSPLLPEglTV 100
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVsstsKQKEIKPVRKKVGVVfqfPESQLFEE--TV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 101 YELVSRGRfpwQNFIRQWSDADEQAVEEaLKLTG-TQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDLR 179
Cdd:PRK13643 103 LKDVAFGP---QNFGIPKEKAEKIAAEK-LEMVGlADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPK 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446863618 180 YQVEILELLHDLtRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:PRK13643 179 ARIEMMQLFESI-HQSGQTVVLVTHLMDDVADYADYVYLLEKGHII 223
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
10-207 |
1.80e-21 |
|
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: 89.09 E-value: 1.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQpTKALSRRLGILP 89
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQ-RDSIARGLLYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 90 QSPLLPEGLTVYElvsrgrfpwqNfIRQW-SDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYIL 168
Cdd:cd03231 80 HAPGIKTTLSVLE----------N-LRFWhADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWI 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 446863618 169 LDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLN 207
Cdd:cd03231 149 LDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLG 187
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
10-226 |
2.53e-21 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 92.80 E-value: 2.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGY--HKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLGI 87
Cdd:TIGR01842 317 LSVENVTIVPpgGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGY 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 88 LPQSPLLPEGlTVYelvsrgrfpwQNFIRQWSDADEQAVEEALKLTGTQEF-AHLPV----------EKLSGGQRQRCWI 156
Cdd:TIGR01842 397 LPQDVELFPG-TVA----------ENIARFGENADPEKIIEAAKLAGVHELiLRLPDgydtvigpggATLSGGQRQRIAL 465
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 157 AMVLAQKTPYILLDEPTTWLDLRYQVEILELLHDLtRHHGRTVVVVLHDLNfAVNYGDTLIFLRQGKVVR 226
Cdd:TIGR01842 466 ARALYGDPKLVVLDEPNSNLDEEGEQALANAIKAL-KARGITVVVITHRPS-LLGCVDKILVLQDGRIAR 533
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-220 |
5.45e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 89.33 E-value: 5.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 12 LDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMG-----GSILLDGKAIHEQPTKA--LSRR 84
Cdd:PRK14258 10 VNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERRVNLnrLRRQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 85 LGIL-PQSPLLPegLTVYELVSRGR--FPWQNFIrQWSDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLA 161
Cdd:PRK14258 90 VSMVhPKPNLFP--MSVYDNVAYGVkiVGWRPKL-EIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARALA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446863618 162 QKTPYILLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLR 220
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFK 225
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
25-223 |
6.62e-21 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 88.89 E-value: 6.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 25 VDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSrRLGILP--QSPLLPEGLTVYE 102
Cdd:PRK11300 21 VNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA-RMGVVRtfQHVRLFREMTVIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 103 --LVSRGRFPWQNFIR------QWSDADEQAVEEA---LKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDE 171
Cdd:PRK11300 100 nlLVAQHQQLKTGLFSgllktpAFRRAESEALDRAatwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446863618 172 PTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGK 223
Cdd:PRK11300 180 PAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
8-225 |
8.84e-21 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 91.56 E-value: 8.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 8 QGLI-LDNVSAGY-HKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRL 85
Cdd:PRK13657 332 KGAVeFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 86 GILPQSPLLPEgLTVYELVSRGRfpwqnfirqwSDADEQAVEEALKLTGTQEFahlpVEK---------------LSGGQ 150
Cdd:PRK13657 412 AVVFQDAGLFN-RSIEDNIRVGR----------PDATDEEMRAAAERAQAHDF----IERkpdgydtvvgergrqLSGGE 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446863618 151 RQRCWIAMVLAQKTPYILLDEPTTWLDLRYQVEILELLHDLTrhHGRTVVVVLHDLNfAVNYGDTLIFLRQGKVV 225
Cdd:PRK13657 477 RQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELM--KGRTTFIIAHRLS-TVRNADRILVFDNGRVV 548
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
12-205 |
1.14e-20 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 89.37 E-value: 1.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 12 LDNVSAGYHKK----IIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALS---RR 84
Cdd:COG1135 4 LENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRaarRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 85 LGILPQSP-LLPEgLTVYELVSrgrFPWQnfIRQWSDADEQA-VEEALKLTGTQEFAH-LPVEkLSGGQRQRCWIAMVLA 161
Cdd:COG1135 84 IGMIFQHFnLLSS-RTVAENVA---LPLE--IAGVPKAEIRKrVAELLELVGLSDKADaYPSQ-LSGGQKQRVGIARALA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446863618 162 QKtPYILL-DEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHD 205
Cdd:COG1135 157 NN-PKVLLcDEATSALDPETTRSILDLLKDINRELGLTIVLITHE 200
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
13-218 |
1.65e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 87.92 E-value: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 13 DNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARI--LQP---MGGSILLDGKAIHEQPTK--ALSRRL 85
Cdd:PRK14243 14 ENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPgfrVEGKVTFHGKNLYAPDVDpvEVRRRI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 86 GILPQSPLlPEGLTVY-----------------ELVSRGrfpwqnfIRQWSDADEqaVEEALKLTGTQefahlpvekLSG 148
Cdd:PRK14243 94 GMVFQKPN-PFPKSIYdniaygaringykgdmdELVERS-------LRQAALWDE--VKDKLKQSGLS---------LSG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 149 GQRQRCWIAMVLAQKTPYILLDEPTTWLDLRYQVEILELLHDLTRHHgrTVVVVLHDLNFAVNYGDTLIF 218
Cdd:PRK14243 155 GQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTAF 222
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
10-225 |
2.30e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 88.14 E-value: 2.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHKKI-----IVDGVSFSVPTEKMTVLVGANGCGKSTLLS-TIARILQPMGGSILLDG------KAIHEqp 77
Cdd:PRK13645 7 IILDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQlTNGLIISETGQTIVGDYaipanlKKIKE-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 78 TKALSRRLGILPQSP---LLPEglTVYELVSRGRfpwqnfIRQWSDADE--QAVEEALKLTG-TQEFAHLPVEKLSGGQR 151
Cdd:PRK13645 85 VKRLRKEIGLVFQFPeyqLFQE--TIEKDIAFGP------VNLGENKQEayKKVPELLKLVQlPEDYVKRSPFELSGGQK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446863618 152 QRCWIAMVLAQKTPYILLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:PRK13645 157 RRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVI 230
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
25-225 |
3.29e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 87.17 E-value: 3.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 25 VDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLGILPQSP----LLPeglTV 100
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddqiFSP---TV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 101 YELVSRGrfPWQNFIRQwsDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDLRY 180
Cdd:PRK13652 97 EQDIAFG--PINLGLDE--ETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446863618 181 QVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:PRK13652 173 VKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIV 217
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
3-225 |
4.20e-20 |
|
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: 89.62 E-value: 4.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 3 HNAKGQGLI-LDNVSAGYH--KKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTK 79
Cdd:TIGR03796 470 PPRRLSGYVeLRNITFGYSplEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPRE 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 80 ALSRRLGILPQSPLLPEGlTVYELVS--RGRFPWQNFIRQWSDAdeqAVEEA-LKLTGTQEFahlPVEK----LSGGQRQ 152
Cdd:TIGR03796 550 VLANSVAMVDQDIFLFEG-TVRDNLTlwDPTIPDADLVRACKDA---AIHDViTSRPGGYDA---ELAEgganLSGGQRQ 622
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446863618 153 RCWIAMVLAQKtPYIL-LDEPTTWLDLRYQVEILELLhdltRHHGRTVVVVLHDLNfAVNYGDTLIFLRQGKVV 225
Cdd:TIGR03796 623 RLEIARALVRN-PSILiLDEATSALDPETEKIIDDNL----RRRGCTCIIVAHRLS-TIRDCDEIIVLERGKVV 690
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
25-227 |
5.44e-20 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 88.55 E-value: 5.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 25 VDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALS----RRLGILPQSPLLPEGLTV 100
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 101 YELVSRGrfpwQNFIRQWSDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDLRY 180
Cdd:PRK10070 124 LDNTAFG----MELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446863618 181 QVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVVRV 227
Cdd:PRK10070 200 RTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQV 246
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
25-243 |
5.63e-20 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 89.30 E-value: 5.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 25 VDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIhEQPTKALSRRLGILPQSPLLPEGLTVYELV 104
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHLTVAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 105 srgRFPWQNFIRQWSDAdEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDLRYQVEI 184
Cdd:TIGR01257 1025 ---LFYAQLKGRSWEEA-QLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSI 1100
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446863618 185 LELLhdLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVvrvlnegeHC--TPELVKAVF 243
Cdd:TIGR01257 1101 WDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL--------YCsgTPLFLKNCF 1151
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
13-236 |
6.17e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 86.76 E-value: 6.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 13 DNVSAGYHK-----KIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIH----EQPTKALSR 83
Cdd:PRK13646 6 DNVSYTYQKgtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkDKYIRPVRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 84 RLGILPQsplLPEGLTVYELVSRG-RFPWQNFIRQWSDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQ 162
Cdd:PRK13646 86 RIGMVFQ---FPESQLFEDTVEREiIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAM 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446863618 163 KTPYILLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVVrvlnegEHCTP 236
Cdd:PRK13646 163 NPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIV------SQTSP 230
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
10-225 |
6.43e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 86.70 E-value: 6.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIheqpTKALSRRLGILP 89
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL----DPEDRRRIGYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 90 QSPLLPEGLTVYE-LVSRGRfpwqnfIRQWSDAD-EQAVEEALKLTGTQEFAHLPVEKLSGGQRQRC-WIAMVLAQktPY 166
Cdd:COG4152 78 EERGLYPKMKVGEqLVYLAR------LKGLSKAEaKRRADEWLERLGLGDRANKKVEELSKGNQQKVqLIAALLHD--PE 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 167 IL-LDEPTTWLDLRYQVEILELLHDLTRhHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:COG4152 150 LLiLDEPFSGLDPVNVELLKDVIRELAA-KGTTVIFSSHQMELVEELCDRIVIINKGRKV 208
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
22-225 |
1.45e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 87.84 E-value: 1.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 22 KIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGgSILLDGKAIHEQPTKAL---SRRLGIL---PQSPLLP 95
Cdd:PRK15134 299 NVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQG-EIWFDGQPLHNLNRRQLlpvRHRIQVVfqdPNSSLNP 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 96 EgLTVYELVSRGRFPWQNFIRqwSDADEQAVEEALKLTGTQ-EFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTT 174
Cdd:PRK15134 378 R-LNVLQIIEEGLRVHQPTLS--AAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446863618 175 WLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:PRK15134 455 SLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVV 505
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
7-204 |
1.45e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 87.94 E-value: 1.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 7 GQGLILDNVS-AGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIA--------RILQPMGGSILLdgkaiheqp 77
Cdd:COG4178 360 DGALALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAglwpygsgRIARPAGARVLF--------- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 78 tkalsrrlgiLPQSPLLPEGlTVYELVSrgrFPwqNFIRQWSDAdeqAVEEALKLTGTQEFA-HLPVEK-----LSGGQR 151
Cdd:COG4178 431 ----------LPQRPYLPLG-TLREALL---YP--ATAEAFSDA---ELREALEAVGLGHLAeRLDEEAdwdqvLSLGEQ 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446863618 152 QRCWIAMVLAQKTPYILLDEPTTWLDLRYQVEILELLHDltRHHGRTVVVVLH 204
Cdd:COG4178 492 QRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE--ELPGTTVISVGH 542
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
10-225 |
1.57e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 84.75 E-value: 1.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAiheqptkalsrrlgilp 89
Cdd:COG1134 27 LLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRV----------------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 90 qSPLL-------PEgLTVYELV-SRGRFpwQNFIRQwsDADEQaVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLA 161
Cdd:COG1134 90 -SALLelgagfhPE-LTGRENIyLNGRL--LGLSRK--EIDEK-FDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446863618 162 QKTPYILLDEpttWL---DLRYQVEILELLHDLtRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:COG1134 163 VDPDILLVDE---VLavgDAAFQKKCLARIREL-RESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLV 225
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
9-233 |
1.71e-19 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 87.88 E-value: 1.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 9 GLILDNVSAGYHKK--IIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLG 86
Cdd:TIGR01846 455 AITFENIRFRYAPDspEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMG 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 87 ILPQSPLLPEGlTVYELVSRGRfpwqnfirqwSDADEQAVEEALKLTGTQEF-AHLP-------VEK---LSGGQRQRCW 155
Cdd:TIGR01846 535 VVLQENVLFSR-SIRDNIALCN----------PGAPFEHVIHAAKLAGAHDFiSELPqgyntevGEKganLSGGQRQRIA 603
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446863618 156 IAMVLAQKTPYILLDEPTTWLDLRYQVEILELLHDLTRhhGRTVVVVLHDLNfAVNYGDTLIFLRQGKVVRvlnEGEH 233
Cdd:TIGR01846 604 IARALVGNPRILIFDEATSALDYESEALIMRNMREICR--GRTVIIIAHRLS-TVRACDRIIVLEKGQIAE---SGRH 675
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
9-172 |
2.27e-19 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 84.31 E-value: 2.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 9 GLILDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPtkaLSRR--LG 86
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLP---MHKRarLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 87 I--LPQSPLLPEGLTVyelvsrgrfpWQNF-----IRQWSDAD-EQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAM 158
Cdd:COG1137 80 IgyLPQEASIFRKLTV----------EDNIlavleLRKLSKKErEERLEELLEEFGITHLRKSKAYSLSGGERRRVEIAR 149
|
170
....*....|....
gi 446863618 159 VLAQKTPYILLDEP 172
Cdd:COG1137 150 ALATNPKFILLDEP 163
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
12-225 |
3.04e-19 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 84.03 E-value: 3.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 12 LDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSI-----LLDG-KAIHEQPT--KALSR 83
Cdd:PRK11264 6 VKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTaRSLSQQKGliRQLRQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 84 RLGILPQSPLLPEGLTVYELVSRGRFPWQNFIRQWSDADEQAVEEALKLTGtQEFAHlPvEKLSGGQRQRCWIAMVLAQK 163
Cdd:PRK11264 86 HVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAG-KETSY-P-RRLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446863618 164 TPYILLDEPTTWLDLRYQVEILELLHDLTRHHgRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIV 223
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
40-224 |
3.52e-19 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 84.08 E-value: 3.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 40 LVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSR-------------RLGILPQSPLLPEGLTVYELVSR 106
Cdd:COG4598 39 IIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDGELvpadrrqlqrirtRLGMVFQSFNLWSHMTVLENVIE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 107 GrfPWQNFIRQWSDADEQAvEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDLRYQVEILE 186
Cdd:COG4598 119 A--PVHVLGRPKAEAIERA-EALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLK 195
|
170 180 190
....*....|....*....|....*....|....*...
gi 446863618 187 LLHDLTRhHGRTVVVVLHDLNFAVNYGDTLIFLRQGKV 224
Cdd:COG4598 196 VMRDLAE-EGRTMLVVTHEMGFARDVSSHVVFLHQGRI 232
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
12-225 |
3.57e-19 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 83.91 E-value: 3.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 12 LDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDG------KAIHEQPTKALSRRL 85
Cdd:COG4161 5 LKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRLLRQKV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 86 GILPQSPLLPEGLTVYelvsrgrfpwQNFI----RQWSDADEQAVEEALKLTGT---QEFAHLPVEKLSGGQRQRCWIAM 158
Cdd:COG4161 85 GMVFQQYNLWPHLTVM----------ENLIeapcKVLGLSKEQAREKAMKLLARlrlTDKADRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446863618 159 VLAQKTPYILLDEPTTWLDLRYQVEILELLHDLTrHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:COG4161 155 ALMMEPQVLLFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRII 220
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-225 |
4.61e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 83.94 E-value: 4.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 22 KIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQ------PMGGSILLDGKAIHEQPTKALSRRLGILPQSPLLP 95
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 96 EGLTVYELVSrgrFPWQNFIRQWSDADEQAVEEALKLTGTQEFAH----LPVEKLSGGQRQRCWIAMVLAQKTPYILLDE 171
Cdd:PRK14246 103 PHLSIYDNIA---YPLKSHGIKEKREIKKIVEECLRKVGLWKEVYdrlnSPASQLSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446863618 172 PTTWLDLRYQVEILELLHDLTRHhgRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELV 231
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
10-242 |
4.92e-19 |
|
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: 83.73 E-value: 4.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALS----RRL 85
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLSeaerRRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 86 -----GILPQSPLLPEGLTVYELVSRGRFPWQNFIRQWSDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVL 160
Cdd:TIGR02323 84 mrtewGFVHQNPRDGLRMRVSAGANIGERLMAIGARHYGNIRATAQDWLEEVEIDPTRIDDLPRAFSGGMQQRLQIARNL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 161 AQKTPYILLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV------RVLNEGEH- 233
Cdd:TIGR02323 164 VTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVesgltdQVLDDPQHp 243
|
....*....
gi 446863618 234 CTPELVKAV 242
Cdd:TIGR02323 244 YTQLLVSSI 252
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
12-223 |
7.50e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 84.50 E-value: 7.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 12 LDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQpTKALSRRLGILPQS 91
Cdd:PRK13536 44 LAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPAR-ARLARARIGVVPQF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 92 PLLPEGLTVYE-LVSRGRfpwqnFIRQWSDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLD 170
Cdd:PRK13536 123 DNLDLEFTVREnLLVFGR-----YFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILD 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446863618 171 EPTTWLDLRYQVEILELLHDLTRhHGRTVVVVLHDLNFAVNYGDTLIFLRQGK 223
Cdd:PRK13536 198 EPTTGLDPHARHLIWERLRSLLA-RGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
15-209 |
8.95e-19 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 82.52 E-value: 8.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 15 VSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIH----EQPTKALSRRLGILPQ 90
Cdd:PRK10584 16 VGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHqmdeEARAKLRAKHVGFVFQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 91 SPLLPEGLTVYELVsrgRFPwqNFIRQWSDAD--EQAVEEALKLTGTQEFAHLPVEkLSGGQRQRCWIAMVLAQKTPYIL 168
Cdd:PRK10584 96 SFMLIPTLNALENV---ELP--ALLRGESSRQsrNGAKALLEQLGLGKRLDHLPAQ-LSGGEQQRVALARAFNGRPDVLF 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446863618 169 LDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFA 209
Cdd:PRK10584 170 ADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLA 210
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
12-247 |
9.46e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 83.70 E-value: 9.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 12 LDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKAlSRRLGILPQS 91
Cdd:PRK13537 10 FRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGVVPQF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 92 PLLPEGLTVYE-LVSRGRfpwqnFIRQWSDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLD 170
Cdd:PRK13537 89 DNLDPDFTVREnLLVFGR-----YFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446863618 171 EPTTWLDLRYQVEILELLHDLTRhHGRTVVVVLHDLNFAVNYGDTLIFLRQGkvvRVLNEGEhcTPELVKAVFDVDV 247
Cdd:PRK13537 164 EPTTGLDPQARHLMWERLRSLLA-RGKTILLTTHFMEEAERLCDRLCVIEEG---RKIAEGA--PHALIESEIGCDV 234
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
10-225 |
9.81e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 82.62 E-value: 9.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRR-LGIL 88
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREaVAIV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 89 PQSPLLPEGLTVYELVSRGRF-----PWQNFIRQWSDADEQAVEEALKLTGTqefahlpvekLSGGQRQRCWIAMVLAQK 163
Cdd:PRK11614 86 PEGRRVFSRMTVEENLAMGGFfaerdQFQERIKWVYELFPRLHERRIQRAGT----------MSGGEQQMLAIGRALMSQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446863618 164 TPYILLDEPTTWLDLRYQVEILELLHDLtRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:PRK11614 156 PRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-207 |
1.40e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 83.60 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 19 YHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQpTKALSRRLGI----------- 87
Cdd:COG4586 32 YREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKR-RKEFARRIGVvfgqrsqlwwd 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 88 LPqsplLPEGLT----VYElVSRGRFpwqnfirqwsdadEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQK 163
Cdd:COG4586 111 LP----AIDSFRllkaIYR-IPDAEY-------------KKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHR 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446863618 164 TPYILLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLN 207
Cdd:COG4586 173 PKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMD 216
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
12-204 |
1.75e-18 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 83.31 E-value: 1.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 12 LDNVS---AGYHKKII-VDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALS---RR 84
Cdd:PRK11153 4 LKNISkvfPQGGRTIHaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRkarRQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 85 LGILPQSPLLPEGLTVYELVSrgrFPWQnfIRQWSDAD-EQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQK 163
Cdd:PRK11153 84 IGMIFQHFNLLSSRTVFDNVA---LPLE--LAGTPKAEiKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASN 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446863618 164 tPYILL-DEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLH 204
Cdd:PRK11153 159 -PKVLLcDEATSALDPATTRSILELLKDINRELGLTIVLITH 199
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
10-223 |
2.10e-18 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 79.41 E-value: 2.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHKKIIVDGVSFSVPT-EKMtVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAiheqptkalsrRLGIL 88
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPgDRI-GLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV-----------KIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 89 PQspllpegltvyelvsrgrfpwqnfirqwsdadeqaveealkltgtqefahlpvekLSGGQRQRCWIAMVLAQKTPYIL 168
Cdd:cd03221 69 EQ-------------------------------------------------------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446863618 169 LDEPTTWLDLryqvEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGK 223
Cdd:cd03221 94 LDEPTNHLDL----ESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
10-206 |
2.16e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 81.55 E-value: 2.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHKKIIvdgvSFSV---PTEKMTVLvGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTkalSRR-L 85
Cdd:PRK10771 2 LKLTDITWLYHHLPM----RFDLtveRGERVAIL-GPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPP---SRRpV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 86 GILPQSPLLPEGLTVYELVSRGRFPWQNFirqwSDADEQAVEEALKLTGTQEF-AHLPVEkLSGGQRQRCWIAMVLAQKT 164
Cdd:PRK10771 74 SMLFQENNLFSHLTVAQNIGLGLNPGLKL----NAAQREKLHAIARQMGIEDLlARLPGQ-LSGGQRQRVALARCLVREQ 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446863618 165 PYILLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDL 206
Cdd:PRK10771 149 PILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSL 190
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
21-225 |
3.20e-18 |
|
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: 79.98 E-value: 3.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 21 KKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIA--RILQPMGGSILLDGKAIheqpTKALSRRLGILPQSPLLPEGL 98
Cdd:cd03232 19 KRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAgrKTAGVITGEILINGRPL----DKNFQRSTGYVEQQDVHSPNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 99 TVYElvsrgrfpwqnfirqwsdadeqAVEEALKLTGtqefahlpvekLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDL 178
Cdd:cd03232 95 TVRE----------------------ALRFSALLRG-----------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446863618 179 RYQVEILELLHDLTRhHGRTVVVVLHDLNFAV-NYGDTLIFL-RQGKVV 225
Cdd:cd03232 142 QAAYNIVRFLKKLAD-SGQAILCTIHQPSASIfEKFDRLLLLkRGGKTV 189
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
10-226 |
3.26e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 83.81 E-value: 3.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTK-ALSRRLGIL 88
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALAAGVAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 89 PQS-PLLPEgLTVYELVSRGRFPWQ-NFIRQwSDADEQAVEEaLKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPY 166
Cdd:PRK11288 85 YQElHLVPE-MTVAENLYLGQLPHKgGIVNR-RLLNYEAREQ-LEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446863618 167 ILLDEPTTWLDLRyQVEIL-ELLHDLtRHHGRTVVVVLHDLN--FAVNygDTLIFLRQGKVVR 226
Cdd:PRK11288 162 IAFDEPTSSLSAR-EIEQLfRVIREL-RAEGRVILYVSHRMEeiFALC--DAITVFKDGRYVA 220
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
10-241 |
3.53e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 81.09 E-value: 3.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRR-LGIL 88
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 89 PQSPLLPEGLTVYElvsrgrfpwqNF-----IRQwSDADEQAVEEALKLTGTQEFAHLPV---EKLSGGQRQRCWIAMVL 160
Cdd:PRK10895 84 PQEASIFRRLSVYD----------NLmavlqIRD-DLSAEQREDRANELMEEFHIEHLRDsmgQSLSGGERRRVEIARAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 161 AQKTPYILLDEPTTWLDLRYQVEILELLHDLtRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVVrvlnegEHCTPELVK 240
Cdd:PRK10895 153 AANPKFILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLI------AHGTPTEIL 225
|
.
gi 446863618 241 A 241
Cdd:PRK10895 226 Q 226
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
9-227 |
1.07e-17 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 81.61 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 9 GLILDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKalSRRLGIL 88
Cdd:PRK11000 3 SVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA--ERGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 89 PQSPLLPEGLTVYELVSrgrfpwqnFIRQWSDAD----EQAVEEALKLTgtqEFAHLPVEK---LSGGQRQRCWIAMVLA 161
Cdd:PRK11000 81 FQSYALYPHLSVAENMS--------FGLKLAGAKkeeiNQRVNQVAEVL---QLAHLLDRKpkaLSGGQRQRVAIGRTLV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446863618 162 QKTPYILLDEPTTWLD--LRYQVEIlellhDLTRHH---GRTVVVVLHDLNFAVNYGDTLIFLRQGKVVRV 227
Cdd:PRK11000 150 AEPSVFLLDEPLSNLDaaLRVQMRI-----EISRLHkrlGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQV 215
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
10-233 |
1.07e-17 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 79.97 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHKKIIVDGVSFSV-PTEKMTVlVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALS----RR 84
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLyPGEVLGI-VGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSeaerRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 85 L-----GILPQSPLlpEGL--------TVYE-LVSRGrfpWQNF--IRQ----WSDADEQAVEEALKLTGTqefahlpve 144
Cdd:PRK11701 86 LlrtewGFVHQHPR--DGLrmqvsaggNIGErLMAVG---ARHYgdIRAtagdWLERVEIDAARIDDLPTT--------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 145 kLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKV 224
Cdd:PRK11701 152 -FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRV 230
|
250
....*....|....*
gi 446863618 225 V------RVLNEGEH 233
Cdd:PRK11701 231 VesgltdQVLDDPQH 245
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
25-225 |
1.62e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 81.75 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 25 VDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAiHEQPTKALSRRLG--ILPQSPLLPEGLTVYE 102
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNIN-YNKLDHKLAAQLGigIIYQELSVIDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 103 LVSRGRFPWQNF----IRQWSDADEQAvEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDl 178
Cdd:PRK09700 100 NLYIGRHLTKKVcgvnIIDWREMRVRA-AMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLT- 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446863618 179 RYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:PRK09700 178 NKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSV 224
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
22-209 |
1.77e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 78.31 E-value: 1.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 22 KIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLGILPQSPLLPEgLTvy 101
Cdd:PRK13538 14 RILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLGHQPGIKTE-LT-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 102 elvsrgrfPWQN---FIRQWSDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDl 178
Cdd:PRK13538 91 --------ALENlrfYQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID- 161
|
170 180 190
....*....|....*....|....*....|....*
gi 446863618 179 ryqVEILELLHDLTRHH---GRTVVVVLH-DLNFA 209
Cdd:PRK13538 162 ---KQGVARLEALLAQHaeqGGMVILTTHqDLPVA 193
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
21-225 |
2.02e-17 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 78.73 E-value: 2.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 21 KKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKaiheqptkaLSRRLGIlpQSPLLPEgLTV 100
Cdd:cd03220 34 EFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR---------VSSLLGL--GGGFNPE-LTG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 101 YE-LVSRGRfpwqnfIRQWSDADEQAVEEALK-LTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEpttWL-- 176
Cdd:cd03220 102 REnIYLNGR------LLGLSRKEIDEKIDEIIeFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDE---VLav 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446863618 177 -DLRYQVEILELLHDLTRhHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:cd03220 173 gDAAFQEKCQRRLRELLK-QGKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
24-241 |
2.25e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 81.31 E-value: 2.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 24 IVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALS--RR--LGILPQSPLLPEGLT 99
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAqlRRehFGFIFQRYHLLSHLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 100 ---------VYELVSRGRfpwqnfiRQwsdadEQAVEEALKLtGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLD 170
Cdd:PRK10535 103 aaqnvevpaVYAGLERKQ-------RL-----LRAQELLQRL-GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILAD 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446863618 171 EPTTWLDLRYQVEILELLHDLtRHHGRTVVVVLHDLNFAvNYGDTLIFLRQGKVVRvlNEGEHCTPELVKA 241
Cdd:PRK10535 170 EPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVA-AQAERVIEIRDGEIVR--NPPAQEKVNVAGG 236
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
28-225 |
2.53e-17 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 78.90 E-value: 2.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 28 VSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDG------KAIHEQPTKALSRRLGILPQSPLLPEGLTVY 101
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRELRRNVGMVFQQYNLWPHLTVQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 102 elvsrgrfpwQNFI----RQWSDADEQAVEEALKLTGT---QEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTT 174
Cdd:PRK11124 101 ----------QNLIeapcRVLGLSKDQALARAEKLLERlrlKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446863618 175 WLDLRYQVEILELLHDLtRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:PRK11124 171 ALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIV 220
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
27-237 |
2.71e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 81.32 E-value: 2.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 27 GVSFSV-PTEKMTVlVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLGILPQSPLLPEGlTVyelvs 105
Cdd:PLN03130 1257 GLSFEIsPSEKVGI-VGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSG-TV----- 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 106 rgRFPWQNFiRQWSDADeqaVEEALkltgtqEFAHLPV-----------------EKLSGGQRQRCWIAMVLAQKTPYIL 168
Cdd:PLN03130 1330 --RFNLDPF-NEHNDAD---LWESL------ERAHLKDvirrnslgldaevseagENFSVGQRQLLSLARALLRRSKILV 1397
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446863618 169 LDEPTTWLDLRYQVeileLLHDLTRHHGR--TVVVVLHDLNFAVNyGDTLIFLRQGKVVrvlnegEHCTPE 237
Cdd:PLN03130 1398 LDEATAAVDVRTDA----LIQKTIREEFKscTMLIIAHRLNTIID-CDRILVLDAGRVV------EFDTPE 1457
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
12-221 |
3.01e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 78.62 E-value: 3.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 12 LDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAiheqptkalsrRLGILPQS 91
Cdd:PRK09544 7 LENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKL-----------RIGYVPQK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 92 ----PLLPegLTVyelvsrgrfpwQNFIRQWSDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYI 167
Cdd:PRK09544 76 lyldTTLP--LTV-----------NRFLRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446863618 168 LLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQ 221
Cdd:PRK09544 143 VLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
25-227 |
3.37e-17 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 80.62 E-value: 3.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 25 VDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSI----------------LLDGKAiheqptkalSRRLGIL 88
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdewvdmtkpgpDGRGRA---------KRYIGIL 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 89 PQSpllpegltvYELvsrgrFPWQNFIRQWSDA------DEQAVEEA---LKLTG-TQEFAHLPVEK----LSGGQRQRC 154
Cdd:TIGR03269 371 HQE---------YDL-----YPHRTVLDNLTEAiglelpDELARMKAvitLKMVGfDEEKAEEILDKypdeLSEGERHRV 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446863618 155 WIAMVLAQKTPYILLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVVRV 227
Cdd:TIGR03269 437 ALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKI 509
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
16-233 |
4.00e-17 |
|
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: 80.94 E-value: 4.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 16 SAGYHKKIIVDgVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLGILPQSPLLP 95
Cdd:TIGR01193 482 SYGYGSNILSD-ISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIF 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 96 EGlTVYE---LVSRGRFPWQNFIRQWSDADEQAVEEALKLtGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEP 172
Cdd:TIGR01193 561 SG-SILEnllLGAKENVSQDEIWAACEIAEIKDDIENMPL-GYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDES 638
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446863618 173 TTWLDLRYQVEILELLHDLTRhhgRTVVVVLHDLNFAvNYGDTLIFLRQGKVVRvlnEGEH 233
Cdd:TIGR01193 639 TSNLDTITEKKIVNNLLNLQD---KTIIFVAHRLSVA-KQSDKIIVLDHGKIIE---QGSH 692
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
12-225 |
6.98e-17 |
|
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: 80.00 E-value: 6.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 12 LDNVSAGYHKK--IIVDGVSFSVPTEKMTVLVGANGCGKSTLLstiaRIL----QPMGGSILLDGKAIHEQPTKALSRRL 85
Cdd:TIGR03797 454 VDRVTFRYRPDgpLILDDVSLQIEPGEFVAIVGPSGSGKSTLL----RLLlgfeTPESGSVFYDGQDLAGLDVQAVRRQL 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 86 GILPQSPLLPEGlTVYElvsrgrfpwqNFIRQWSDADEQAvEEALKLTGTQE-FAHLP----------VEKLSGGQRQRC 154
Cdd:TIGR03797 530 GVVLQNGRLMSG-SIFE----------NIAGGAPLTLDEA-WEAARMAGLAEdIRAMPmgmhtvisegGGTLSGGQRQRL 597
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446863618 155 WIAMVLAQKTPYILLDEPTTWLDLRYQVEILELLHDL--TRhhgrtvVVVLHDLNFAVNyGDTLIFLRQGKVV 225
Cdd:TIGR03797 598 LIARALVRKPRILLFDEATSALDNRTQAIVSESLERLkvTR------IVIAHRLSTIRN-ADRIYVLDAGRVV 663
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
5-225 |
7.88e-17 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 79.68 E-value: 7.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 5 AKGQgLILDNVSAGYHKK--IIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALS 82
Cdd:PRK11176 338 AKGD-IEFRNVTFTYPGKevPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 83 RRLGILPQSPLLPEGlTVYELVSRGRfpwqnfIRQWSDADeqaVEEALKLTGTQEFahlpVEK---------------LS 147
Cdd:PRK11176 417 NQVALVSQNVHLFND-TIANNIAYAR------TEQYSREQ---IEEAARMAYAMDF----INKmdngldtvigengvlLS 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446863618 148 GGQRQRCWIAMVLAQKTPYILLDEPTTWLDLRYQVEILELLHDLTRHhgRTVVVVLHDLNfAVNYGDTLIFLRQGKVV 225
Cdd:PRK11176 483 GGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKN--RTSLVIAHRLS-TIEKADEILVVEDGEIV 557
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
10-226 |
1.07e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 78.20 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHKKI-----IVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHE--------- 75
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 76 -------QPT--------KALSRRLGILPQspllpegLTVYEL-------------VSRGRFPwqnfirqwsdadEQAVE 127
Cdd:PRK13651 83 vleklviQKTrfkkikkiKEIRRRVGVVFQ-------FAEYQLfeqtiekdiifgpVSMGVSK------------EEAKK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 128 EALKLTgtqEFAHLPVE-------KLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDLRYQVEILELLHDLTRhHGRTVV 200
Cdd:PRK13651 144 RAAKYI---ELVGLDESylqrspfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNK-QGKTII 219
|
250 260
....*....|....*....|....*.
gi 446863618 201 VVLHDLNFAVNYGDTLIFLRQGKVVR 226
Cdd:PRK13651 220 LVTHDLDNVLEWTKRTIFFKDGKIIK 245
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
21-225 |
1.34e-16 |
|
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: 77.15 E-value: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 21 KKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHE---QPTKALSRRLGILPQ---SPLL 94
Cdd:TIGR02769 23 RAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQldrKQRRAFRRDVQLVFQdspSAVN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 95 PEgLTVYELVsrgRFPWQNFIRQWSDADEQAVEEALKLTG--TQEFAHLPVEkLSGGQRQRCWIAMVLAQKTPYILLDEP 172
Cdd:TIGR02769 103 PR-MTVRQII---GEPLRHLTSLDESEQKARIAELLDMVGlrSEDADKLPRQ-LSGGQLQRINIARALAVKPKLIVLDEA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446863618 173 TTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:TIGR02769 178 VSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIV 230
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
22-225 |
1.43e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 78.94 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 22 KIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIA-RILQPM--GGSILLDGKAIHeqpTKALSRRLGILPQSPLLPEGL 98
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAfRSPKGVkgSGSVLLNGMPID---AKEMRAISAYVQQDDLFIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 99 TVYE-LVSRGRFPWQNfiRQWSDADEQAVEEALKLTGTQEFAHL------PVEKLSGGQRQRCWIAMVLAQKTPYILLDE 171
Cdd:TIGR00955 115 TVREhLMFQAHLRMPR--RVTKKEKRERVDEVLQALGLRKCANTrigvpgRVKGLSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 172 PTTWLDLRYQVEILELLHDLTRhHGRTVVVVLH----DL--NFavnygDTLIFLRQGKVV 225
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVLKGLAQ-KGKTIICTIHqpssELfeLF-----DKIILMAEGRVA 246
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
25-206 |
2.26e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 77.31 E-value: 2.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 25 VDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPT---KALSRRLGILPQSP---LLPE-- 96
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPeaqKLLRQKIQIVFQNPygsLNPRkk 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 97 -GLTVYElvsrgrfPWQnfIRQWSDADEQA--VEEALKLTGTQ-EFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEP 172
Cdd:PRK11308 111 vGQILEE-------PLL--INTSLSAAERRekALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEP 181
|
170 180 190
....*....|....*....|....*....|....
gi 446863618 173 TTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDL 206
Cdd:PRK11308 182 VSALDVSVQAQVLNLMMDLQQELGLSYVFISHDL 215
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
10-224 |
3.13e-16 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 77.90 E-value: 3.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHKKIIVDGVSFS-VPTEKMTVLvGANGCGKSTLLSTIARILQPMGGSILLdGKAIheqptkalsrRLGIL 88
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNlVPGSRIGLL-GRNGAGKSTLIKLLAGELAPVSGEIGL-AKGI----------KLGYF 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 89 PQSPLlpegltvyELVSRGRFPWQNFIRQWSDADEQAVEEALKLTGTQ-EFAHLPVEKLSGGQRQRCWIAMVLAQKTPYI 167
Cdd:PRK10636 381 AQHQL--------EFLRADESPLQHLARLAPQELEQKLRDYLGGFGFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLL 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446863618 168 LLDEPTTWLDLRYQVEILELLHDLTrhhgRTVVVVLHDLNFAVNYGDTLIFLRQGKV 224
Cdd:PRK10636 453 LLDEPTNHLDLDMRQALTEALIDFE----GALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
22-264 |
4.49e-16 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 75.96 E-value: 4.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 22 KIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIheqptKALSR--------RLGILPQSPL 93
Cdd:PRK11831 20 RCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENI-----PAMSRsrlytvrkRMSMLFQSGA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 94 LPEGLTVYELVSrgrFPWQNFIRQWSDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPT 173
Cdd:PRK11831 95 LFTDMNVFDNVA---YPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 174 TWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVVrvlnegEHCTPELVKAVFDVDVHASINP 253
Cdd:PRK11831 172 VGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIV------AHGSAQALQANPDPRVRQFLDG 245
|
250
....*....|.
gi 446863618 254 LTGKPffMPFR 264
Cdd:PRK11831 246 IADGP--VPFR 254
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
24-237 |
5.35e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 77.71 E-value: 5.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 24 IVDGVSFSV-PTEKMTVlVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLGILPQSPLLPEGLTVYE 102
Cdd:PLN03232 1251 VLHGLSFFVsPSEKVGV-VGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFN 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 103 LvsrGRFPWQNFIRQWSDADEQAVEEALKLT--GTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDLRy 180
Cdd:PLN03232 1330 I---DPFSEHNDADLWEALERAHIKDVIDRNpfGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVR- 1405
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446863618 181 qveILELLHDLTRHHGR--TVVVVLHDLNFAVNYgDTLIFLRQGKVVrvlnegEHCTPE 237
Cdd:PLN03232 1406 ---TDSLIQRTIREEFKscTMLVIAHRLNTIIDC-DKILVLSSGQVL------EYDSPQ 1454
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-225 |
6.02e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 75.52 E-value: 6.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 14 NVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGG-----SILLDGKAI-HEQPTKALSRRLGI 87
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfNYRDVLEFRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 88 LPQSP-LLP--------EGLTVYELVSRGRFPwqnfirqwSDADEQAVEEALKLTGTQEFAHLPVeKLSGGQRQRCWIAM 158
Cdd:PRK14271 106 LFQRPnPFPmsimdnvlAGVRAHKLVPRKEFR--------GVAQARLTEVGLWDAVKDRLSDSPF-RLSGGQQQLLCLAR 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446863618 159 VLAQKTPYILLDEPTTWLDLRYQVEILELLHDLTRHhgRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:PRK14271 177 TLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLV 241
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
12-227 |
6.38e-16 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 76.28 E-value: 6.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 12 LDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEqpTKALSRRLGILPQS 91
Cdd:PRK10851 5 IANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSR--LHARDRKVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 92 PLLPEGLTVYELVSRGRFPWQNFIRQWSDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDE 171
Cdd:PRK10851 83 YALFRHMTVFDNIAFGLTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446863618 172 PTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVVRV 227
Cdd:PRK10851 163 PFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQA 218
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
12-233 |
9.42e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 76.68 E-value: 9.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 12 LDNVSAGYHK-KIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLGILPQ 90
Cdd:PRK10790 343 IDNVSFAYRDdNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQ 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 91 SPLLPEGlTVYELVSRGRfpwqnfirqwsDADEQAVEEALKLTGTQEFAH-LPV----------EKLSGGQRQRCWIAMV 159
Cdd:PRK10790 423 DPVVLAD-TFLANVTLGR-----------DISEEQVWQALETVQLAELARsLPDglytplgeqgNNLSVGQKQLLALARV 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446863618 160 LAQkTPYIL-LDEPTTWLDLRYQVEILELLHDLTRHhgRTVVVVLHDLNFAVNyGDTLIFLRQGKVVRvlnEGEH 233
Cdd:PRK10790 491 LVQ-TPQILiLDEATANIDSGTEQAIQQALAAVREH--TTLVVIAHRLSTIVE-ADTILVLHRGQAVE---QGTH 558
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
21-208 |
1.12e-15 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 76.51 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 21 KKIIVDGVSFS-VPTEKMTVLvGANGCGKSTLLSTIARILQPMGGSILLdgkaiheqptkALSRRLGILPQSPLLPEGLT 99
Cdd:TIGR03719 17 KKEILKDISLSfFPGAKIGVL-GLNGAGKSTLLRIMAGVDKDFNGEARP-----------QPGIKVGYLPQEPQLDPTKT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 100 VYELVSRGRFPWQNFIRQWS---------DAD------EQA-VEEALKLTGTQEFAH---------------LPVEKLSG 148
Cdd:TIGR03719 85 VRENVEEGVAEIKDALDRFNeisakyaepDADfdklaaEQAeLQEIIDAADAWDLDSqleiamdalrcppwdADVTKLSG 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 149 GQRQRCWIAMVLAQKTPYILLDEPTTWLDLRyQVEILEllHDLTRHHGrTVVVVLHDLNF 208
Cdd:TIGR03719 165 GERRRVALCRLLLSKPDMLLLDEPTNHLDAE-SVAWLE--RHLQEYPG-TVVAVTHDRYF 220
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
10-225 |
1.32e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 76.28 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGY----HKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQ--PM---GGSILLDGKAIHEQPTKA 80
Cdd:PRK15134 6 LAIENLSVAFrqqqTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPspPVvypSGDIRFHGESLLHASEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 81 LSR----RLGILPQSPL--------LPEGLtvYELVS--RGrfpwqnfIRQwsDADEQAVEEALKLTGTQ-------EFA 139
Cdd:PRK15134 86 LRGvrgnKIAMIFQEPMvslnplhtLEKQL--YEVLSlhRG-------MRR--EAARGEILNCLDRVGIRqaakrltDYP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 140 HlpveKLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFL 219
Cdd:PRK15134 155 H----QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVM 230
|
....*.
gi 446863618 220 RQGKVV 225
Cdd:PRK15134 231 QNGRCV 236
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
27-225 |
2.09e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 72.99 E-value: 2.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 27 GVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKA---LSRRLGILPQSPLLPEGLTVYEL 103
Cdd:PRK10908 20 GVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDHHLLMDRTVYDN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 104 VSrgrFPWqnFIRQWSDAD-EQAVEEALKLTGTQEFA-HLPVEkLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDLRYQ 181
Cdd:PRK10908 100 VA---IPL--IIAGASGDDiRRRVSAALDKVGLLDKAkNFPIQ-LSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALS 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446863618 182 VEILELLHDLTRhHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:PRK10908 174 EGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
10-240 |
2.53e-15 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 73.18 E-value: 2.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARI--LQPMGGSILLDGKAIHEQPT--KAlsrRL 85
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPdeRA---RA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 86 GILP--QSPLLPEGLTVYEL-------VSRGRFPWQNFIRQwsdadeqaVEEALKLTG-TQEFAHLPV-EKLSGGQRQRC 154
Cdd:COG0396 78 GIFLafQYPVEIPGVSVSNFlrtalnaRRGEELSAREFLKL--------LKEKMKELGlDEDFLDRYVnEGFSGGEKKRN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 155 WIAMVLAQKTPYILLDEPTTWLD---LRYQVEILELLHDltrhHGRTVVVVLHD---LNFAVnyGDTLIFLRQGKVVRvl 228
Cdd:COG0396 150 EILQMLLLEPKLAILDETDSGLDidaLRIVAEGVNKLRS----PDRGILIITHYqriLDYIK--PDFVHVLVDGRIVK-- 221
|
250
....*....|..
gi 446863618 229 nEGehcTPELVK 240
Cdd:COG0396 222 -SG---GKELAL 229
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
25-223 |
2.54e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 75.35 E-value: 2.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 25 VDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILqPMG---GSILLDGKAIHEQPTKAlSRRLG--ILPQSPLLPEGLT 99
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEGEELQASNIRD-TERAGiaIIHQELALVKELS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 100 VYELVSRGRFPWQNFIRQWsDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDlR 179
Cdd:PRK13549 99 VLENIFLGNEITPGGIMDY-DAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLT-E 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446863618 180 YQVEIL-ELLHDLtRHHGRTVVVVLHDLN--FAVNygDTLIFLRQGK 223
Cdd:PRK13549 177 SETAVLlDIIRDL-KAHGIACIYISHKLNevKAIS--DTICVIRDGR 220
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
13-205 |
2.66e-15 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 75.36 E-value: 2.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 13 DNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLdGKAIHeqptkalsrrLGILPQSp 92
Cdd:TIGR03719 326 ENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK----------LAYVDQS- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 93 llPEGL----TVYELVSRG------------------RFpwqNFirqwSDADEQaveealKLTGtqefahlpveKLSGGQ 150
Cdd:TIGR03719 394 --RDALdpnkTVWEEISGGldiiklgkreipsrayvgRF---NF----KGSDQQ------KKVG----------QLSGGE 448
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446863618 151 RQRCWIAMVLAQKTPYILLDEPTTWLDlryqVEILELLHDLTRHHGRTVVVVLHD 205
Cdd:TIGR03719 449 RNRVHLAKTLKSGGNVLLLDEPTNDLD----VETLRALEEALLNFAGCAVVISHD 499
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
28-222 |
3.32e-15 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 72.36 E-value: 3.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 28 VSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRR----LGILPQSPLLPEGlTVYEL 103
Cdd:cd03290 20 INIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLLNA-TVEEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 104 VSRGR-FPWQNFirqwsdadeQAVEEALKLT--------GTQ-EFAHLPVeKLSGGQRQRCWIAMVLAQKTPYILLDEPT 173
Cdd:cd03290 99 ITFGSpFNKQRY---------KAVTDACSLQpdidllpfGDQtEIGERGI-NLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446863618 174 TWLDLR-----YQVEILELLHDltrhHGRTVVVVLHDLNFaVNYGDTLIFLRQG 222
Cdd:cd03290 169 SALDIHlsdhlMQEGILKFLQD----DKRTLVLVTHKLQY-LPHADWIIAMKDG 217
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
8-208 |
4.16e-15 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 74.54 E-value: 4.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 8 QGLILDNVSAGYHKKIIVDGVSFSV-PTEKMTVLvGANGCGKSTLLSTIARILQPMGGSILLDGKAiheqptkalsrRLG 86
Cdd:PRK15064 318 NALEVENLTKGFDNGPLFKNLNLLLeAGERLAII-GENGVGKTTLLRTLVGELEPDSGTVKWSENA-----------NIG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 87 ILPQ--SPLLPEGLTVYElvsrgrfpWqnfIRQWSDA--DEQAVEEAL-KLTGTQEFAHLPVEKLSGGQRQRCWIAMVLA 161
Cdd:PRK15064 386 YYAQdhAYDFENDLTLFD--------W---MSQWRQEgdDEQAVRGTLgRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMM 454
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446863618 162 QKTPYILLDEPTTWLDLryqvEILELLHDLTRHHGRTVVVVLHDLNF 208
Cdd:PRK15064 455 QKPNVLVMDEPTNHMDM----ESIESLNMALEKYEGTLIFVSHDREF 497
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
10-226 |
4.29e-15 |
|
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: 71.79 E-value: 4.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIA--RILQPMGGSILLDGKAIHEQPTKALSRR-LG 86
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMghPKYEVTEGEILFKGEDITDLPPEERARLgIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 87 ILPQSPLLPEGLTVyelvsrgrfpwQNFIRqwsdadeqaveealkltgtqefahlPV-EKLSGGQRQRCWIAMVLAQKTP 165
Cdd:cd03217 81 LAFQYPPEIPGVKN-----------ADFLR-------------------------YVnEGFSGGEKKRNEILQLLLLEPD 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446863618 166 YILLDEPTTWLD---LRYQVEILELLHDLtrhhGRTVVVVLHDLNFAvNY--GDTLIFLRQGKVVR 226
Cdd:cd03217 125 LAILDEPDSGLDidaLRLVAEVINKLREE----GKSVLIITHYQRLL-DYikPDRVHVLYDGRIVK 185
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
12-211 |
5.24e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 74.60 E-value: 5.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 12 LDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGK---AIHEQPTKALSrrlgil 88
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKlevAYFDQHRAELD------ 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 89 pqspllPEGlTVYELVSRGRfpwqnfirqwsdadeQAVE----EALKLTGTQEF------AHLPVEKLSGGQRQRCWIAM 158
Cdd:PRK11147 396 ------PEK-TVMDNLAEGK---------------QEVMvngrPRHVLGYLQDFlfhpkrAMTPVKALSGGERNRLLLAR 453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446863618 159 VLAQKTPYILLDEPTTWLDlryqVEILELLHDLTRHHGRTVVVVLHDLNFAVN 211
Cdd:PRK11147 454 LFLKPSNLLILDEPTNDLD----VETLELLEELLDSYQGTVLLVSHDRQFVDN 502
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
21-235 |
9.83e-15 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 73.99 E-value: 9.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 21 KKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQpMG----GSILLDGKAIHEqptkALSRRLGILPQSPLLPE 96
Cdd:TIGR00956 775 KRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVT-TGvitgGDRLVNGRPLDS----SFQRSIGYVQQQDLHLP 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 97 GLTVYELVsrgRFpwQNFIRQ---WSDADE-QAVEEALKLTGTQEFAH----LPVEKLSGGQRQRCWIAMVLAQKTPYIL 168
Cdd:TIGR00956 850 TSTVRESL---RF--SAYLRQpksVSKSEKmEYVEEVIKLLEMESYADavvgVPGEGLNVEQRKRLTIGVELVAKPKLLL 924
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446863618 169 -LDEPTTWLDLRYQVEILELLHDLTRhHGRTVVVVLH----DL--NFavnygDTLIFLRQG-KVVRVLNEGEHCT 235
Cdd:TIGR00956 925 fLDEPTSGLDSQTAWSICKLMRKLAD-HGQAILCTIHqpsaILfeEF-----DRLLLLQKGgQTVYFGDLGENSH 993
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
25-206 |
1.16e-14 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 72.45 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 25 VDGVSFSVPTEKMTVLVGANGCGKST-------LLSTIARIlqpmGGSILLDGKAIHEQPTKALSR----RLGILPQSPL 93
Cdd:PRK09473 32 VNDLNFSLRAGETLGIVGESGSGKSQtafalmgLLAANGRI----GGSATFNGREILNLPEKELNKlraeQISMIFQDPM 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 94 ------------LPEGLTVYELVSRgrfpwqnfirqwSDADEQAVE--EALKLTGTQEFAHLPVEKLSGGQRQRCWIAMV 159
Cdd:PRK09473 108 tslnpymrvgeqLMEVLMLHKGMSK------------AEAFEESVRmlDAVKMPEARKRMKMYPHEFSGGMRQRVMIAMA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446863618 160 LAQKTPYILLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDL 206
Cdd:PRK09473 176 LLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDL 222
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
21-205 |
2.25e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 72.46 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 21 KKIIVDGVSFS-VPTEKMTVLvGANGCGKSTLLSTIARILQPmggsilLDGKAIHEQPTKalsrrLGILPQSPLLPEGLT 99
Cdd:PRK11819 19 KKQILKDISLSfFPGAKIGVL-GLNGAGKSTLLRIMAGVDKE------FEGEARPAPGIK-----VGYLPQEPQLDPEKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 100 VYELVSRG---------RFP--WQNFIRQWSD----ADEQA-VEEAL------KLTGTQEFA----HLP-----VEKLSG 148
Cdd:PRK11819 87 VRENVEEGvaevkaaldRFNeiYAAYAEPDADfdalAAEQGeLQEIIdaadawDLDSQLEIAmdalRCPpwdakVTKLSG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446863618 149 GQRQRCWIAMVLAQKTPYILLDEPTTWLDLRyQVEILEllHDLTRHHGrTVVVVLHD 205
Cdd:PRK11819 167 GERRRVALCRLLLEKPDMLLLDEPTNHLDAE-SVAWLE--QFLHDYPG-TVVAVTHD 219
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
25-225 |
2.86e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 72.20 E-value: 2.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 25 VDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGK----------AIHEQPTKALSRRLG----ILPQ 90
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqviELSEQSAAQMRHVRGadmaMIFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 91 SPL--LPEGLTVYELVSRGRFPWQNFIRQWSDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYIL 168
Cdd:PRK10261 112 EPMtsLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLI 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446863618 169 LDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:PRK10261 192 ADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
21-223 |
3.04e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 72.22 E-value: 3.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 21 KKIIVDGVS-FSVPTEKMTVLvGANGCGKSTLLSTIARILQPMG--GSILLDGKaiheQPTKALSRRLGILPQSPLLPEG 97
Cdd:PLN03211 80 ERTILNGVTgMASPGEILAVL-GPSGSGKSTLLNALAGRIQGNNftGTILANNR----KPTKQILKRTGFVTQDDILYPH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 98 LTVYE---LVSRGRFPwQNFIRQWSDADEQAVEEALKLT--GTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEP 172
Cdd:PLN03211 155 LTVREtlvFCSLLRLP-KSLTKQEKILVAESVISELGLTkcENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEP 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446863618 173 TTWLDLRYQVEILELLHDLTrHHGRTVVVVLHDLNFAV-NYGDTLIFLRQGK 223
Cdd:PLN03211 234 TSGLDATAAYRLVLTLGSLA-QKGKTIVTSMHQPSSRVyQMFDSVLVLSEGR 284
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
25-208 |
6.42e-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: 69.00 E-value: 6.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 25 VDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSIL-------LDGKAIHEQPTKALSRR--------LGILP 89
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILvrhdggwVDLAQASPREILALRRRtigyvsqfLRVIP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 90 QSPLLPeglTVYE-LVSRGRfpwqnfirqwsdADEQAVEEALKLtgtqeFAHLPV-EKL--------SGGQRQRCWIAMV 159
Cdd:COG4778 107 RVSALD---VVAEpLLERGV------------DREEARARAREL-----LARLNLpERLwdlppatfSGGEQQRVNIARG 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446863618 160 LAQKTPYILLDEPTTWLDLRYQVEILELLHDLtRHHGRTVVVVLHDLNF 208
Cdd:COG4778 167 FIADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDEEV 214
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
12-237 |
6.63e-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: 6.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 12 LDNVSAGYHkkiiVDGVSFSV-PTEkmtVL--VGANGCGKSTLLSTIARILQPMGGSILLDGKAIH-EQPTKALSRRLGi 87
Cdd:COG1129 259 VEGLSVGGV----VRDVSFSVrAGE---ILgiAGLVGAGRTELARALFGADPADSGEIRLDGKPVRiRSPRDAIRAGIA- 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 88 lpqspLLPE---------GLTVYE---LVSRGRFPWQNFIRQwsDADEQAVEEALKL----TGTQEfahLPVEKLSGGQR 151
Cdd:COG1129 331 -----YVPEdrkgeglvlDLSIREnitLASLDRLSRGGLLDR--RRERALAEEYIKRlrikTPSPE---QPVGNLSGGNQ 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 152 QRCWIAMVLAQKTPYILLDEPTTWLDLRYQVEILELLHDLTRhHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVVRVLnEG 231
Cdd:COG1129 401 QKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAA-EGKAVIVISSELPELLGLSDRILVMREGRIVGEL-DR 478
|
....*.
gi 446863618 232 EHCTPE 237
Cdd:COG1129 479 EEATEE 484
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
14-225 |
7.19e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 69.72 E-value: 7.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 14 NVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLlstiARIL----QPMGGSILLDGKAIHEQPT---KALSRRLG 86
Cdd:PRK10419 17 GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTL----ARLLvgleSPSQGNVSWRGEPLAKLNRaqrKAFRRDIQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 87 ILPQSPL--LPEGLTVYELVsrgRFPWQNFIRqWSDADEQA-VEEALKLTG-TQEFAHLPVEKLSGGQRQRCWIAMVLAQ 162
Cdd:PRK10419 93 MVFQDSIsaVNPRKTVREII---REPLRHLLS-LDKAERLArASEMLRAVDlDDSVLDKRPPQLSGGQLQRVCLARALAV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446863618 163 KTPYILLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:PRK10419 169 EPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
25-206 |
9.93e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 69.74 E-value: 9.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 25 VDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTK---ALSRRLGILPQSPL--LPEGLT 99
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDewrAVRSDIQMIFQDPLasLNPRMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 100 VYELVSRgrfPWQNFIRQWSDAD-EQAVEEALKLTG-----TQEFAHlpveKLSGGQRQRCWIAMVLAQKTPYILLDEPT 173
Cdd:PRK15079 117 IGEIIAE---PLRTYHPKLSRQEvKDRVKAMMLKVGllpnlINRYPH----EFSGGQCQRIGIARALILEPKLIICDEPV 189
|
170 180 190
....*....|....*....|....*....|...
gi 446863618 174 TWLDLRYQVEILELLHDLTRHHGRTVVVVLHDL 206
Cdd:PRK15079 190 SALDVSIQAQVVNLLQQLQREMGLSLIFIAHDL 222
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
16-223 |
1.04e-13 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 67.88 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 16 SAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSIlldgkaiheqptkALSRRLGILPQSPLLP 95
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV-------------SVPGSIAYVSQEPWIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 96 EGlTVYElvsrgrfpwqN--FIRQWsdaDEQAVEEALKLTG-TQEFAHLPV-------EK---LSGGQRQRCWIAMVLAQ 162
Cdd:cd03250 79 NG-TIRE----------NilFGKPF---DEERYEKVIKACAlEPDLEILPDgdlteigEKginLSGGQKQRISLARAVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446863618 163 KTPYILLDEPTTWLDLRYQVEILE--LLHDLtrHHGRTVVVVLHDLNFaVNYGDTLIFLRQGK 223
Cdd:cd03250 145 DADIYLLDDPLSAVDAHVGRHIFEncILGLL--LNNKTRILVTHQLQL-LPHADQIVVLDNGR 204
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
20-233 |
1.08e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 70.51 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 20 HKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLGILPQSPLLPEGlT 99
Cdd:PRK10789 326 TDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSD-T 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 100 VYELVSRGRfpwqnfirqwSDADEQAVEEALKLTGTQE-FAHLPV-------EK---LSGGQRQRCWIAMVLAQKTPYIL 168
Cdd:PRK10789 405 VANNIALGR----------PDATQQEIEHVARLASVHDdILRLPQgydtevgERgvmLSGGQKQRISIARALLLNAEILI 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446863618 169 LDEPTTWLDLRYQVEIlelLHDLTR-HHGRTVVVVLHDLNfAVNYGDTLIFLRQGKVVRvlnEGEH 233
Cdd:PRK10789 475 LDDALSAVDGRTEHQI---LHNLRQwGEGRTVIISAHRLS-ALTEASEILVMQHGHIAQ---RGNH 533
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
39-217 |
1.33e-13 |
|
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: 68.59 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 39 VLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKalsrrlgILPQSPLlpeglTVYELVSRgrfpwqnfIRQW 118
Cdd:cd03237 29 GILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQY-------IKADYEG-----TVRDLLSS--------ITKD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 119 SDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDLRYQVEILELLHDLTRHHGRT 198
Cdd:cd03237 89 FYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKT 168
|
170
....*....|....*....
gi 446863618 199 VVVVLHDLNFAVNYGDTLI 217
Cdd:cd03237 169 AFVVEHDIIMIDYLADRLI 187
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
11-206 |
1.51e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 70.27 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 11 ILDNVSAGYHKkiiVDGVSFSV-PTEKMTvLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPT---KALSRRLG 86
Cdd:PRK10261 329 LLNRVTREVHA---VEKVSFDLwPGETLS-LVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPgklQALRRDIQ 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 87 ILPQSP---LLPEGLTVYELVSRGRFpwQNFIRqwSDADEQAVEEALKLTGTQ-EFAHLPVEKLSGGQRQRCWIAMVLAQ 162
Cdd:PRK10261 405 FIFQDPyasLDPRQTVGDSIMEPLRV--HGLLP--GKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALAL 480
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446863618 163 KTPYILLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDL 206
Cdd:PRK10261 481 NPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDM 524
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
13-205 |
1.92e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 69.76 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 13 DNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLdGKAIHeqptkalsrrLGILPQSp 92
Cdd:PRK11819 328 ENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVK----------LAYVDQS- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 93 llPEGL----TVYELVSRG------------------RFpwqNFirqwSDADEQaveealKLTGTqefahlpvekLSGGQ 150
Cdd:PRK11819 396 --RDALdpnkTVWEEISGGldiikvgnreipsrayvgRF---NF----KGGDQQ------KKVGV----------LSGGE 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446863618 151 RQRCWIAMVLAQKTPYILLDEPTTWLDlryqVEILELLHDLTRHHGRTVVVVLHD 205
Cdd:PRK11819 451 RNRLHLAKTLKQGGNVLLLDEPTNDLD----VETLRALEEALLEFPGCAVVISHD 501
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-206 |
1.97e-13 |
|
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: 68.16 E-value: 1.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 32 VPTE-KMTVLVGANGCGKSTLLSTIARILQPMGGSI--------LLD---GKAIHEQPTKALSRRLG--ILPQS-PLLPE 96
Cdd:cd03236 22 VPREgQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeILDefrGSELQNYFTKLLEGDVKviVKPQYvDLIPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 97 GL--TVYELVSRgrfpwqnfirqwsdADEQA----VEEALKLTGTQEFAhlpVEKLSGGQRQRCWIAMVLAQKTPYILLD 170
Cdd:cd03236 102 AVkgKVGELLKK--------------KDERGkldeLVDQLELRHVLDRN---IDQLSGGELQRVAIAAALARDADFYFFD 164
|
170 180 190
....*....|....*....|....*....|....*.
gi 446863618 171 EPTTWLDLRYQVEILELLHDLTRhHGRTVVVVLHDL 206
Cdd:cd03236 165 EPSSYLDIKQRLNAARLIRELAE-DDNYVLVVEHDL 199
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
12-177 |
2.24e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 69.77 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 12 LDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIA--RILQpmGGSI-LLDG---KAIHEQptkALSRRL 85
Cdd:NF033858 4 LEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAgaRKIQ--QGRVeVLGGdmaDARHRR---AVCPRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 86 GILPQ---SPLLPEgLTVYELVsrgrfpwQNFIRQWS-DADE--QAVEEALKLTGTQEFAHLPVEKLSGGQRQR----Cw 155
Cdd:NF033858 79 AYMPQglgKNLYPT-LSVFENL-------DFFGRLFGqDAAErrRRIDELLRATGLAPFADRPAGKLSGGMKQKlglcC- 149
|
170 180
....*....|....*....|...
gi 446863618 156 iAMVlaqKTPYIL-LDEPTTWLD 177
Cdd:NF033858 150 -ALI---HDPDLLiLDEPTTGVD 168
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
6-226 |
3.98e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 67.95 E-value: 3.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 6 KGQGLILDNVSAGYHKK-----IIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSI-----LLDGKAIHE 75
Cdd:PRK13631 18 DDIILRVKNLYCVFDEKqenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiYIGDKKNNH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 76 QPT-----------KALSRRLGILPQSP---LLPEglTVYELVSRGRFpwqNFIRQWSDADEQAVEEALKLTGTQEFAHL 141
Cdd:PRK13631 98 ELItnpyskkiknfKELRRRVSMVFQFPeyqLFKD--TIEKDIMFGPV---ALGVKKSEAKKLAKFYLNKMGLDDSYLER 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 142 PVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDLRYQVEILELLHDlTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQ 221
Cdd:PRK13631 173 SPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDK 251
|
....*
gi 446863618 222 GKVVR 226
Cdd:PRK13631 252 GKILK 256
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
3-224 |
4.20e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 69.04 E-value: 4.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 3 HNAKGQGLILDNVSAGYHK--KIIVDGVSFSV-PTEKMTVlVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTK 79
Cdd:PTZ00243 1302 HPVQAGSLVFEGVQMRYREglPLVLRGVSFRIaPREKVGI-VGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLR 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 80 ALSRRLGILPQSPLLPEGlTVYelvsrgrfpwQNfIRQWSDADEQAVEEALKLTGTQEFAHLPVEKL-----------SG 148
Cdd:PTZ00243 1381 ELRRQFSMIPQDPVLFDG-TVR----------QN-VDPFLEASSAEVWAALELVGLRERVASESEGIdsrvleggsnySV 1448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446863618 149 GQRQRCWIAMVLAQK-TPYILLDEPTTWLDLRYQVEILELLhdLTRHHGRTVVVVLHDLNFAVNYgDTLIFLRQGKV 224
Cdd:PTZ00243 1449 GQRQLMCMARALLKKgSGFILMDEATANIDPALDRQIQATV--MSAFSAYTVITIAHRLHTVAQY-DKIIVMDHGAV 1522
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
10-224 |
4.77e-13 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 65.53 E-value: 4.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHkkiiVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIH-EQPTKALSRRLGIL 88
Cdd:cd03215 5 LEVRGLSVKGA----VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTrRSPRDAIRAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 89 PQSPLLpEGLtvyelvsrgrfpwqnfirqwsdADEQAVEEALKLtgtqefAHLpvekLSGGQRQRCWIAMVLAQKTPYIL 168
Cdd:cd03215 81 PEDRKR-EGL----------------------VLDLSVAENIAL------SSL----LSGGNQQKVVLARWLARDPRVLI 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446863618 169 LDEPTTWLDLRYQVEILELLHDLTRhHGRTVVVVLHDLNFAVNYGDTLIFLRQGKV 224
Cdd:cd03215 128 LDEPTRGVDVGAKAEIYRLIRELAD-AGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
9-224 |
7.05e-13 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 67.56 E-value: 7.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 9 GLILDNVSAGYHKKI-IVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAI-HEQPTKalsRRLG 86
Cdd:PRK11650 3 GLKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVnELEPAD---RDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 87 ILPQSPLLPEGLTVYElvsrgrfpwqNF-----IRQWSDAD-EQAVEEALKLTGTQEFAHLPVEKLSGGQRQRcwIAM-- 158
Cdd:PRK11650 80 MVFQNYALYPHMSVRE----------NMayglkIRGMPKAEiEERVAEAARILELEPLLDRKPRELSGGQRQR--VAMgr 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 159 VLAQKTPYILLDEPTTWLD--LRYQ--VEILElLHdltRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKV 224
Cdd:PRK11650 148 AIVREPAVFLFDEPLSNLDakLRVQmrLEIQR-LH---RRLKTTSLYVTHDQVEAMTLADRVVVMNGGVA 213
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
25-225 |
8.05e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 66.74 E-value: 8.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 25 VDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLGILPQSPllpegltVYELV 104
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDP-------STSLN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 105 SRGR------FPWQNFIRQWSDADEQAVEEALKLTG-TQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLD 177
Cdd:PRK15112 102 PRQRisqildFPLRLNTDLEPEQREKQIIETLRQVGlLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLD 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446863618 178 LRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:PRK15112 182 MSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVV 229
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
12-239 |
1.07e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 66.55 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 12 LDNVSAGYHKKI-IVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEqPTK--ALSRRLGIL 88
Cdd:PRK13644 4 LENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGD-FSKlqGIRKLVGIV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 89 PQSPLLP-EGLTVYELVSRGRfpwQNF------IRQwsdadeqAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLA 161
Cdd:PRK13644 83 FQNPETQfVGRTVEEDLAFGP---ENLclppieIRK-------RVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446863618 162 QKTPYILLDEPTTWLDLRYQVEILELLHDLTRhHGRTVVVVLHDLNfAVNYGDTLIFLRQGKVVRvlnEGEhctPELV 239
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLHE-KGKTIVYITHNLE-ELHDADRIIVMDRGKIVL---EGE---PENV 222
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
40-224 |
5.47e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 65.74 E-value: 5.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 40 LVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLGILPQSPLLPEGLTVYELVSRGrfpwqnfirQWS 119
Cdd:TIGR00957 1317 IVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFS---------QYS 1387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 120 DADeqaVEEALKLTGTQEF-AHLPV----------EKLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDLRYQVEILELL 188
Cdd:TIGR00957 1388 DEE---VWWALELAHLKTFvSALPDkldhecaeggENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTI 1464
|
170 180 190
....*....|....*....|....*....|....*.
gi 446863618 189 HdlTRHHGRTVVVVLHDLNFAVNYGDTLIfLRQGKV 224
Cdd:TIGR00957 1465 R--TQFEDCTVLTIAHRLNTIMDYTRVIV-LDKGEV 1497
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
14-176 |
6.89e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.07 E-value: 6.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 14 NVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAI-HEQPTKAlsRRLGI--LPQ 90
Cdd:PRK15439 16 SISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCaRLTPAKA--HQLGIylVPQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 91 SPLLPEGLTVYELVSrgrfpwqnFIRQWSDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLD 170
Cdd:PRK15439 94 EPLLFPNLSVKENIL--------FGLPKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILD 165
|
....*.
gi 446863618 171 EPTTWL 176
Cdd:PRK15439 166 EPTASL 171
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
26-230 |
9.15e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 64.64 E-value: 9.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 26 DGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIH-EQPTKALSRRLGILPQS-PLLPEgLTVYEL 103
Cdd:PRK10762 21 SGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSSQEAGIGIIHQElNLIPQ-LTIAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 104 VSRGRFPWQNFIR-QWSDADEQAvEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDLRYQV 182
Cdd:PRK10762 100 IFLGREFVNRFGRiDWKKMYAEA-DKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446863618 183 EILELLHDLtRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGK-----VVRVLNE 230
Cdd:PRK10762 179 SLFRVIREL-KSQGRGIVYISHRLKEIFEICDDVTVFRDGQfiaerEVADLTE 230
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
10-204 |
1.27e-11 |
|
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: 61.40 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVS----AGyhkKIIVDGVSFSVPtEKMTVLV-GANGCGKSTLLSTIARILQPMGGSIlldgkaihEQPTKAlsrR 84
Cdd:cd03223 1 IELENLSlatpDG---RVLLKDLSFEIK-PGDRLLItGPSGTGKSSLFRALAGLWPWGSGRI--------GMPEGE---D 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 85 LGILPQSPLLPEGlTVYELVSrgrFPWQnfirqwsdadeqaveealkltgtqefahlpvEKLSGGQRQRCWIAMVLAQKT 164
Cdd:cd03223 66 LLFLPQRPYLPLG-TLREQLI---YPWD-------------------------------DVLSGGEQQRLAFARLLLHKP 110
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446863618 165 PYILLDEPTTWLDlryqVEILELLHDLTRHHGRTVVVVLH 204
Cdd:cd03223 111 KFVFLDEATSALD----EESEDRLYQLLKELGITVISVGH 146
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
145-225 |
1.69e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 63.22 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 145 KLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKV 224
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQV 232
|
.
gi 446863618 225 V 225
Cdd:PRK11022 233 V 233
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
26-228 |
2.80e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 63.27 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 26 DGVSFSVPTEKMTVLVGANGCGKSTL---LSTIarilQPMG---GSILLDGKAIHEQPTKAlSRRLGI------LPQSPL 93
Cdd:NF040905 18 DDVNLSVREGEIHALCGENGAGKSTLmkvLSGV----YPHGsyeGEILFDGEVCRFKDIRD-SEALGIviihqeLALIPY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 94 LpeglTVYELVSRGRFPWQNFIRQWSDADEQAvEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPT 173
Cdd:NF040905 93 L----SIAENIFLGNERAKRGVIDWNETNRRA-RELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446863618 174 TWLDLRYQVEILELLHDLtRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVVRVL 228
Cdd:NF040905 168 AALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRTIETL 221
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
24-233 |
3.40e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 63.51 E-value: 3.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 24 IVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARIL-----------------------------QPMG----------- 63
Cdd:PTZ00265 1183 IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfknehtndmtneqdyqgdeeQNVGmknvnefsltk 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 64 --------------GSILLDGKAIHEQPTKALSRRLGILPQSPLLpEGLTVYELVSRGRfpwqnfirqwSDADEQAVEEA 129
Cdd:PTZ00265 1263 eggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPML-FNMSIYENIKFGK----------EDATREDVKRA 1331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 130 LKLTGTQEFAH-LPVE----------KLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDLRYQVEILELLHDLTRHHGRT 198
Cdd:PTZ00265 1332 CKFAAIDEFIEsLPNKydtnvgpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKT 1411
|
250 260 270
....*....|....*....|....*....|....*....
gi 446863618 199 VVVVLHDLNfAVNYGDTLIFL----RQGKVVRvlNEGEH 233
Cdd:PTZ00265 1412 IITIAHRIA-SIKRSDKIVVFnnpdRTGSFVQ--AHGTH 1447
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
14-203 |
5.77e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 60.35 E-value: 5.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 14 NVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAI------HEQPTKALSRRLGI 87
Cdd:PRK13540 6 ELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIkkdlctYQKQLCFVGHRSGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 88 LPQspllpegLTVYElvsrgrfpwQNFIRQWSDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYI 167
Cdd:PRK13540 86 NPY-------LTLRE---------NCLYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLW 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 446863618 168 LLDEPTTWLDlryQVEILELLHDLTRHHGRTVVVVL 203
Cdd:PRK13540 150 LLDEPLVALD---ELSLLTIITKIQEHRAKGGAVLL 182
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
24-237 |
6.91e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 62.35 E-value: 6.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 24 IVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILL-DGKAIHEQPTKALSRRLGILPQSPLL-------- 94
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLfsnsiknn 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 95 -------------------PEGLTVYE-LVSRGRFPWQ-----NFIRQWSDADE--------------QAVEEALKLTGT 135
Cdd:PTZ00265 480 ikyslyslkdlealsnyynEDGNDSQEnKNKRNSCRAKcagdlNDMSNTTDSNEliemrknyqtikdsEVVDVSKKVLIH 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 136 QEFAHLP----------VEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHD 205
Cdd:PTZ00265 560 DFVSALPdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHR 639
|
250 260 270
....*....|....*....|....*....|....*
gi 446863618 206 LNfAVNYGDTLIFL---RQGKVVRVLNEGEHCTPE 237
Cdd:PTZ00265 640 LS-TIRYANTIFVLsnrERGSTVDVDIIGEDPTKD 673
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
28-232 |
8.97e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.47 E-value: 8.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 28 VSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIH-EQPTKALsrRLGILpqspLLPE---------G 97
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDiRSPRDAI--RAGIM----LCPEdrkaegiipV 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 98 LTVYE---LVSRGRF-PWQNFI-RQWSD--ADEQAVEEALKLTGTQEfahlPVEKLSGGQRQRCWIAMVLAQKTPYILLD 170
Cdd:PRK11288 346 HSVADninISARRHHlRAGCLInNRWEAenADRFIRSLNIKTPSREQ----LIMNLSGGNQQKAILGRWLSEDMKVILLD 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446863618 171 EPTTWLDLRYQVEILELLHDLTRhHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVVRVLNEGE 232
Cdd:PRK11288 422 EPTRGIDVGAKHEIYNVIYELAA-QGVAVLFVSSDLPEVLGVADRIVVMREGRIAGELAREQ 482
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-206 |
1.31e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 61.36 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 32 VPTE-KMTVLVGANGCGKSTLLSTIARILQP-MG----------------GSILLD-------G--KAIHEqptkalsrr 84
Cdd:PRK13409 95 IPKEgKVTGILGPNGIGKTTAVKILSGELIPnLGdyeeepswdevlkrfrGTELQNyfkklynGeiKVVHK--------- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 85 lgilPQS-PLLPEGL--TVYELVSRgrfpwqnfirqwsdADEQ-AVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVL 160
Cdd:PRK13409 166 ----PQYvDLIPKVFkgKVRELLKK--------------VDERgKLDEVVERLGLENILDRDISELSGGELQRVAIAAAL 227
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446863618 161 AQKTPYILLDEPTTWLDLRYQVEILELLHDLTRhhGRTVVVVLHDL 206
Cdd:PRK13409 228 LRDADFYFFDEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHDL 271
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
14-227 |
1.47e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.59 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 14 NVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPmggsilLDGKAIHEQPTKALSRRLGILPQSPL 93
Cdd:COG2401 35 GVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKG------TPVAGCVDVPDNQFGREASLIDAIGR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 94 LPEGLTVYELVSRGRFpwqnfirqwSDAdeqaveeALKLTgtqefahlPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPT 173
Cdd:COG2401 109 KGDFKDAVELLNAVGL---------SDA-------VLWLR--------RFKELSTGQKFRFRLALLLAERPKLLVIDEFC 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446863618 174 TWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFaVNY--GDTLIFLRQGKVVRV 227
Cdd:COG2401 165 SHLDRQTAKRVARNLQKLARRAGITLVVATHHYDV-IDDlqPDLLIFVGYGGVPEE 219
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-206 |
2.01e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 60.57 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 32 VPTE-KMTVLVGANGCGKSTLLSTIARILQP-MG----------------GSILLDG-KAIHEQPTKAlSRRlgilPQS- 91
Cdd:COG1245 95 VPKKgKVTGILGPNGIGKSTALKILSGELKPnLGdydeepswdevlkrfrGTELQDYfKKLANGEIKV-AHK----PQYv 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 92 PLLPEGL--TVYELVSRgrfpwqnfirqwsdADEQ-AVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYIL 168
Cdd:COG1245 170 DLIPKVFkgTVRELLEK--------------VDERgKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190
....*....|....*....|....*....|....*...
gi 446863618 169 LDEPTTWLDLRYQVEILELLHDLTRhHGRTVVVVLHDL 206
Cdd:COG1245 236 FDEPSSYLDIYQRLNVARLIRELAE-EGKYVLVVEHDL 272
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
28-224 |
3.33e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 60.26 E-value: 3.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 28 VSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAiheqptkalsrRLGILPQSPLlpEGLtvyELVSRg 107
Cdd:PLN03073 528 LNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKV-----------RMAVFSQHHV--DGL---DLSSN- 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 108 rfPWQNFIRQWSDADEQAVEEALKLTG-TQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDLRyQVEilE 186
Cdd:PLN03073 591 --PLLYMMRCFPGVPEQKLRAHLGSFGvTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLD-AVE--A 665
|
170 180 190
....*....|....*....|....*....|....*...
gi 446863618 187 LLHDLTRHHGrTVVVVLHDLNFAVNYGDTLIFLRQGKV 224
Cdd:PLN03073 666 LIQGLVLFQG-GVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
41-206 |
3.34e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 60.18 E-value: 3.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 41 VGANGCGKSTLLSTIARILQPMGGSILLDGKaiheqptkaLSRRlgilPQ--SPLLPEglTVYEL---VSRGRFPwQNFI 115
Cdd:COG1245 372 VGPNGIGKTTFAKILAGVLKPDEGEVDEDLK---------ISYK----PQyiSPDYDG--TVEEFlrsANTDDFG-SSYY 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 116 RqwsdadeqavEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDLRYQVEILELLHDLTRHH 195
Cdd:COG1245 436 K----------TEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENR 505
|
170
....*....|.
gi 446863618 196 GRTVVVVLHDL 206
Cdd:COG1245 506 GKTAMVVDHDI 516
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
25-225 |
5.38e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 59.45 E-value: 5.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 25 VDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARIlQPMG---GSILLDGKAIHEQPTKALSRR-LGILPQSPLLPEGLTV 100
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHGtwdGEIYWSGSPLKASNIRDTERAgIVIIHQELTLVPELSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 101 YELVSRGRFPWQNFIRQWSDADEQAVEEALK-LTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDLR 179
Cdd:TIGR02633 96 AENIFLGNEITLPGGRMAYNAMYLRAKNLLReLQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEK 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446863618 180 YQVEILELLHDLTRhHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:TIGR02633 176 ETEILLDIIRDLKA-HGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
25-224 |
6.59e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 59.07 E-value: 6.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 25 VDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQ-PMGGSILLDGKAIH-EQPTKALSRRLGILPQS-------PLLP 95
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPVDiRNPAQAIRAGIAMVPEDrkrhgivPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 96 EGLTVyELVSRGRFPWQNFIRqwSDADEQAVEEALKLTGTQEFA-HLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTT 174
Cdd:TIGR02633 356 VGKNI-TLSVLKSFCFKMRID--AAAELQIIGSAIQRLKVKTASpFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446863618 175 WLDLRYQVEILELLHDLTRhHGRTVVVVLHDLNFAVNYGDTLIFLRQGKV 224
Cdd:TIGR02633 433 GVDVGAKYEIYKLINQLAQ-EGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
41-206 |
8.70e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 58.67 E-value: 8.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 41 VGANGCGKSTLLSTIARILQPMGGSILLDGKaIHEQPTKalsrrlgILPQSPLlpeglTVYELVSR--GRF---PWQNfi 115
Cdd:PRK13409 371 VGPNGIGKTTFAKLLAGVLKPDEGEVDPELK-ISYKPQY-------IKPDYDG-----TVEDLLRSitDDLgssYYKS-- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 116 rqwsdadeqaveEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDLRYQVEILELLHDLTRHH 195
Cdd:PRK13409 436 ------------EIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEER 503
|
170
....*....|.
gi 446863618 196 GRTVVVVLHDL 206
Cdd:PRK13409 504 EATALVVDHDI 514
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
11-203 |
1.43e-09 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 56.50 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 11 ILDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMG---GSILLDGKAIHEQPTKAlSRRLGI 87
Cdd:cd03233 9 ISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEFAEKY-PGEIIY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 88 LPQSPLLPEGLTVyelvsrgrfpwqnfirqwsdadEQAVEEALKLTGTQEfahlpVEKLSGGQRQRCWIAMVLAQKTPYI 167
Cdd:cd03233 88 VSEEDVHFPTLTV----------------------RETLDFALRCKGNEF-----VRGISGGERKRVSIAEALVSRASVL 140
|
170 180 190
....*....|....*....|....*....|....*.
gi 446863618 168 LLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVL 203
Cdd:cd03233 141 CWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSL 176
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
40-227 |
1.56e-09 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 57.89 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 40 LVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKA-------------LSRRLgILPQSPLLPEgltvyelvsr 106
Cdd:COG4615 363 IVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAyrqlfsavfsdfhLFDRL-LGLDGEADPA---------- 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 107 grfpwqnFIRQWsdadeqavEEALKLtgtqefAH-LPVE-------KLSGGQRQRcwIAMVLA--QKTPYILLDE----- 171
Cdd:COG4615 432 -------RAREL--------LERLEL------DHkVSVEdgrfsttDLSQGQRKR--LALLVAllEDRPILVFDEwaadq 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446863618 172 -PTtwldLR---YQveilELLHDLtRHHGRTVVVVLHDLN-FAVnyGDTLIFLRQGKVVRV 227
Cdd:COG4615 489 dPE----FRrvfYT----ELLPEL-KARGKTVIAISHDDRyFDL--ADRVLKMDYGKLVEL 538
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
38-220 |
3.03e-09 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 55.31 E-value: 3.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 38 TVLVGANGCGKSTLLSTIARIL---QPMGG-SILLDGKAIHEQPTKA---------------LSRRLGILPQSPllpegl 98
Cdd:cd03240 25 TLIVGQNGAGKTTIIEALKYALtgeLPPNSkGGAHDPKLIREGEVRAqvklafenangkkytITRSLAILENVI------ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 99 tvyelvsrgrfpwqnFIRQwsdadeqavEEALKLtgtqefAHLPVEKLSGGQRQ------RCWIAMVLAQKTPYILLDEP 172
Cdd:cd03240 99 ---------------FCHQ---------GESNWP------LLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEP 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446863618 173 TTWLDlRYQVE--ILELLHDLTRHHGRTVVVVLHDLNFaVNYGDTLIFLR 220
Cdd:cd03240 149 TTNLD-EENIEesLAEIIEERKSQKNFQLIVITHDEEL-VDAADHIYRVE 196
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
8-223 |
4.19e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 56.52 E-value: 4.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 8 QGLILDNVSAGYHKKiivdgvSFSVPTEKMTV-------LVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKA 80
Cdd:PRK10522 321 QTLELRNVTFAYQDN------GFSVGPINLTIkrgellfLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPED 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 81 LSRrlgilpqspLLPEGLTVYELVSRGRFPwQNFirqwsDADEQAVEEALKLTGTQEfaHLPVE-------KLSGGQRQR 153
Cdd:PRK10522 395 YRK---------LFSAVFTDFHLFDQLLGP-EGK-----PANPALVEKWLERLKMAH--KLELEdgrisnlKLSKGQKKR 457
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 154 CWIAMVLAQKTPYILLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFaVNYGDTLIFLRQGK 223
Cdd:PRK10522 458 LALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHY-FIHADRLLEMRNGQ 526
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
8-204 |
6.82e-09 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 56.30 E-value: 6.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 8 QGLILDNVS----AGyhkKIIVDGVSFSVPtEKMTVLV-GANGCGKSTLLSTIARILQPMGGSIlldgkaiheqpTKALS 82
Cdd:TIGR00954 450 NGIKFENIPlvtpNG---DVLIESLSFEVP-SGNNLLIcGPNGCGKSSLFRILGELWPVYGGRL-----------TKPAK 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 83 RRLGILPQSPLLPEGlTVYELVSRGRFPWQNFIRQWSDADEQAVEEALKLTG--TQEFAHLPV----EKLSGGQRQRCWI 156
Cdd:TIGR00954 515 GKLFYVPQRPYMTLG-TLRDQIIYPDSSEDMKRRGLSDKDLEQILDNVQLTHilEREGGWSAVqdwmDVLSGGEKQRIAM 593
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446863618 157 AMVLAQKTPYILLDEPTTWLdlryQVEILELLHDLTRHHGRTVVVVLH 204
Cdd:TIGR00954 594 ARLFYHKPQFAILDECTSAV----SVDVEGYMYRLCREFGITLFSVSH 637
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
42-198 |
8.83e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.47 E-value: 8.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 42 GANGCGKSTLLSTIARILQPMGGSILLDGkaiHEQPTKALSRRLGILPQSPLLPEGLTVYELVS-----RGRFPwqnfir 116
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQIDG---KTATRGDRSRFMAYLGHLPGLKADLSTLENLHflcglHGRRA------ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 117 qwsdadEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDLryqvEILELLHDLTRHHG 196
Cdd:PRK13543 115 ------KQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL----EGITLVNRMISAHL 184
|
..
gi 446863618 197 RT 198
Cdd:PRK13543 185 RG 186
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
10-232 |
1.05e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 55.42 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSA-GYHKKIIVDGVSFSV-PTEkmtVL--VGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALsRRL 85
Cdd:COG3845 258 LEVENLSVrDDRGVPALKDVSLEVrAGE---ILgiAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRER-RRL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 86 GI--LPQSPL---LPEGLTVYE---LVSRGRFPWQN--FIRqWSDADEQAvEEALKltgtqEF------AHLPVEKLSGG 149
Cdd:COG3845 334 GVayIPEDRLgrgLVPDMSVAEnliLGRYRRPPFSRggFLD-RKAIRAFA-EELIE-----EFdvrtpgPDTPARSLSGG 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 150 QRQRCWIAMVLAQKTPYILLDEPTTWLDLRYQVEILELLHDLtRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVVRVLN 229
Cdd:COG3845 407 NQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVP 485
|
...
gi 446863618 230 EGE 232
Cdd:COG3845 486 AAE 488
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
6-208 |
1.19e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.56 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 6 KGQGLILDNVSAGYHkkiivdgvsfsvPTEKMTvLVGANGCGKSTLLSTIARILQPMGGSILLDGK---AIHEQPTKALS 82
Cdd:PRK10636 11 RGVRVLLDNATATIN------------PGQKVG-LVGKNGCGKSTLLALLKNEISADGGSYTFPGNwqlAWVNQETPALP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 83 RrlgilpqsPLLpegltvyELVSRGRFPWQNFIRQWSDADEQAVEEALK---------------------LTG---TQEF 138
Cdd:PRK10636 78 Q--------PAL-------EYVIDGDREYRQLEAQLHDANERNDGHAIAtihgkldaidawtirsraaslLHGlgfSNEQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 139 AHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDLRyqvEILELLHDLTRHHGrTVVVVLHDLNF 208
Cdd:PRK10636 143 LERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLD---AVIWLEKWLKSYQG-TLILISHDRDF 208
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
27-223 |
1.40e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 53.10 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 27 GVSFSVPTEKMTVLVGANGCGKSTLLSTIARilqpmggsilldgkaiheqptKALSRRLGILPqsPLLPEGLTVyelvsr 106
Cdd:cd03238 13 NLDVSIPLNVLVVVTGVSGSGKSTLVNEGLY---------------------ASGKARLISFL--PKFSRNKLI------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 107 grfpwqnFIRQwsdadeqaveeaLKLTGTQEFAHLPVEK----LSGGQRQRCWIAMVLAQKTPYIL--LDEPTTWLDLRY 180
Cdd:cd03238 64 -------FIDQ------------LQFLIDVGLGYLTLGQklstLSGGELQRVKLASELFSEPPGTLfiLDEPSTGLHQQD 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446863618 181 QVEILELLHDLtRHHGRTVVVVLHDLNFaVNYGDTLIFL--RQGK 223
Cdd:cd03238 125 INQLLEVIKGL-IDLGNTVILIEHNLDV-LSSADWIIDFgpGSGK 167
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
8-182 |
2.31e-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: 54.92 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 8 QGLILDNVSAGyhkKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQpMGGSILLDGKAIHEQPTKALSRRLGI 87
Cdd:TIGR01271 1221 QGLTAKYTEAG---RAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 88 LPQSPLLPEG-----LTVYElvsrgrfpwqnfirQWSDADEQAVEEALKLTGTQEfaHLPVE----------KLSGGQRQ 152
Cdd:TIGR01271 1297 IPQKVFIFSGtfrknLDPYE--------------QWSDEEIWKVAEEVGLKSVIE--QFPDKldfvlvdggyVLSNGHKQ 1360
|
170 180 190
....*....|....*....|....*....|.
gi 446863618 153 RCWIAMVLAQKTPYILLDEPTTWLD-LRYQV 182
Cdd:TIGR01271 1361 LMCLARSILSKAKILLLDEPSAHLDpVTLQI 1391
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
39-217 |
3.38e-08 |
|
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: 52.19 E-value: 3.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 39 VLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKAlsrrlgilpqspllpegltvyelvsrgrfpwqnfirqw 118
Cdd:cd03222 29 GIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQYI-------------------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 119 sdadeqaveealkltgtqefahlpveKLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDLRYQVEILELLHDLTRHHGRT 198
Cdd:cd03222 71 --------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKT 124
|
170
....*....|....*....
gi 446863618 199 VVVVLHDLNFAVNYGDTLI 217
Cdd:cd03222 125 ALVVEHDLAVLDYLSDRIH 143
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
24-225 |
3.54e-08 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 53.37 E-value: 3.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 24 IVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQP----------MGGSILLdgKAIHEQPTKALSRRLGIL---PQ 90
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvtadrfrWNGIDLL--KLSPRERRKIIGREIAMIfqePS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 91 SPLLPEGLTVYELVS-------RGRFpWQNFirQWSDadEQAVEEaLKLTGTQEFAHL----PVEkLSGGQRQRCWIAMV 159
Cdd:COG4170 100 SCLDPSAKIGDQLIEaipswtfKGKW-WQRF--KWRK--KRAIEL-LHRVGIKDHKDImnsyPHE-LTEGECQKVMIAMA 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446863618 160 LAQKTPYILLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:COG4170 173 IANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTV 238
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
40-225 |
4.33e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.80 E-value: 4.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 40 LVGANGCGKSTLLSTIArilqpmgGSILLD-GKAIHEQPTKaLSRrlgiLPQSPLLPEGLTVYELVSRG---------RF 109
Cdd:PRK11147 34 LVGRNGAGKSTLMKILN-------GEVLLDdGRIIYEQDLI-VAR----LQQDPPRNVEGTVYDFVAEGieeqaeylkRY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 110 ----------PWQNFIRQWSDADEQ--------------AVEEALKLTgtqefAHLPVEKLSGGQRQRCWIAMVLAQKTP 165
Cdd:PRK11147 102 hdishlvetdPSEKNLNELAKLQEQldhhnlwqlenrinEVLAQLGLD-----PDAALSSLSGGWLRKAALGRALVSNPD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 166 YILLDEPTTWLDlryqVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:PRK11147 177 VLLLDEPTNHLD----IETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
24-182 |
3.05e-07 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 50.24 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 24 IVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQpMGGSILLDGKAIHEQPTKALSRRLGILPQSPLLPEGLTVYEL 103
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 104 VSRGrfpwqnfirQWSDAD--EQAVEEALKLTGTQEFAHLPVE------KLSGGQRQRCWIAMVLAQKTPYILLDEPTTW 175
Cdd:cd03289 98 DPYG---------KWSDEEiwKVAEEVGLKSVIEQFPGQLDFVlvdggcVLSHGHKQLMCLARSVLSKAKILLLDEPSAH 168
|
....*...
gi 446863618 176 LD-LRYQV 182
Cdd:cd03289 169 LDpITYQV 176
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
25-224 |
3.59e-07 |
|
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: 51.10 E-value: 3.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 25 VDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHeqptkalsrrlgiLPQSPLLpEGLTVYELV 104
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAY-------------VPQQAWI-QNDSLRENI 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 105 SRGRFPWQNFIRQwsdadeqaVEEALKLTGTQEFahLPV-------EK---LSGGQRQRCWIAMVLAQKTPYILLDEPTT 174
Cdd:TIGR00957 720 LFGKALNEKYYQQ--------VLEACALLPDLEI--LPSgdrteigEKgvnLSGGQKQRVSLARAVYSNADIYLFDDPLS 789
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446863618 175 WLDLRYQVEILE-LLHDLTRHHGRTVVVVLHDLNFaVNYGDTLIFLRQGKV 224
Cdd:TIGR00957 790 AVDAHVGKHIFEhVIGPEGVLKNKTRILVTHGISY-LPQVDVIIVMSGGKI 839
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
14-237 |
3.93e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 50.55 E-value: 3.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 14 NVSAGYHKKiiVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHeqptkalsrrlgilPQSPL 93
Cdd:PRK09700 270 NVTSRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS--------------PRSPL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 94 --LPEGLTvYELVSR---GRFPwqNF-IRQ-------------------WSDADEQAVEE------ALKLTGTQEfahlP 142
Cdd:PRK09700 334 daVKKGMA-YITESRrdnGFFP--NFsIAQnmaisrslkdggykgamglFHEVDEQRTAEnqrellALKCHSVNQ----N 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 143 VEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDLRYQVEILELLHDLTrHHGRTVVVVLHDLNFAVNYGDTLIFLRQG 222
Cdd:PRK09700 407 ITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLA-DDGKVILMVSSELPEIITVCDRIAVFCEG 485
|
250
....*....|....*
gi 446863618 223 KVVRVLNEGEHCTPE 237
Cdd:PRK09700 486 RLTQILTNRDDMSEE 500
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
33-220 |
5.46e-07 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 49.52 E-value: 5.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 33 PTEKMTVlVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLGILPQSPLLPEGLTVYELVSRGRFPWQ 112
Cdd:cd03288 46 PGQKVGI-CGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECKCTDD 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 113 NFIRQWSDADEQAVEEALKlTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDLRYQvEILELLhDLT 192
Cdd:cd03288 125 RLWEALEIAQLKNMVKSLP-GGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE-NILQKV-VMT 201
|
170 180
....*....|....*....|....*...
gi 446863618 193 RHHGRTVVVVLHDLNFAVNYGDTLIFLR 220
Cdd:cd03288 202 AFADRTVVTIAHRVSTILDADLVLVLSR 229
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
142-239 |
7.15e-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: 50.01 E-value: 7.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 142 PVEKLSGGQRQRCWIAMVLAQK----TPYILlDEPTTWLDLRYQVEILELLHDLtRHHGRTVVVVLHDLNfAVNYGDTLI 217
Cdd:TIGR00630 826 PATTLSGGEAQRIKLAKELSKRstgrTLYIL-DEPTTGLHFDDIKKLLEVLQRL-VDKGNTVVVIEHNLD-VIKTADYII 902
|
90 100
....*....|....*....|....*...
gi 446863618 218 FL------RQGKVVRVlnegehCTPELV 239
Cdd:TIGR00630 903 DLgpeggdGGGTVVAS------GTPEEV 924
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
28-224 |
8.73e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 49.66 E-value: 8.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 28 VSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKA-LSRRLGILP----QSPLL---PEGLT 99
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPedrqSSGLYldaPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 100 VYELVsRGRFPWqnFIRQwsdADEQAVEE------ALKLTGTQEfahlPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPT 173
Cdd:PRK15439 362 VCALT-HNRRGF--WIKP---ARENAVLEryrralNIKFNHAEQ----AARTLSGGNQQKVLIAKCLEASPQLLIVDEPT 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446863618 174 TWLDLRYQVEILELLHDLTRhHGRTVVVVLHDLNFAVNYGDTLIFLRQGKV 224
Cdd:PRK15439 432 RGVDVSARNDIYQLIRSIAA-QNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
25-225 |
1.14e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.34 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 25 VDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTK-ALSRRLGILPQSPLLPEGLTVYEL 103
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKeALENGISMVHQELNLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 104 VSRGRFPWQNFIrqwsdadeqaVEEALKLTGTQE-FAHL-----PVEK---LSGGQRQRCWIAMVLAQKTPYILLDEPTT 174
Cdd:PRK10982 94 MWLGRYPTKGMF----------VDQDKMYRDTKAiFDELdididPRAKvatLSVSQMQMIEIAKAFSYNAKIVIMDEPTS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446863618 175 WLDLRyQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:PRK10982 164 SLTEK-EVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
20-217 |
1.82e-06 |
|
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: 46.97 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 20 HKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQpMGGSILLDGKAIHEQPTKALSR--RLGILPQspllpeg 97
Cdd:cd03227 6 RFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALG-GAQSATRRRSGVKAGCIVAAVSaeLIFTRLQ------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 98 ltvyelvsrgrfpwqnfirqwsdadeqaveealkltgtqefahlpvekLSGGQRQRCWIAMVLA----QKTPYILLDEPT 173
Cdd:cd03227 78 ------------------------------------------------LSGGEKELSALALILAlaslKPRPLYILDEID 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446863618 174 TWLDLRYQVEILELLHDLtRHHGRTVVVVLHDLNFAVNYgDTLI 217
Cdd:cd03227 110 RGLDPRDGQALAEAILEH-LVKGAQVIVITHLPELAELA-DKLI 151
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
20-202 |
2.05e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.39 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 20 HKKIiVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIarilqpMG-------GSILLDGKAIH-EQPTKALSRRLGILPQS 91
Cdd:PRK13549 274 HIKR-VDDVSFSLRRGEILGIAGLVGAGRTELVQCL------FGaypgrweGEIFIDGKPVKiRNPQQAIAQGIAMVPED 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 92 -------PLLPEGLTVyELVSRGRFPWQNFIRqwsDADEQ--AVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIA-MVLA 161
Cdd:PRK13549 347 rkrdgivPVMGVGKNI-TLAALDRFTGGSRID---DAAELktILESIQRLKVKTASPELAIARLSGGNQQKAVLAkCLLL 422
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446863618 162 QktPYIL-LDEPTTWLDLRYQVEILELLHDLTRhHGRTVVVV 202
Cdd:PRK13549 423 N--PKILiLDEPTRGIDVGAKYEIYKLINQLVQ-QGVAIIVI 461
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
28-206 |
2.60e-06 |
|
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: 47.61 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 28 VSFSVPTEKMTVLVGANGCGKSTLlstiarilqpmggsilldgkaIHEQPTKALSRRLGILPQSPLLPEGLTVYELVSR- 106
Cdd:cd03271 14 IDVDIPLGVLTCVTGVSGSGKSSL---------------------INDTLYPALARRLHLKKEQPGNHDRIEGLEHIDKv 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 107 --------GRFPWQN---------FIRQW------------------------SDADEQAVEEAL-----------KLTG 134
Cdd:cd03271 73 ividqspiGRTPRSNpatytgvfdEIRELfcevckgkrynretlevrykgksiADVLDMTVEEALeffenipkiarKLQT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 135 TQE----FAHL--PVEKLSGGQRQRCWIAMVLAQ----KTPYILlDEPTTWL---DLRYQVEILELLHDLtrhhGRTVVV 201
Cdd:cd03271 153 LCDvglgYIKLgqPATTLSGGEAQRIKLAKELSKrstgKTLYIL-DEPTTGLhfhDVKKLLEVLQRLVDK----GNTVVV 227
|
....*
gi 446863618 202 VLHDL 206
Cdd:cd03271 228 IEHNL 232
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
36-229 |
4.33e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 45.44 E-value: 4.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 36 KMTVLVGANGCGKSTLLSTIARILQPMGGS-ILLDGKAIHEQPTKALSrrlgilpqspllpegltvyelvsrgrfpwqnf 114
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLL-------------------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 115 irqwsdadeqaveealkltgtQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDLRYQVEILEL-----LH 189
Cdd:smart00382 51 ---------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLL 109
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446863618 190 DLTRHHGRTVVVVLHDLNFavnYGDTLIFLRQGKVVRVLN 229
Cdd:smart00382 110 LLKSEKNLTVILTTNDEKD---LGPALLRRRFDRRIVLLL 146
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
25-209 |
4.91e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 47.43 E-value: 4.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 25 VDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAI--HEQPTKalsRRLGILPQSPLLPEGLTVYE 102
Cdd:NF033858 282 VDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdaGDIATR---RRVGYMSQAFSLYGELTVRQ 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 103 -LVSRGR-FpwqnfirQWSDAD-EQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKtPYIL-LDEPTT---- 174
Cdd:NF033858 359 nLELHARlF-------HLPAAEiAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHK-PELLiLDEPTSgvdp 430
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446863618 175 ------WldlryqveilELLHDLTRHHGRTVVVVLHDLNFA 209
Cdd:NF033858 431 vardmfW----------RLLIELSREDGVTIFISTHFMNEA 461
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
78-243 |
5.03e-06 |
|
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: 47.10 E-value: 5.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 78 TKALSRRLGILPQSPL-LPEGLTVYElvsrgrfpwqNFIRQWSDAD---EQAVEEALKLTGTQEFAHLPVE---KLSGGQ 150
Cdd:TIGR03269 104 RRRIRKRIAIMLQRTFaLYGDDTVLD----------NVLEALEEIGyegKEAVGRAVDLIEMVQLSHRITHiarDLSGGE 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 151 RQRCWIAMVLAqKTPYILL-DEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVVRvln 229
Cdd:TIGR03269 174 KQRVVLARQLA-KEPFLFLaDEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIKE--- 249
|
170
....*....|....
gi 446863618 230 EGehcTPELVKAVF 243
Cdd:TIGR03269 250 EG---TPDEVVAVF 260
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
40-206 |
7.71e-06 |
|
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: 46.93 E-value: 7.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 40 LVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKaLSRRLGILPQSPLLPEGLTVYE---LVSRGR-FPwqnfi 115
Cdd:TIGR01257 1970 LLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISD-VHQNMGYCPQFDAIDDLLTGREhlyLYARLRgVP----- 2043
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 116 rqwSDADEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDLRYQVEILELLHDLTRhH 195
Cdd:TIGR01257 2044 ---AEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIR-E 2119
|
170
....*....|.
gi 446863618 196 GRTVVVVLHDL 206
Cdd:TIGR01257 2120 GRAVVLTSHSM 2130
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
144-205 |
8.22e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.96 E-value: 8.22e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446863618 144 EKLSGGQRQ------RCWIAMVLAQ------KTPYILLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHD 205
Cdd:PRK02224 780 EQLSGGERAlfnlslRCAIYRLLAEgiegdaPLPPLILDEPTVFLDSGHVSQLVDLVESMRRLGVEQIVVVSHD 853
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
22-225 |
8.41e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.08 E-value: 8.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 22 KIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIarilqpMGGSILLDGKAIHEqptkalsRRLGILPQSPLLPEGlTVy 101
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSL------LSQFEISEGRVWAE-------RSIAYVPQQAWIMNA-TV- 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 102 elvsRGRfpwqnfIRQWSDADEQAVEEALKLTGTQ-EFAHLPV-------EK---LSGGQRQRCWIA-MVLAQKTPYiLL 169
Cdd:PTZ00243 738 ----RGN------ILFFDEEDAARLADAVRVSQLEaDLAQLGGgleteigEKgvnLSGGQKARVSLArAVYANRDVY-LL 806
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446863618 170 DEPTTWLDLRYQVEILELLHdLTRHHGRTVVVVLHDLNFaVNYGDTLIFLRQGKVV 225
Cdd:PTZ00243 807 DDPLSALDAHVGERVVEECF-LGALAGKTRVLATHQVHV-VPRADYVVALGDGRVE 860
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
28-66 |
9.15e-06 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 45.76 E-value: 9.15e-06
10 20 30
....*....|....*....|....*....|....*....
gi 446863618 28 VSFSVPtEKMTVLVGANGCGKSTLLSTIARILQPMGGSI 66
Cdd:COG3950 19 IDFDNP-PRLTVLVGENGSGKTTLLEAIALALSGLLSRL 56
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
37-225 |
1.39e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 46.38 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 37 MTVLVGANGCGKSTLLSTIARilQPMGGSILLDGKaIHEQPTK--ALSRRLGILPQSPLLPEGLTVYElvsrgRFPWQNF 114
Cdd:PLN03140 908 LTALMGVSGAGKTTLMDVLAG--RKTGGYIEGDIR-ISGFPKKqeTFARISGYCEQNDIHSPQVTVRE-----SLIYSAF 979
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 115 IRQWSDADEQA----VEEALKLTGTQEFAH----LP-VEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDLRYQVEIL 185
Cdd:PLN03140 980 LRLPKEVSKEEkmmfVDEVMELVELDNLKDaivgLPgVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVM 1059
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446863618 186 ELLHDlTRHHGRTVVVVLHDLNFAV--NYGDTLIFLRQGKVV 225
Cdd:PLN03140 1060 RTVRN-TVDTGRTVVCTIHQPSIDIfeAFDELLLMKRGGQVI 1100
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
19-224 |
2.70e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 45.27 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 19 YHKKIivDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRLGILPQSPL--LPE 96
Cdd:PRK13545 36 YHYAL--NNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTGIENIELkgLMM 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 97 GLTVYELvsrgrfpwqnfirqwsdadEQAVEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTWL 176
Cdd:PRK13545 114 GLTKEKI-------------------KEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVG 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446863618 177 DLRYQVEILELLHDLtRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKV 224
Cdd:PRK13545 175 DQTFTKKCLDKMNEF-KEQGKTIFFISHSLSQVKSFCTKALWLHYGQV 221
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
10-177 |
3.69e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 43.32 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 10 LILDNVSAGYHKKIIVDgVSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALS---RRLG 86
Cdd:PRK13541 2 LSLHQLQFNIEQKNLFD-LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTyigHNLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 87 ilpqsplLPEGLTVYElvsrgrfpwqnFIRQWSDADEQA--VEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKT 164
Cdd:PRK13541 81 -------LKLEMTVFE-----------NLKFWSEIYNSAetLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQS 142
|
170
....*....|...
gi 446863618 165 PYILLDEPTTWLD 177
Cdd:PRK13541 143 DLWLLDEVETNLS 155
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
145-225 |
7.22e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 43.25 E-value: 7.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 145 KLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKV 224
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQT 237
|
.
gi 446863618 225 V 225
Cdd:PRK15093 238 V 238
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
120-225 |
9.57e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.19 E-value: 9.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 120 DADEQAvEEALKLTGTQEFAHLPVEKLSGGQRQRCWIAMVLAQKTPYILLDEPTTWLDLRYQVEILELLHDLTRhHGRTV 199
Cdd:NF000106 120 DARARA-DELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVR-DGATV 197
|
90 100
....*....|....*....|....*.
gi 446863618 200 VVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:NF000106 198 LLTTQYMEEAEQLAHELTVIDRGRVI 223
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
146-206 |
1.01e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 43.52 E-value: 1.01e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446863618 146 LSGGQRQRCWIAMVLAQ----KTPYILlDEPTTWL---DLRyqvEILELLHDLtRHHGRTVVVVLHDL 206
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKrstgKTLYIL-DEPTTGLhfeDIR---KLLEVLHRL-VDKGNTVVVIEHNL 893
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
146-205 |
1.12e-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: 42.24 E-value: 1.12e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446863618 146 LSGGQRQRCWIAMVLAQKTPYIL--LDEPTTWLDLRYQVEILELLHDLtRHHGRTVVVVLHD 205
Cdd:cd03270 138 LSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHD 198
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
28-225 |
1.18e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 42.94 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 28 VSFSVPTEKMTVLVGANGCGKSTLLSTIARILQPMGGSILLDG-------KAIHEQPTKalsRRLGILPQ-SPLLPEgLT 99
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaeKGICLPPEK---RRIGYVFQdARLFPH-YK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 100 VyelvsRGrfpwqNFIRQWSDADEQAVEEALKLTGTQefaHL----PVeKLSGGQRQRCWIAMVLAQKTPYILLDEPTTW 175
Cdd:PRK11144 93 V-----RG-----NLRYGMAKSMVAQFDKIVALLGIE---PLldryPG-SLSGGEKQRVAIGRALLTAPELLLMDEPLAS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446863618 176 LDLRYQVEILELLHDLTRHHGRTVVVVLHDLNFAVNYGDTLIFLRQGKVV 225
Cdd:PRK11144 159 LDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVK 208
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
11-177 |
1.64e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.69 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 11 ILDNVSAGYHKKIIVDGVSFSVPTEKMTVLVGANGCGKSTLLSTIARIlQPMGGS---ILL-----DGKAIHEqptkaLS 82
Cdd:PRK10938 262 VLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGD-HPQGYSndlTLFgrrrgSGETIWD-----IK 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 83 RRLGILPQSPLLPE--GLTVYELVSRGRFPWQNFIRQWSDADEQAVEEALKLTG-TQEFAHLPVEKLSGGQRQRCWIAMV 159
Cdd:PRK10938 336 KHIGYVSSSLHLDYrvSTSVRNVILSGFFDSIGIYQAVSDRQQKLAQQWLDILGiDKRTADAPFHSLSWGQQRLALIVRA 415
|
170
....*....|....*...
gi 446863618 160 LAQKTPYILLDEPTTWLD 177
Cdd:PRK10938 416 LVKHPTLLILDEPLQGLD 433
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
21-60 |
1.83e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 42.23 E-value: 1.83e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 446863618 21 KKIIVDG----VSFSVPTEKMTVLVGANGCGKSTLLSTIaRILQ 60
Cdd:COG4637 3 TRIRIKNfkslRDLELPLGPLTVLIGANGSGKSNLLDAL-RFLS 45
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
146-206 |
2.13e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 42.32 E-value: 2.13e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446863618 146 LSGGQRQRCWIAMVLAQ----KTPYILlDEPTTWL---DLRyqvEILELLHDLtRHHGRTVVVVLHDL 206
Cdd:COG0178 827 LSGGEAQRVKLASELSKrstgKTLYIL-DEPTTGLhfhDIR---KLLEVLHRL-VDKGNTVVVIEHNL 889
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
38-66 |
2.93e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 41.29 E-value: 2.93e-04
10 20 30
....*....|....*....|....*....|.
gi 446863618 38 TVLVGANGCGKSTLLSTIARILQ--PMGGSI 66
Cdd:COG3910 40 TFFVGENGSGKSTLLEAIAVAAGfnPEGGSK 70
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
142-207 |
3.12e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.12 E-value: 3.12e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 142 PVEKLSGGQRQRCWIAMVL--AQKTP--YILlDEPTTWLDLRYQVEILELLHDLTrHHGRTVVVVLHDLN 207
Cdd:PRK00635 806 PLSSLSGGEIQRLKLAYELlaPSKKPtlYVL-DEPTTGLHTHDIKALIYVLQSLT-HQGHTVVIIEHNMH 873
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
40-90 |
5.66e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.03 E-value: 5.66e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 446863618 40 LVGANGCGKSTLLSTIARILQPMGGSILLDgkaiheqptkaLSRRLGILPQ 90
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEPSAGNVSLD-----------PNERLGKLRQ 71
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
35-61 |
6.03e-04 |
|
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: 40.76 E-value: 6.03e-04
10 20
....*....|....*....|....*..
gi 446863618 35 EKMTVLVGANGCGKSTLLSTIARILQP 61
Cdd:COG3593 23 DDLTVLVGENNSGKSSILEALRLLLGP 49
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
37-85 |
7.87e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 40.07 E-value: 7.87e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 446863618 37 MTVLVGANGCGKSTLLSTIARILQPMGGSILLDGKAIHEQPTKALSRRL 85
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTDERSRNGGIGGIPSLL 49
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
131-191 |
4.27e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 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: 213239 [Multi-domain] Cd Length: 243 Bit Score: 37.62 E-value: 4.27e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446863618 131 KLTGTQEFAHLPVEKLSGGQRQRCWIAMVLA-QKT---PYILLDEPTTWLDLRYQVEILELLHDL 191
Cdd:cd03272 144 SLTNMKQDEQQEMQQLSGGQKSLVALALIFAiQKCdpaPFYLFDEIDAALDAQYRTAVANMIKEL 208
|
|
| DEXSc_RecD-like |
cd17933 |
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ... |
35-87 |
5.48e-03 |
|
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350691 [Multi-domain] Cd Length: 155 Bit Score: 36.38 E-value: 5.48e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 446863618 35 EKMTVLVGANGCGKSTLLSTIARILQPMGGSILL---DGKAiheqpTKALSRRLGI 87
Cdd:cd17933 12 NRVSVLTGGAGTGKTTTLKALLAALEAEGKRVVLaapTGKA-----AKRLSESTGI 62
|
|
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
34-87 |
6.03e-03 |
|
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];
Pssm-ID: 440273 [Multi-domain] Cd Length: 514 Bit Score: 37.65 E-value: 6.03e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 446863618 34 TEKMTVLVGANGCGKSTLLSTIARILQPMGGSILL---DGKAiheqpTKALSRRLGI 87
Cdd:COG0507 139 TRRVSVLTGGAGTGKTTTLRALLAALEALGLRVALaapTGKA-----AKRLSESTGI 190
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
39-200 |
9.05e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 35.94 E-value: 9.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 39 VLVGANGCGKSTLLSTIARILQPMGGsILLDGKAIHEQPTKALSRrlgILPQSPLLPEGLTvyELVSRGRFPWQNFIrqw 118
Cdd:pfam13191 28 LLTGEAGTGKTTLLRELLRALERDGG-YFLRGKCDENLPYSPLLE---ALTREGLLRQLLD--ELESSLLEAWRAAL--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446863618 119 sdADEQAVEEALKLTGTQEFAHLPVEKLSGGQRqrcwiamvlAQKTPYILLDEpTTWLDLRYQvEILELLHDLTRHHGRT 198
Cdd:pfam13191 99 --LEALAPVPELPGDLAERLLDLLLRLLDLLAR---------GERPLVLVLDD-LQWADEASL-QLLAALLRLLESLPLL 165
|
..
gi 446863618 199 VV 200
Cdd:pfam13191 166 VV 167
|
|
| |
