|
Name |
Accession |
Description |
Interval |
E-value |
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-252 |
0e+00 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 509.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSIL 80
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 81 KQSNHISLRLTVRELVSFGRFPYSQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILLD 160
Cdd:COG4604 81 RQENHINSRLTVRELVAFGRFPYSKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 161 EPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENIIQSNVLRGIYDMDIEIE 240
Cdd:COG4604 161 EPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEVLSDIYDTDIEVE 240
|
250
....*....|..
gi 261284556 241 EINDNRVCVYYG 252
Cdd:COG4604 241 EIDGKRICVYFR 252
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-241 |
1.67e-106 |
|
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: 308.13 E-value: 1.67e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSIL 80
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 81 KQSNHISLRLTVRELVSFGRFPYSQ--GRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYIL 158
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGRYPHLGlfGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 159 LDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENIIQSNVLRGIYDMDIE 238
Cdd:COG1120 161 LDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVYGVEAR 240
|
...
gi 261284556 239 IEE 241
Cdd:COG1120 241 VIE 243
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-249 |
1.47e-81 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 244.92 E-value: 1.47e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSIL 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 81 KQSNHISLRLTVRELVSFGRFPYSQ--GRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYIL 158
Cdd:PRK11231 82 PQHHLTPEGITVRELVAYGRSPWLSlwGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 159 LDEPLNNLDMKHSVQIMKILRKLVTDlNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENIIQSNVLRGIYDMDIE 238
Cdd:PRK11231 162 LDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVFDVEAE 240
|
250
....*....|...
gi 261284556 239 I--EEINDNRVCV 249
Cdd:PRK11231 241 IhpEPVSGTPMCV 253
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-218 |
9.19e-73 |
|
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: 220.00 E-value: 9.19e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 3 QVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSILKQ 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 83 snhislrltvrelvsfgrfpysqgrlnaedekfvdeAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILLDEP 162
Cdd:cd03214 81 ------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 261284556 163 LNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEG 218
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-239 |
4.82e-66 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 205.39 E-value: 4.82e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSIL 80
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 81 KQSNHISLRLTVRELVSFGRFPYSQGRlnAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTE----- 155
Cdd:PRK13548 82 PQHSSLSFPFTVEEVVAMGRAPHGLSR--AEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQLWEpdgpp 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 156 -YILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENIIQSNVLRGIYD 234
Cdd:PRK13548 160 rWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPETLRRVYG 239
|
....*
gi 261284556 235 MDIEI 239
Cdd:PRK13548 240 ADVLV 244
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-239 |
8.00e-66 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 204.96 E-value: 8.00e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSIL 80
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 81 KQSNHISLRLTVRELVSFGRFPYSQGRlnAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTE----- 155
Cdd:COG4559 81 PQHSSLAFPFTVEEVVALGRAPHGSSA--AQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQLWEpvdgg 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 156 --YILLDEPLNNLDMKHSVQIMKILRKLvTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENIIQSNVLRGIY 233
Cdd:COG4559 159 prWLFLDEPTSALDLAHQHAVLRLARQL-ARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELLERVY 237
|
....*.
gi 261284556 234 DMDIEI 239
Cdd:COG4559 238 GADLRV 243
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-239 |
1.85e-63 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 198.39 E-value: 1.85e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKsgdlaKKVSIL 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRAR-----RRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 81 KQSNHI--SLRLTVRELVSFGRFPYS--QGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEY 156
Cdd:COG1121 81 PQRAEVdwDFPITVRDVVLMGRYGRRglFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 157 ILLDEPLNNLDMKHSVQIMKILRKLVtDLNKTIVIVIHDINFASFYSDYIVALKDGAIeSEGKTENIIQSNVLRGIYDMD 236
Cdd:COG1121 161 LLLDEPFAGVDAATEEALYELLRELR-REGKTILVVTHDLGAVREYFDRVLLLNRGLV-AHGPPEEVLTPENLSRAYGGP 238
|
...
gi 261284556 237 IEI 239
Cdd:COG1121 239 VAL 241
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
3-233 |
1.87e-63 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 199.24 E-value: 1.87e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 3 QVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSILKQ 82
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 83 SNHISLRLTVRELVSFGRFPY--SQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILLD 160
Cdd:PRK10575 93 QLPAAEGMTVRELVAIGRYPWhgALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLD 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 261284556 161 EPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENIIQSNVLRGIY 233
Cdd:PRK10575 173 EPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIY 245
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-238 |
1.24e-59 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 188.73 E-value: 1.24e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVY-GGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAK---K 76
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRlrrR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 77 VSILKQSNHISLRLTVRELVSFGRFPYSQ------GRLNAEDekfVDEAISYME---LEDMQHKYLHQLSGGQTQRAFIA 147
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVLAGRLGRTStwrsllGLFPPED---RERALEALErvgLADKAYQRADQLSGGQQQRVAIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 148 MVIAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENiIQSN 227
Cdd:COG3638 159 RALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAE-LTDA 237
|
250
....*....|.
gi 261284556 228 VLRGIYDMDIE 238
Cdd:COG3638 238 VLREIYGGEAE 248
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
11-235 |
9.98e-58 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 184.42 E-value: 9.98e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 11 YGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSILKQSNHISLRL 90
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 91 TVRELVSFGRFPYSQ--GRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILLDEPLNNLDM 168
Cdd:PRK10253 97 TVQELVARGRYPHQPlfTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 261284556 169 KHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENIIQSNVLRGIYDM 235
Cdd:PRK10253 177 SHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYGL 243
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-224 |
2.39e-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: 2.39e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVY-GGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSIL 80
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 81 KQ-SNHISLRLTVRELVSFGrfPYSQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILL 159
Cdd:COG1122 81 FQnPDDQLFAPTVEEDVAFG--PENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 261284556 160 DEPLNNLDMKHSVQIMKILRKLvTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENII 224
Cdd:COG1122 159 DEPTAGLDPRGRRELLELLKRL-NKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVF 222
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-214 |
5.41e-57 |
|
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: 181.15 E-value: 5.41e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKK----VVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLA--- 74
Cdd:cd03255 1 IELKNLSKTYGGGGekvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 75 -KKVSILKQSNHISLRLTVRELVSFGRFPysQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQN 153
Cdd:cd03255 81 rRHIGFVFQSFNLLPDLTALENVELPLLL--AGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 261284556 154 TEYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASfYSDYIVALKDGAI 214
Cdd:cd03255 159 PKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-210 |
6.30e-57 |
|
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: 180.81 E-value: 6.30e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 3 QVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKsgdlaKKVSILKQ 82
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER-----KRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 83 SNHI--SLRLTVRELVSFGRFPYS--QGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYIL 158
Cdd:cd03235 76 RRSIdrDFPISVRDVVLMGLYGHKglFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 261284556 159 LDEPLNNLDMKHSVQIMKILRKLvTDLNKTIVIVIHDINFASFYSDYIVALK 210
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLREL-RREGMTILVVTHDLGLVLEYFDRVLLLN 206
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-226 |
5.26e-56 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 179.10 E-value: 5.26e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQwKSGDLAKKVSILK 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 82 QSNHISLRLTVRELVSF-GRFpysQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILLD 160
Cdd:COG1131 80 QEPALYPDLTVRENLRFfARL---YGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 261284556 161 EPLNNLDMKHSVQIMKILRKLVTDlNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENIIQS 226
Cdd:COG1131 157 EPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-239 |
7.75e-56 |
|
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: 178.90 E-value: 7.75e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLaKKVSIL 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREAR-RQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 81 KQSNHISLRLTVRE-LVSFGRFpysQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILL 159
Cdd:COG4555 80 PDERGLYDRLTVREnIRYFAEL---YGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 160 DEPLNNLDMKHSVQIMKILRKLvTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENIIQSNVLRGIYDMDIEI 239
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEENLEDAFVAL 235
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-212 |
2.00e-55 |
|
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: 176.89 E-value: 2.00e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 3 QVTNVSKVYGG--KKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSIL 80
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 81 KQ-SNHISLRLTVRELVSFGrfPYSQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILL 159
Cdd:cd03225 81 FQnPDDQFFGPTVEEEVAFG--LENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 261284556 160 DEPLNNLDMKHSVQIMKILRKLvTDLNKTIVIVIHDINFASFYSDYIVALKDG 212
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKL-KAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-233 |
2.09e-55 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 177.76 E-value: 2.09e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYG-GKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLA---KKV 77
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRqlrRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 78 SILKQSNHISLRLTVRELVSFGRFPY-----SQGRLNAEDEKfvDEAISYME---LEDMQHKYLHQLSGGQTQRAFIAMV 149
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRLGRrstwrSLFGLFPKEEK--QRALAALErvgLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 150 IAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENiIQSNVL 229
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAE-LTDEVL 237
|
....
gi 261284556 230 RGIY 233
Cdd:cd03256 238 DEIY 241
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-234 |
2.29e-53 |
|
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: 172.48 E-value: 2.29e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYG-GKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDL----AK 75
Cdd:TIGR02315 1 MLEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLrklrRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 76 KVSILKQSNHISlRLTVRELVSFGRFPYSQ------GRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMV 149
Cdd:TIGR02315 81 IGMIFQHYNLIE-RLTVLENVLHGRLGYKPtwrsllGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 150 IAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENIIQsNVL 229
Cdd:TIGR02315 160 LAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDD-EVL 238
|
....*
gi 261284556 230 RGIYD 234
Cdd:TIGR02315 239 RHIYG 243
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-217 |
9.11e-53 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 170.61 E-value: 9.11e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKK----VVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAK- 75
Cdd:COG1136 4 LLELRNLTKSYGTGEgevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 76 ---KVSILKQSNHISLRLTVRELVSFGRFPysQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQ 152
Cdd:COG1136 84 rrrHIGFVFQFFNLLPELTALENVALPLLL--AGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 261284556 153 NTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASfYSDYIVALKDGAIESE 217
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAA-RADRVIRLRDGRIVSD 225
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-223 |
2.07e-52 |
|
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: 170.37 E-value: 2.07e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYG----GKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKK 76
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 77 VSILKQSNHISL--RLTVRELVSFgrfPY-SQGRLNAEDEkfVDEAISYMEL-EDMQHKYLHQLSGGQTQRAFIAMVIAQ 152
Cdd:COG1124 81 VQMVFQDPYASLhpRHTVDRILAE---PLrIHGLPDREER--IAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 261284556 153 NTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENI 223
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADL 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-226 |
9.93e-51 |
|
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: 172.78 E-value: 9.93e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVY-----GGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGD--- 72
Cdd:COG1123 260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlre 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 73 LAKKVSILKQSNHISL--RLTVRELVSFGrfPYSQGRLNAED-EKFVDEAISYMEL-EDMQHKYLHQLSGGQTQRAFIAM 148
Cdd:COG1123 340 LRRRVQMVFQDPYSSLnpRMTVGDIIAEP--LRLHGLLSRAErRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIAR 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 261284556 149 VIAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENIIQS 226
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-234 |
6.39e-50 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 168.48 E-value: 6.39e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSIL 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 81 KQSNHISLRLTVRELVSFGRFPYSQ--GRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYIL 158
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVEMGRTPHRSrfDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 261284556 159 LDEPLNNLDMKHSVQIMKILRKLVTDlNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENIIQSNVLRGIYD 234
Cdd:PRK09536 163 LDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFD 237
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-218 |
1.35e-49 |
|
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: 161.92 E-value: 1.35e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDlaKKVSILK 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER--RNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 82 QSN----HislrLTVRELVSFGrfPYSQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYI 157
Cdd:cd03259 79 QDYalfpH----LTVAENIAFG--LKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 261284556 158 LLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEG 218
Cdd:cd03259 153 LLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-218 |
5.78e-48 |
|
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: 158.44 E-value: 5.78e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGK----KVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLA-- 74
Cdd:cd03257 1 LLEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 75 -KKVSILKQSNHISL--RLTVRELVsfgRFPY-SQGRLNAEDEKfvdEAISYMEL------EDMQHKYLHQLSGGQTQRA 144
Cdd:cd03257 81 rKEIQMVFQDPMSSLnpRMTIGEQI---AEPLrIHGKLSKKEAR---KEAVLLLLvgvglpEEVLNRYPHELSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 261284556 145 FIAMVIAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEG 218
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-226 |
8.57e-48 |
|
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: 158.23 E-value: 8.57e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVY-GGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSIL 80
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 81 KQSnhISL--RLTVRELVsfGRFPYSQGRLNAEDEKFVDEAISYMELEDMQ--HKYLHQLSGGQTQRAFIAMVIAQNTEY 156
Cdd:cd03295 81 IQQ--IGLfpHMTVEENI--ALVPKLLKWPKEKIRERADELLALVGLDPAEfaDRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 157 ILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENIIQS 226
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-226 |
4.94e-47 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 156.12 E-value: 4.94e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDL---AKKVS 78
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrlRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 79 ILKQSNHISLRLTVRELVSFgrfPYSQ-GRLNAED-EKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEY 156
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAF---PLREhTRLSEEEiREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPEL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 157 ILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENIIQS 226
Cdd:cd03261 158 LLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRAS 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-226 |
7.19e-47 |
|
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: 162.77 E-value: 7.19e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVY--GGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRL---TGKDSGLITVDGKEVSQWKSGDLAK 75
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 76 KVSILKQSNHISL-RLTVRELVSFGrfPYSQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNT 154
Cdd:COG1123 84 RIGMVFQDPMTQLnPVTVGDQIAEA--LENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 261284556 155 EYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENIIQS 226
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-209 |
3.27e-46 |
|
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: 153.40 E-value: 3.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGK----KVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQwksgdLAKKV 77
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 78 SILKQSNHISLRLTVRELVSFGrfPYSQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYI 157
Cdd:cd03293 76 GYVFQQDALLPWLTVLDNVALG--LELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 261284556 158 LLDEPLNNLD--MKHSVQ--IMKILRKlvtdLNKTIVIVIHDINFASFYSDYIVAL 209
Cdd:cd03293 154 LLDEPFSALDalTREQLQeeLLDIWRE----TGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-212 |
6.59e-46 |
|
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: 151.19 E-value: 6.59e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQ--WKSGDLAKKVSI 79
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDleDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 80 LKQSNHISLRLTVRELVSFGrfpysqgrlnaedekfvdeaisymeledmqhkylhqLSGGQTQRAFIAMVIAQNTEYILL 159
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG------------------------------------LSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 261284556 160 DEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDG 212
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-212 |
4.20e-45 |
|
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: 149.08 E-value: 4.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQwKSGDLAKKVSILK 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 82 QSNHISLRLTVRELVsfgrfpysqgrlnaedekfvdeaisymeledmqhkylhQLSGGQTQRAFIAMVIAQNTEYILLDE 161
Cdd:cd03230 80 EEPSLYENLTVRENL--------------------------------------KLSGGMKQRLALAQALLHDPELLILDE 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 261284556 162 PLNNLDMKHSVQIMKILRKLVTDlNKTIVIVIHDINFASFYSDYIVALKDG 212
Cdd:cd03230 122 PTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNG 171
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-223 |
1.24e-44 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 153.33 E-value: 1.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDlaKKVSIL 80
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK--RNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 81 KQS----NHislrLTVRELVSFG----RFPysqgrlNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQ 152
Cdd:COG3842 83 FQDyalfPH----LTVAENVAFGlrmrGVP------KAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 261284556 153 NTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENI 223
Cdd:COG3842 153 EPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-227 |
2.25e-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: 2.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLA---KKV 77
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelrRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 78 SILKQSNhiSL--RLTVRELVSFG-RFpysQGRLNAED-EKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQN 153
Cdd:COG1127 85 GMLFQGG--ALfdSLTVFENVAFPlRE---HTDLSEAEiRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 261284556 154 TEYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENIIQSN 227
Cdd:COG1127 160 PEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD 233
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
11-200 |
1.34e-43 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 145.84 E-value: 1.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 11 YGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGkevsqwksgdlAKKVSILKQSNHI--SL 88
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRSEVpdSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 89 RLTVRELVSFGRFPY--SQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILLDEPLNNL 166
Cdd:NF040873 71 PLTVRDLVAMGRWARrgLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190
....*....|....*....|....*....|....
gi 261284556 167 DMKHSVQIMKILRKLVTDlNKTIVIVIHDINFAS 200
Cdd:NF040873 151 DAESRERIIALLAEEHAR-GATVVVVTHDLELVR 183
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-212 |
1.84e-43 |
|
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: 144.31 E-value: 1.84e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 3 QVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSilkq 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIG---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 83 snhislrltvrelvsfgrfpysqgrlnaedekfvdeaisymeledmqhkYLHQLSGGQTQRAFIAMVIAQNTEYILLDEP 162
Cdd:cd00267 77 -------------------------------------------------YVPQLSGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 261284556 163 LNNLDMKHSVQIMKILRKLVtDLNKTIVIVIHDINFASFYSDYIVALKDG 212
Cdd:cd00267 108 TSGLDPASRERLLELLRELA-EEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-212 |
2.37e-42 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 144.85 E-value: 2.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVY----GGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQwksgdLAKK 76
Cdd:COG1116 7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----PGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 77 VSILKQSNhislRL----TVRELVSFG-RFpysQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIA 151
Cdd:COG1116 82 RGVVFQEP----ALlpwlTVLDNVALGlEL---RGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 261284556 152 QNTEYILLDEPLNNLD--MKHSVQimKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDG 212
Cdd:COG1116 155 NDPEVLLMDEPFGALDalTRERLQ--DELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-219 |
1.18e-41 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 141.73 E-value: 1.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVY-GGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAK---K 76
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYlrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 77 VSILKQSNHISLRLTVRELVSFG-RFpysQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTE 155
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPlRV---TGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 261284556 156 YILLDEPLNNLDMKHSVQIMKILRKLvTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGK 219
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEI-NRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEA 220
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-223 |
1.65e-41 |
|
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: 141.61 E-value: 1.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQ---WKsgdlaKKVS 78
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlppHK-----RPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 79 ILKQSNHISLRLTVRELVSFG-RFpysQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYI 157
Cdd:cd03300 76 TVFQNYALFPHLTVFENIAFGlRL---KKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 261284556 158 LLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENI 223
Cdd:cd03300 153 LLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-223 |
6.38e-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: 140.26 E-value: 6.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKK----- 76
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgigrt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 77 ---VSILKqsnhislRLTVRELV------------SFGRFPYSQGRLNAEdekfVDEAISYMELEDMQHKYLHQLSGGQT 141
Cdd:cd03219 81 fqiPRLFP-------ELTVLENVmvaaqartgsglLLARARREEREARER----AEELLERVGLADLADRPAGELSYGQQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 142 QRAFIAMVIAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVtDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTE 221
Cdd:cd03219 150 RRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELR-ERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPD 228
|
..
gi 261284556 222 NI 223
Cdd:cd03219 229 EV 230
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-223 |
6.86e-41 |
|
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: 140.94 E-value: 6.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKK---- 76
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLgiar 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 77 ----VSILKqsnhislRLTVRE--------------LVSFGRFPYSQGRLNAEDEKfVDEAISYMELEDMQHKYLHQLSG 138
Cdd:COG0411 84 tfqnPRLFP-------ELTVLEnvlvaaharlgrglLAALLRLPRARREEREARER-AEELLERVGLADRADEPAGNLSY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 139 GQTQRAFIAMVIAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEG 218
Cdd:COG0411 156 GQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEG 235
|
....*
gi 261284556 219 KTENI 223
Cdd:COG0411 236 TPAEV 240
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-227 |
6.90e-41 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 140.28 E-value: 6.90e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVvdNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDlaKKVSIL 80
Cdd:COG3840 1 MLRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--RPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 81 KQSNHISLRLTVRELVSFGRFPysQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILLD 160
Cdd:COG3840 77 FQENNLFPHLTVAQNIGLGLRP--GLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 261284556 161 EPLNNLD--MKHsvQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENIIQSN 227
Cdd:COG3840 155 EPFSALDpaLRQ--EMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGE 221
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-218 |
1.05e-40 |
|
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: 139.31 E-value: 1.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDlaKKVSILK 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 82 QSNHISLRLTVRELVSFGRfpYSQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILLDE 161
Cdd:cd03301 79 QNYALYPHMTVYDNIAFGL--KLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 261284556 162 PLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEG 218
Cdd:cd03301 157 PLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-243 |
1.69e-40 |
|
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: 139.83 E-value: 1.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGL-ITVDGKEVSQWKSGDLAKKVSI 79
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 80 LKQSNH--ISLRLTVRELV------SFGRFPysqgRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIA 151
Cdd:COG1119 83 VSPALQlrFPRDETVLDVVlsgffdSIGLYR----EPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 152 QNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDIN--FASFysDYIVALKDGAIESEGKTENIIQSNVL 229
Cdd:COG1119 159 KDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEeiPPGI--THVLLLKDGRVVAAGPKEEVLTSENL 236
|
250
....*....|....
gi 261284556 230 RGIYDMDIEIEEIN 243
Cdd:COG1119 237 SEAFGLPVEVERRD 250
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-223 |
6.96e-40 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 138.74 E-value: 6.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGG-----KKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQ---WKSGDL 73
Cdd:TIGR04521 1 IKLKNVSYIYQPgtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAkkkKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 74 AKKVSILKQ-SNHISLRLTVRELVSFGrfPYSQGRLNAEDEKFVDEAISYMEL-EDMQHKYLHQLSGGQTQRAFIAMVIA 151
Cdd:TIGR04521 81 RKKVGLVFQfPEHQLFEETVYKDIAFG--PKNLGLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGVLA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 261284556 152 QNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENI 223
Cdd:TIGR04521 159 MEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREV 230
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-223 |
7.68e-40 |
|
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: 137.86 E-value: 7.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDlaKKVSILK 81
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 82 QsnHISL--RLTVRELVSFG-RF-PYSQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYI 157
Cdd:cd03296 81 Q--HYALfrHMTVFDNVAFGlRVkPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 261284556 158 LLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENI 223
Cdd:cd03296 159 LLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-223 |
1.07e-39 |
|
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: 136.93 E-value: 1.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTG-----KDSGLITVDGKEVSQWKSGDLA-- 74
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDVLElr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 75 KKVSILKQSNHIsLRLTVRELVSFGrfPYSQG-RLNAEDEKFVDEAISYMELEDMQHKYLH--QLSGGQTQRAFIAMVIA 151
Cdd:cd03260 81 RRVGMVFQKPNP-FPGSIYDNVAYG--LRLHGiKLKEELDERVEEALRKAALWDEVKDRLHalGLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 261284556 152 QNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLnkTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENI 223
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-223 |
1.71e-39 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 139.82 E-value: 1.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDlaKKVSIL 80
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD--RNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 81 KQS----NHislrLTVRELVSFG----RFPysqgrlNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQ 152
Cdd:COG3839 81 FQSyalyPH----MTVYENIAFPlklrKVP------KAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 261284556 153 NTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENI 223
Cdd:COG3839 151 EPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-223 |
6.62e-39 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 137.97 E-value: 6.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKS-GDlaKKVSIL 80
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPpRE--RRVGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 81 KQsnHISL--RLTVRELVSFGrfPYSQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYIL 158
Cdd:COG1118 81 FQ--HYALfpHMTVAENIAFG--LRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 261284556 159 LDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENI 223
Cdd:COG1118 157 LDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-223 |
6.73e-39 |
|
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: 134.80 E-value: 6.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQwKSGDLAKKVSILK 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 82 QSNHISLRLTVRE-LVSFGRFpysQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILLD 160
Cdd:cd03265 80 QDLSVDDELTGWEnLYIHARL---YGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 261284556 161 EPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENI 223
Cdd:cd03265 157 EPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-224 |
2.20e-38 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 133.97 E-value: 2.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQwKSGDLAK---KV 77
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD-SKKDINKlrrKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 78 SILKQS----NHislrLTVRELVSFGrfP-YSQGRLNAEDEKfvdEAISYME---LEDMQHKYLHQLSGGQTQRAFIAMV 149
Cdd:COG1126 80 GMVFQQfnlfPH----LTVLENVTLA--PiKVKKMSKAEAEE---RAMELLErvgLADKADAYPAQLSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 261284556 150 IAQNTEYILLDEPLNNLD--MKHSV-QIMKILRKlvtdLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENII 224
Cdd:COG1126 151 LAMEPKVMLFDEPTSALDpeLVGEVlDVMRDLAK----EGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFF 224
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-214 |
2.68e-38 |
|
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: 133.04 E-value: 2.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSG--DLAKKVSI 79
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 80 LKQSNHISLRLTVRELVSFGrfP-YSQGRLNAEDEKfvdEAISYME---LEDMQHKYLHQLSGGQTQRAFIAMVIAQNTE 155
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLA--PiKVKGMSKAEAEE---RALELLEkvgLADKADAYPAQLSGGQQQRVAIARALAMNPK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 261284556 156 YILLDEPLNNLD--MKHSVqiMKILRKLVTDlNKTIVIVIHDINFASFYSDYIVALKDGAI 214
Cdd:cd03262 156 VMLFDEPTSALDpeLVGEV--LDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-164 |
2.76e-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: 130.85 E-value: 2.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 17 VDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSILKQSNHISLRLTVRELV 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 261284556 97 SFGRfpYSQGRLNAEDEKFVDEAISYMELEDM----QHKYLHQLSGGQTQRAFIAMVIAQNTEYILLDEPLN 164
Cdd:pfam00005 81 RLGL--LLKGLSKREKDARAEEALEKLGLGDLadrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-212 |
3.67e-38 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 132.63 E-value: 3.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGG--KKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSgDLAKKVSI 79
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRK-AARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 80 LKQSNHISLRLTVRELVSF-GRFpysQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYIL 158
Cdd:cd03263 80 CPQFDALFDELTVREHLRFyARL---KGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 261284556 159 LDEPLNNLDMKHSVQIMKILRKLVTdlNKTIVIVIHDINFASFYSDYIVALKDG 212
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDG 208
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
17-246 |
1.26e-37 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 132.27 E-value: 1.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 17 VDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKdSGLITVDGKEVSQWKSGDLAKKVSILKQSNHISLRLTVRELV 96
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLSDWSAAELARHRAYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 97 SFGrfpYSQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQ-----NTE--YILLDEPLNNLDMK 169
Cdd:COG4138 91 ALH---QPAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptiNPEgqLLLLDEPMNSLDVA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 261284556 170 HSVQIMKILRKLvTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENIIQSNVLRGIYDMDIEIEEINDNR 246
Cdd:COG4138 168 QQAALDRLLREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVFGVKFRRLEVEGHR 243
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-224 |
1.32e-37 |
|
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: 131.55 E-value: 1.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGK----KVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKK 76
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 77 VS----ILKQSNHISLRlTVRELVSFgrfPYSQGRL-NAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIA 151
Cdd:cd03258 81 RRrigmIFQHFNLLSSR-TVFENVAL---PLEIAGVpKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 261284556 152 QNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENII 224
Cdd:cd03258 157 NNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVF 229
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-225 |
1.95e-37 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 133.29 E-value: 1.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVY-GGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQwksgdlakkvsi 79
Cdd:COG1125 1 MIEFENVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRD------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 80 lkqSNHISLR---------------LTVRE---LVsfgrfPYSQGRLNAEDEKFVDEAISYMEL--EDMQHKYLHQLSGG 139
Cdd:COG1125 69 ---LDPVELRrrigyviqqiglfphMTVAEniaTV-----PRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 140 QTQRAFIAMVIAQNTEYILLDEPLNNLD--MKHSVQimKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESE 217
Cdd:COG1125 141 QQQRVGVARALAADPPILLMDEPFGALDpiTREQLQ--DELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQY 218
|
....*...
gi 261284556 218 GKTENIIQ 225
Cdd:COG1125 219 DTPEEILA 226
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-218 |
2.33e-37 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 134.69 E-value: 2.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDlaKKVSILK 81
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN--RHVNTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 82 QSNHISLRLTVRELVSFG-RFpysQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILLD 160
Cdd:PRK09452 93 QSYALFPHMTVFENVAFGlRM---QKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 261284556 161 EPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEG 218
Cdd:PRK09452 170 ESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDG 227
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-230 |
2.89e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 132.17 E-value: 2.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVY-GGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSIL 80
Cdd:PRK13647 5 IEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 81 KQSNHISL-RLTVRELVSFGrfPYSQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILL 159
Cdd:PRK13647 85 FQDPDDQVfSSTVWDDVAFG--PVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 261284556 160 DEPLNNLDMKHSVQIMKILRKLvTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKT-----ENIIQSNVLR 230
Cdd:PRK13647 163 DEPMAYLDPRGQETLMEILDRL-HNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKslltdEDIVEQAGLR 237
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-173 |
4.20e-37 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 129.52 E-value: 4.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSgDLAKKVSIL 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARE-DYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 81 KQSNHISLRLTVRELVSFgrfpYSQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILLD 160
Cdd:COG4133 81 GHADGLKPELTVRENLRF----WAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLD 156
|
170
....*....|...
gi 261284556 161 EPLNNLDmKHSVQ 173
Cdd:COG4133 157 EPFTALD-AAGVA 168
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-218 |
1.93e-36 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 128.08 E-value: 1.93e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKKVVDNVSVTIPKGqITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGdLAKKVSILK 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-LRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 82 QSNHISLRLTVRELVSFgrFPYSQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILLDE 161
Cdd:cd03264 79 QEFGVYPNFTVREFLDY--IAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 261284556 162 PLNNLDMKHSVQimkiLRKLVTDL--NKTIVIVIHDINFASFYSDYIVALKDGAIESEG 218
Cdd:cd03264 157 PTAGLDPEERIR----FRNLLSELgeDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-218 |
7.12e-36 |
|
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: 126.56 E-value: 7.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGdlAKKVSILK 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA--LRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 82 QSNHISLRLTVRELVSFGrfpysqGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILLDE 161
Cdd:cd03268 79 EAPGFYPNLTARENLRLL------ARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 162 PLNNLDMKHsvqiMKILRKLVTDLNK---TIVIVIHDINFASFYSDYIVALKDGAIESEG 218
Cdd:cd03268 153 PTNGLDPDG----IKELRELILSLRDqgiTVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-227 |
2.98e-35 |
|
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: 131.80 E-value: 2.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVY-GGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSIL 80
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 81 KQSNHIsLRLTVRELVSFGRfPysqgrlNAEDEKfVDEAI--SYME--LEDMQHKYLHQ-------LSGGQTQRAFIAMV 149
Cdd:COG4988 417 PQNPYL-FAGTIRENLRLGR-P------DASDEE-LEAALeaAGLDefVAALPDGLDTPlgeggrgLSGGQAQRLALARA 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 261284556 150 IAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDlnKTIVIVIHDINFASFYsDYIVALKDGAIESEGKTENIIQSN 227
Cdd:COG4988 488 LLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKG--RTVILITHRLALLAQA-DRILVLDDGRIVEQGTHEELLAKN 562
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
11-214 |
3.58e-35 |
|
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: 124.68 E-value: 3.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 11 YGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWksgDLAKKVSILKQ-SNHISLR 89
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK---ERRKSIGYVMQdVDYQLFT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 90 LTVRELVSFGRFPYSQGRLNAEdekfvdEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILLDEPLNNLDMK 169
Cdd:cd03226 87 DSVREELLLGLKELDAGNEQAE------TVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 261284556 170 HSVQIMKILRKLVTDlNKTIVIVIHDINFASFYSDYIVALKDGAI 214
Cdd:cd03226 161 NMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-231 |
5.17e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 126.35 E-value: 5.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVY-GGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLA--KKV 77
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEvrKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 78 SILKQSNHISLRL-TVRELVSFGrfPYSQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEY 156
Cdd:PRK13639 81 GIVFQNPDDQLFApTVEEDVAFG--PLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 261284556 157 ILLDEPLNNLDMKHSVQIMKILRklvtDLNK---TIVIVIHDINFASFYSDYIVALKDGAIESEGKTENII-QSNVLRG 231
Cdd:PRK13639 159 IVLDEPTSGLDPMGASQIMKLLY----DLNKegiTIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFsDIETIRK 233
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-218 |
8.80e-35 |
|
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: 124.02 E-value: 8.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKK----VVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSgDLAKK 76
Cdd:cd03266 1 MITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPA-EARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 77 VSILKQSNHISLRLTVRE-LVSFGRFpYSQGRLNAEDEkfVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTE 155
Cdd:cd03266 80 LGFVSDSTGLYDRLTAREnLEYFAGL-YGLKGDELTAR--LEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 261284556 156 YILLDEPLNNLDMKHSVQIMKILRKLvTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEG 218
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
13-246 |
1.38e-34 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 124.94 E-value: 1.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 13 GKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMIS-RLTGKD-------SGLITVDGKEVSQWKSGDLAKKVSILKQSN 84
Cdd:PRK13547 13 HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 85 HISLRLTVRELVSFGRFPYSQ--GRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQ---------N 153
Cdd:PRK13547 93 QPAFAFSAREIVLLGRYPHARraGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaqP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 154 TEYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENIIQSNVLRGIY 233
Cdd:PRK13547 173 PRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLTPAHIARCY 252
|
250
....*....|...
gi 261284556 234 DMDIEIEEINDNR 246
Cdd:PRK13547 253 GFAVRLVDAGDGV 265
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-197 |
1.39e-34 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 126.73 E-value: 1.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKK----VVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLA-- 74
Cdd:COG1135 1 MIELENLSKTFPTKGgpvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRaa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 75 -KKVS-ILKQSNHISLRlTVRELVSfgrFP-YSQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIA 151
Cdd:COG1135 81 rRKIGmIFQHFNLLSSR-TVAENVA---LPlEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 261284556 152 QNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDIN 197
Cdd:COG1135 157 NNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMD 202
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-212 |
1.52e-34 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 123.13 E-value: 1.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVY-GGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAK---K 76
Cdd:TIGR02673 1 MIEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLlrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 77 VSILKQSNHISLRLTVRELVSFgrfPYS-QGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTE 155
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVAL---PLEvRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 261284556 156 YILLDEPLNNLDMKHSVQIMKILRKLvTDLNKTIVIVIHDINFASFYSDYIVALKDG 212
Cdd:TIGR02673 158 LLLADEPTGNLDPDLSERILDLLKRL-NKRGTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-214 |
1.61e-34 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 123.00 E-value: 1.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSILK 81
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 82 QSNHIsLRLTVRELVsfgRFPYsQGRLNAEDEKFVDEAISYMEL-EDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILLD 160
Cdd:COG4619 81 QEPAL-WGGTVRDNL---PFPF-QLRERKFDRERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 261284556 161 EPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAI 214
Cdd:COG4619 156 EPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-223 |
6.29e-34 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 125.20 E-value: 6.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDlaKKVSILK 81
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 82 QsnHISL--RLTVRELVSFG--RFPYSQgRLN-AEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEY 156
Cdd:PRK10851 81 Q--HYALfrHMTVFDNIAFGltVLPRRE-RPNaAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 261284556 157 ILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENI 223
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-214 |
1.14e-33 |
|
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: 120.98 E-value: 1.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVY-GGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAK---KV 77
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYlrrKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 78 SILKQSNHISLRLTVRELVSFG-RFPYSQGRlnaEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEY 156
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFAlEVTGVPPR---EIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 261284556 157 ILLDEPLNNLDMKHSVQIMKILRKlVTDLNKTIVIVIHDINFASFYSDYIVALKDGAI 214
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKK-INKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
2-226 |
4.12e-33 |
|
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: 121.21 E-value: 4.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKK------------------------VVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGL 57
Cdd:cd03294 1 IKIKGLYKIFGKNPqkafkllakgkskeeilkktgqtvGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 58 ITVDGKEVSQWKSGDL----AKKVSILKQSNHISLRLTVRELVSFGRfpYSQGRLNAEDEKFVDEAISYMELEDMQHKYL 133
Cdd:cd03294 81 VLIDGQDIAAMSRKELrelrRKKISMVFQSFALLPHRTVLENVAFGL--EVQGVPRAEREERAAEALELVGLEGWEHKYP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 134 HQLSGGQTQRAFIAMVIAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGA 213
Cdd:cd03294 159 DELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGR 238
|
250
....*....|...
gi 261284556 214 IESEGKTENIIQS 226
Cdd:cd03294 239 LVQVGTPEEILTN 251
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
19-218 |
7.30e-33 |
|
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: 118.94 E-value: 7.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 19 NVSVTIPkGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKE-VSQWKSGDLA---KKVSILKQSNHISLRLTVRE 94
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlFDSRKKINLPpqqRKIGLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 95 LVSFGrfpySQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILLDEPLNNLDMKHSVQI 174
Cdd:cd03297 95 NLAFG----LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 261284556 175 MKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEG 218
Cdd:cd03297 171 LPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-225 |
8.41e-33 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 119.43 E-value: 8.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGD--LAKKVS 78
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 79 ILKQSNHISLRLTVRELVSFGrfP-YSQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYI 157
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFG--PlRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 158 LLDEPLNNLD--MKHSVqiMKILRKLVTDlNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENIIQ 225
Cdd:PRK09493 159 LFDEPTSALDpeLRHEV--LKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIK 225
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-223 |
4.86e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 119.06 E-value: 4.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQwksgdlakkvsil 80
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 81 KQSNHISL---------RLTVRE-LVSFGRF---PYSQGRLNAED--EKFvdeaisymELEDMQHKYLHQLSGGQTQRA- 144
Cdd:COG4152 68 EDRRRIGYlpeerglypKMKVGEqLVYLARLkglSKAEAKRRADEwlERL--------GLGDRANKKVEELSKGNQQKVq 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 145 FIAMVIAqNTEYILLDEPLNNLDmKHSVQIMK-ILRKLvTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENI 223
Cdd:COG4152 140 LIAALLH-DPELLILDEPFSGLD-PVNVELLKdVIREL-AAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-227 |
6.49e-32 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 118.19 E-value: 6.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGG--KKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSI 79
Cdd:PRK13635 6 IRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 80 LKQS--NHIsLRLTVRELVSFGRfpYSQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYI 157
Cdd:PRK13635 86 VFQNpdNQF-VGATVQDDVAFGL--ENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDII 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 158 LLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFySDYIVALKDGAIESEGKTENIIQSN 227
Cdd:PRK13635 163 ILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKSG 231
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-212 |
9.26e-32 |
|
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: 114.79 E-value: 9.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGG--KKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSI 79
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 80 LKQSNHIsLRLTVRELVsfgrfpysqgrlnaedekfvdeaisymeledmqhkylhqLSGGQTQRAFIAMVIAQNTEYILL 159
Cdd:cd03228 81 VPQDPFL-FSGTIRENI---------------------------------------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 261284556 160 DEPLNNLDMKHSVQIMKILRKLvtDLNKTIVIVIHDINFASFYsDYIVALKDG 212
Cdd:cd03228 121 DEATSALDPETEALILEALRAL--AKGKTVIVIAHRLSTIRDA-DRIIVLDDG 170
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
21-218 |
1.37e-31 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 115.67 E-value: 1.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 21 SVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDlaKKVSILKQSNHISLRLTVRELVSFGR 100
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSMLFQENNLFAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 101 FPysQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILLDEPLNNLDMKHSVQIMKILRK 180
Cdd:cd03298 96 SP--GLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLD 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 261284556 181 LVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEG 218
Cdd:cd03298 174 LHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-223 |
2.11e-31 |
|
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: 115.22 E-value: 2.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKK-VSIL 80
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 81 KQSNHISLRLTVRELVSFGRFPysqgRLNAEDEKFVDEAISYM-ELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILL 159
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYA----RRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 261284556 160 DEPLNNLDMKHSVQIMKILRKLvTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENI 223
Cdd:cd03224 157 DEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-232 |
5.73e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 115.72 E-value: 5.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYG-GKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSG--DLAKKV 77
Cdd:PRK13636 5 ILKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGlmKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 78 SILKQS-NHISLRLTVRELVSFGrfPYSQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEY 156
Cdd:PRK13636 85 GMVFQDpDNQLFSASVYQDVSFG--AVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 261284556 157 ILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGK-TENIIQSNVLRGI 232
Cdd:PRK13636 163 LVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNpKEVFAEKEMLRKV 239
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-221 |
7.89e-31 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 115.37 E-value: 7.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVY-GGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLakkVSIL 80
Cdd:PRK15056 7 IVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 81 KQSNHI--SLRLTVRELVSFGRFPYSQ--GRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEY 156
Cdd:PRK15056 84 PQSEEVdwSFPVLVEDVVMMGRYGHMGwlRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 261284556 157 ILLDEPLNNLDMKHSVQIMKILRKLvTDLNKTIVIVIHDINFASFYSDYIVALKdGAIESEGKTE 221
Cdd:PRK15056 164 ILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDYTVMVK-GTVLASGPTE 226
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-233 |
1.11e-30 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 113.79 E-value: 1.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKK-VSIL 80
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 81 KQSNHISLRLTVRE-LVSFGRFpysQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILL 159
Cdd:cd03218 81 PQEASIFRKLTVEEnILAVLEI---RGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 261284556 160 DEPLNNLDMKhSVQ-IMKILRKLVtdlNKTIVIVIHDIN----FASFYSDYIvaLKDGAIESEGKTENIIQSNVLRGIY 233
Cdd:cd03218 158 DEPFAGVDPI-AVQdIQKIIKILK---DRGIGVLITDHNvretLSITDRAYI--IYEGKVLAEGTPEEIAANELVRKVY 230
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
2-246 |
1.55e-30 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 113.87 E-value: 1.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSkvyggkkvVDN----VSVTIPKGQITSFIGPNGAGKSTLLSMISRLTgKDSGLITVDGKEVSQWKSGDLAKKV 77
Cdd:PRK03695 1 MQLNDVA--------VSTrlgpLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 78 SILKQSNHISLRLTVrelvsfgrFPY-----SQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQ 152
Cdd:PRK03695 72 AYLSQQQTPPFAMPV--------FQYltlhqPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 153 -------NTEYILLDEPLNNLDMKHSVQIMKILRKLvTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENIIQ 225
Cdd:PRK03695 144 vwpdinpAGQLLLLDEPMNSLDVAQQAALDRLLSEL-CQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLT 222
|
250 260
....*....|....*....|.
gi 261284556 226 SNVLRGIYDMDIEIEEINDNR 246
Cdd:PRK03695 223 PENLAQVFGVNFRRLDVEGHP 243
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-223 |
1.56e-30 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 114.13 E-value: 1.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSIL 80
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDGELVPADR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 81 KQSNHISLRL-------------TVRELVSFGrfP-YSQGRLNAEdekFVDEAISYME---LEDMQHKYLHQLSGGQTQR 143
Cdd:COG4598 88 RQLQRIRTRLgmvfqsfnlwshmTVLENVIEA--PvHVLGRPKAE---AIERAEALLAkvgLADKRDAYPAHLSGGQQQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 144 AFIAMVIAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDlNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENI 223
Cdd:COG4598 163 AAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEV 241
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
6-214 |
5.27e-30 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 114.82 E-value: 5.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 6 NVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSqwKSGDLAKKVSILKQSNH 85
Cdd:PRK11432 11 NITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT--HRSIQQRDICMVFQSYA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 86 ISLRLTVRELVSFGRfpYSQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILLDEPLNN 165
Cdd:PRK11432 89 LFPHMSLGENVGYGL--KMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 261284556 166 LDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAI 214
Cdd:PRK11432 167 LDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKI 215
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-228 |
5.43e-30 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 114.54 E-value: 5.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEV-SQWKSGdlAKKVSIL 80
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVpARARLA--RARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 81 KQSNHISLRLTVRE-LVSFGRFpysqGRLNAED-EKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYIL 158
Cdd:PRK13536 120 PQFDNLDLEFTVREnLLVFGRY----FGMSTREiEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLI 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 159 LDEPLNNLDMKHSVQIMKILRKLVTdLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENIIQSNV 228
Cdd:PRK13536 196 LDEPTTGLDPHARHLIWERLRSLLA-RGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHI 264
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-227 |
1.01e-29 |
|
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: 116.40 E-value: 1.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVY--GGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSI 79
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 80 LKQSNHIsLRLTVRE--LVsfgrfpysqGRLNAEDEKFVdEAISYMELEDM---QHKYLH--------QLSGGQTQRAFI 146
Cdd:COG4987 414 VPQRPHL-FDTTLREnlRL---------ARPDATDEELW-AALERVGLGDWlaaLPDGLDtwlgeggrRLSGGERRRLAL 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 147 AMVIAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDlnKTIVIVIHDINFASfYSDYIVALKDGAIESEGKTENIIQS 226
Cdd:COG4987 483 ARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAG--RTVLLITHRLAGLE-RMDRILVLEDGRIVEQGTHEELLAQ 559
|
.
gi 261284556 227 N 227
Cdd:COG4987 560 N 560
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
21-220 |
1.15e-29 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 110.72 E-value: 1.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 21 SVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSqwKSGDLAKKVSILKQSNHISLRLTVRELVSFGR 100
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHT--GLAPYQRPVSMLFQENNLFAHLTVRQNIGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 101 FPysQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILLDEPLNNLDMKHSVQIMKILRK 180
Cdd:TIGR01277 96 HP--GLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQ 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 261284556 181 LVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKT 220
Cdd:TIGR01277 174 LCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSDC 213
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-194 |
1.43e-29 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 113.36 E-value: 1.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKK----VVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAK- 75
Cdd:PRK11153 1 MIELKNISKVFPQGGrtihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 76 --KVSILKQS-NHISLRlTVRELVSfgrFPYS-QGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIA 151
Cdd:PRK11153 81 rrQIGMIFQHfNLLSSR-TVFDNVA---LPLElAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 261284556 152 QNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIH 194
Cdd:PRK11153 157 SNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITH 199
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-233 |
2.67e-29 |
|
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: 115.70 E-value: 2.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGG--KKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSI 79
Cdd:COG2274 474 IELENVSFRYPGdsPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 80 LKQSNHIsLRLTVRELVSFgrfpysqGRLNAEDEKfVDEAISYMELED----MQHKYLHQ-------LSGGQTQRAFIAM 148
Cdd:COG2274 554 VLQDVFL-FSGTIRENITL-------GDPDATDEE-IIEAARLAGLHDfieaLPMGYDTVvgeggsnLSGGQRQRLAIAR 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 149 VIAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTdlNKTIVIVIHDINFASfYSDYIVALKDGAIESEGKTENIIQsnv 228
Cdd:COG2274 625 ALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIR-LADRIIVLDKGRIVEDGTHEELLA--- 698
|
....*
gi 261284556 229 LRGIY 233
Cdd:COG2274 699 RKGLY 703
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-207 |
3.01e-29 |
|
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: 112.07 E-value: 3.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGK----KVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRL---TGKDSGLITVDGKEVSQWKSGDL 73
Cdd:COG0444 1 LLEVRNLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLlppPGITSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 74 ----AKKVSILKQSNHISL--RLTVRElvSFGRFPYSQGRLNAEDEKfvDEAISYMEL------EDMQHKYLHQLSGGQT 141
Cdd:COG0444 81 rkirGREIQMIFQDPMTSLnpVMTVGD--QIAEPLRIHGGLSKAEAR--ERAIELLERvglpdpERRLDRYPHELSGGMR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 261284556 142 QRAFIAMVIAQNTEYILLDEPLNNLDMkhSVQ--IMKILRKLVTDLNKTIVIVIHDINFASFYSDYIV 207
Cdd:COG0444 157 QRVMIARALALEPKLLIADEPTTALDV--TIQaqILNLLKDLQRELGLAILFITHDLGVVAEIADRVA 222
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-212 |
8.73e-29 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 109.40 E-value: 8.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVsqwkSGDLAKKVSIL 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV----EGPGAERGVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 81 KQSNHISLRlTVRELVSFGRFPYSQGRlnAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILLD 160
Cdd:PRK11248 77 QNEGLLPWR-NVQDNVAFGLQLAGVEK--MQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 261284556 161 EPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDG 212
Cdd:PRK11248 154 EPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-212 |
1.07e-28 |
|
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: 107.75 E-value: 1.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGD--------- 72
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRigylpeerg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 73 LAKKVSILKQsnhislrltvreLVSFGRFpysQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRA-FIAMVIa 151
Cdd:cd03269 81 LYPKMKVIDQ------------LVYLAQL---KGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVqFIAAVI- 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 261284556 152 QNTEYILLDEPLNNLDMKHSVQIMKILRKLvTDLNKTIVIVIHDINFASFYSDYIVALKDG 212
Cdd:cd03269 145 HDPELLILDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKG 204
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-201 |
1.15e-28 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 109.18 E-value: 1.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKK----VVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQwKSGDLAkk 76
Cdd:COG4525 3 MLTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGADRG-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 77 vsILKQsNHISLR-LTVRELVSFG-RFpysQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNT 154
Cdd:COG4525 80 --VVFQ-KDALLPwLNVLDNVAFGlRL---RGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADP 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 261284556 155 EYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASF 201
Cdd:COG4525 154 RFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALF 200
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-223 |
1.57e-28 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 111.08 E-value: 1.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSgdLAKKVSIL 80
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP--YQRPINMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 81 KQSNHISLRLTVRELVSFGrfpYSQGRL-NAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILL 159
Cdd:PRK11607 97 FQSYALFPHMTVEQNIAFG---LKQDKLpKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 261284556 160 DEPLNNLDMK----HSVQIMKILRKlvtdLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENI 223
Cdd:PRK11607 174 DEPMGALDKKlrdrMQLEVVDILER----VGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-226 |
2.57e-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: 107.42 E-value: 2.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKKVvDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDlaKKVSILK 81
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK--RDISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 82 QSNHISLRLTVRELVSFGRfpYSQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILLDE 161
Cdd:cd03299 78 QNYALFPHMTVYKNIAYGL--KKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 261284556 162 PLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENIIQS 226
Cdd:cd03299 156 PFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-223 |
4.33e-28 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 107.75 E-value: 4.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSILK 81
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLKVADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 82 QSNHISLRLTV-----------RELVSFGRFPYSQGRLNAEDEKfvDEAISYMEL----EDMQHKYLHQLSGGQTQRAFI 146
Cdd:PRK10619 86 QLRLLRTRLTMvfqhfnlwshmTVLENVMEAPIQVLGLSKQEAR--ERAVKYLAKvgidERAQGKYPVHLSGGQQQRVSI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 261284556 147 AMVIAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDlNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENI 223
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-212 |
5.34e-28 |
|
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: 106.78 E-value: 5.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 17 VDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLakkvsILKQSNHISLRLTVRELV 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPWLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 97 SFGRFPYSQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILLDEPLNNLDMKHSVQIMK 176
Cdd:TIGR01184 76 ALAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQE 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 261284556 177 ILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDG 212
Cdd:TIGR01184 156 ELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-227 |
8.83e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 106.35 E-value: 8.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMIsrlTGK---DSGLITVDGKEVSQWKSGDLAK-- 75
Cdd:COG4674 10 ILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVI---TGKtrpDSGSVLFGGTDLTGLDEHEIARlg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 76 ------KVSILKQsnhislrLTVRE--LVSFGR----FPYSQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQR 143
Cdd:COG4674 87 igrkfqKPTVFEE-------LTVFEnlELALKGdrgvFASLFARLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 144 AFIAMVIAQNTEYILLDEP---LNNLDMKHSVQIMKILRKlvtdlNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKT 220
Cdd:COG4674 160 LEIGMLLAQDPKLLLLDEPvagMTDAETERTAELLKSLAG-----KHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGSL 234
|
....*..
gi 261284556 221 ENiIQSN 227
Cdd:COG4674 235 DE-VQAD 240
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-229 |
9.21e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 107.19 E-value: 9.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVY--GGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDS---GLITVDGKEVSQWKSGDLAKK 76
Cdd:PRK13640 6 VEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 77 VSILKQS-NHISLRLTVRELVSFGRfpYSQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTE 155
Cdd:PRK13640 86 VGIVFQNpDNQFVGATVGDDVAFGL--ENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPK 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 261284556 156 YILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASfYSDYIVALKDGAIESEGKTENIIQSNVL 229
Cdd:PRK13640 164 IIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPVEIFSKVEM 236
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
3-230 |
9.90e-28 |
|
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: 106.07 E-value: 9.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 3 QVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKK-VSILK 81
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAgIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 82 QSNHISLRLTVRE--LVSFGRFPysqgrlnAEDEKFVDEAISYME-LEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYIL 158
Cdd:TIGR03410 82 QGREIFPRLTVEEnlLTGLAALP-------RRSRKIPDEIYELFPvLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 261284556 159 LDEPLNNLdmKHSV--QIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENIIQSNVLR 230
Cdd:TIGR03410 155 LDEPTEGI--QPSIikDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDKVRR 226
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-223 |
1.37e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 106.15 E-value: 1.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLT-----GKDSGLITVDGKEVSQWKSGDLAKK 76
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIFKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 77 VSILKQSNHISLRLTVRELVSFG----RFPYSQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQ 152
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALGlklnRLVKSKKELQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAF 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 261284556 153 NTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLnkTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENI 223
Cdd:PRK14247 164 QPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-214 |
1.47e-27 |
|
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: 103.66 E-value: 1.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDlAKKVSIlk 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD-ARRAGI-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 82 qsnhislrltvrELVsfgrfpysqgrlnaedekfvdeaisymeledmqhkylHQLSGGQTQRAFIAMVIAQNTEYILLDE 161
Cdd:cd03216 78 ------------AMV-------------------------------------YQLSVGERQMVEIARALARNARLLILDE 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 261284556 162 PLNNLDMKHSVQIMKILRKLvTDLNKTIVIVIHDINFASFYSDYIVALKDGAI 214
Cdd:cd03216 109 PTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-233 |
2.05e-27 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 109.87 E-value: 2.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVY-GGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSIL 80
Cdd:COG1132 340 IEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 81 KQSNHIsLRLTVRELVSFgrfpysqGRLNAEDEKfVDEAISYMELED----MQHKYLHQ-------LSGGQTQRAFIAMV 149
Cdd:COG1132 420 PQDTFL-FSGTIRENIRY-------GRPDATDEE-VEEAAKAAQAHEfieaLPDGYDTVvgergvnLSGGQRQRIAIARA 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 150 IAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDlnKTIVIVIHD---INFAsfysDYIVALKDGAIESEGKTENIIQS 226
Cdd:COG1132 491 LLKDPPILILDEATSALDTETEALIQEALERLMKG--RTTIVIAHRlstIRNA----DRILVLDDGRIVEQGTHEELLAR 564
|
....*..
gi 261284556 227 NvlrGIY 233
Cdd:COG1132 565 G---GLY 568
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-225 |
3.49e-27 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 104.71 E-value: 3.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDG------KEVSQWKSGDLAK 75
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 76 KVSILKQSNHISLRLTVRE-LVSFgrfPYSQGRLNAEDEKF-VDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQN 153
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMEnLIEA---PCKVLGLSKEQAREkAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 261284556 154 TEYILLDEPLNNLDMKHSVQIMKILRKLvTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENIIQ 225
Cdd:COG4161 160 PQVLLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDASHFTQ 230
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-209 |
3.91e-27 |
|
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: 108.91 E-value: 3.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGK-KVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSIL 80
Cdd:TIGR02857 322 LEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 81 KQSNHIsLRLTVRELVSFGRfpysqgrlNAEDEKFVDEAISYM-------ELEDMQHKYL----HQLSGGQTQRAFIAMV 149
Cdd:TIGR02857 402 PQHPFL-FAGTIAENIRLAR--------PDASDAEIREALERAgldefvaALPQGLDTPIgeggAGLSGGQAQRLALARA 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 150 IAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTdlNKTIVIVIHDINFASFYsDYIVAL 209
Cdd:TIGR02857 473 FLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALA-DRIVVL 529
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-233 |
5.09e-27 |
|
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: 104.29 E-value: 5.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKK-VSI 79
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 80 LKQSNHISLRLTVRELVSFGRFPYSQGRLNAEDekfVDEAISYM-ELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYIL 158
Cdd:COG0410 83 VPEGRRIFPSLTVEENLLLGAYARRDRAEVRAD---LERVYELFpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 159 LDEPlnnldmkhS-------V-QIMKILRKLVtDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENIIQSNVLR 230
Cdd:COG0410 160 LDEP--------SlglapliVeEIFEIIRRLN-REGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEVR 230
|
...
gi 261284556 231 GIY 233
Cdd:COG0410 231 EAY 233
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
33-223 |
5.69e-27 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 106.04 E-value: 5.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 33 IGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDlaKKVSILKQSNHISLRLTVRELVSFGRfpYSQGRLNAED 112
Cdd:TIGR01187 2 LGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHL--RHINMVFQSYALFPHMTVEENVAFGL--KMRKVPRAEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 113 EKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIV 192
Cdd:TIGR01187 78 KPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFV 157
|
170 180 190
....*....|....*....|....*....|.
gi 261284556 193 IHDINFASFYSDYIVALKDGAIESEGKTENI 223
Cdd:TIGR01187 158 THDQEEAMTMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-235 |
8.54e-27 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 103.46 E-value: 8.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKK--VVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSI 79
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 80 LKQSNHIsLRLTVRELVSFGRFpysqgrlNAEDEKFVDEA-ISY-----MELEDMQHKYLH----QLSGGQTQRAFIAMV 149
Cdd:cd03251 81 VSQDVFL-FNDTVAENIAYGRP-------GATREEVEEAArAANahefiMELPEGYDTVIGergvKLSGGQRQRIAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 150 IAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTdlNKTIVIVIH---DINFAsfysDYIVALKDGAIESEGKTENIIQS 226
Cdd:cd03251 153 LLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHrlsTIENA----DRIVVLEDGKIVERGTHEELLAQ 226
|
....*....
gi 261284556 227 NvlrGIYDM 235
Cdd:cd03251 227 G---GVYAK 232
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-221 |
1.59e-26 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 103.55 E-value: 1.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGL---ITVDGKEVSqwKSGDLAKKV 77
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAgshIELLGRTVQ--REGRLARDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 78 S--------ILKQSNHISlRLTVRELV---SFGRFPYSQGRL---NAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQR 143
Cdd:PRK09984 82 RksrantgyIFQQFNLVN-RLSVLENVligALGSTPFWRTCFswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 261284556 144 AFIAMVIAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTE 221
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQ 238
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
14-194 |
1.89e-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: 102.35 E-value: 1.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 14 KKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRL---TGKDSGLITVDGKEVS--QWKsgdlaKKVSILKQSNHISL 88
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRvegGGTTSGQILFNGQPRKpdQFQ-----KCVAYVRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 89 RLTVRELVSF-----GRFPYSQGRLNAEDEkfvDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILLDEPL 163
Cdd:cd03234 95 GLTVRETLTYtailrLPRKSSDAIRKKRVE---DVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190
....*....|....*....|....*....|.
gi 261284556 164 NNLDMKHSVQIMKILRKLVTDlNKTIVIVIH 194
Cdd:cd03234 172 SGLDSFTALNLVSTLSQLARR-NRIVILTIH 201
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-215 |
2.39e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 106.69 E-value: 2.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVdGKEVsqwksgdlakKVSIL 80
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------KIGYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 81 KQsNHISLR--LTVRELVsfgrfpySQGRLNAEDEkfvdEAISYMEL----EDMQHKYLHQLSGGQTQRAFIAMVIAQNT 154
Cdd:COG0488 384 DQ-HQEELDpdKTVLDEL-------RDGAPGGTEQ----EVRGYLGRflfsGDDAFKPVGVLSGGEKARLALAKLLLSPP 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 261284556 155 EYILLDEPLNNLDMkHSVQimkILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIE 215
Cdd:COG0488 452 NVLLLDEPTNHLDI-ETLE---ALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-219 |
2.95e-26 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 104.73 E-value: 2.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVT--NVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGK---EVSQWKSGdlak 75
Cdd:PRK11000 1 MASVTlrNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmnDVPPAERG---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 76 kVSILKQSNHISLRLTVRELVSFGRFPYSQGRlnAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTE 155
Cdd:PRK11000 77 -VGMVFQSYALYPHLSVAENMSFGLKLAGAKK--EEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 261284556 156 YILLDEPLNNLDMKHSVQiMKI-LRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGK 219
Cdd:PRK11000 154 VFLLDEPLSNLDAALRVQ-MRIeISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGK 217
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-218 |
9.61e-26 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 100.86 E-value: 9.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITV-----DGKEVSQWKSG-DLAK 75
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagnhfDFSKTPSDKAIrELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 76 KVSILKQSNHISLRLTVRE-LVsfgRFPYS-QGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQN 153
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQnLI---EAPCRvLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 261284556 154 TEYILLDEPLNNLDMKHSVQIMKILRKLvTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEG 218
Cdd:PRK11124 160 PQVLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-230 |
1.36e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 101.42 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVY-GGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSI 79
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 80 LKQ-SNHISLRLTVRELVSFGrfPYSQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYIL 158
Cdd:PRK13652 83 VFQnPDDQIFSPTVEQDIAFG--PINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 261284556 159 LDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENI-IQSNVLR 230
Cdd:PRK13652 161 LDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIfLQPDLLA 233
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-223 |
1.46e-25 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 100.88 E-value: 1.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTgkD-------SGLITVDGKEVsqwksgdLA 74
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMN--DlipgarvEGEILLDGEDI-------YD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 75 KKVSIlkqsnhISLR--------------LTVRELVSFGrfPYSQGRLNAE--DEKfVDEAIS----YMELEDMQHKYLH 134
Cdd:COG1117 83 PDVDV------VELRrrvgmvfqkpnpfpKSIYDNVAYG--LRLHGIKSKSelDEI-VEESLRkaalWDEVKDRLKKSAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 135 QLSGGQTQRAFIAMVIAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLnkTIVIVIHDINFASFYSDYIVALKDGAI 214
Cdd:COG1117 154 GLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLGEL 231
|
....*....
gi 261284556 215 ESEGKTENI 223
Cdd:COG1117 232 VEFGPTEQI 240
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
19-225 |
1.48e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 101.64 E-value: 1.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 19 NVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSG----DLAKKVSILKQ-SNHISLRLTVR 93
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNkklkPLRKKVGIVFQfPEHQLFEETVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 94 ELVSFGrfPYSQGRLNAEDEKFVDEAISYMEL-EDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILLDEPLNNLDMKHSV 172
Cdd:PRK13634 105 KDICFG--PMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRK 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 261284556 173 QIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENIIQ 225
Cdd:PRK13634 183 EMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFA 235
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-233 |
1.87e-25 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 100.00 E-value: 1.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYG-GKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSIL 80
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 81 KQsNHISLRLTVRELVSFgrfpysqGRLNAEDEKFVDEAISYM---ELEDMQHKYLHQ-------LSGGQTQRAFIAMVI 150
Cdd:cd03253 81 PQ-DTVLFNDTIGYNIRY-------GRPDATDEEVIEAAKAAQihdKIMRFPDGYDTIvgerglkLSGGEKQRVAIARAI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 151 AQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTdlNKTIVIVIHDINFASfYSDYIVALKDGAIESEGKTENIIQSNvlr 230
Cdd:cd03253 153 LKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIV-NADKIIVLKDGRIVERGTHEELLAKG--- 226
|
...
gi 261284556 231 GIY 233
Cdd:cd03253 227 GLY 229
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-243 |
1.99e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 100.84 E-value: 1.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGG--KKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVS 78
Cdd:PRK13632 7 MIKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 79 ILKQS--NHIsLRLTVRELVSFG----RFPYSqgrlnaEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQ 152
Cdd:PRK13632 87 IIFQNpdNQF-IGATVEDDIAFGlenkKVPPK------KMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 153 NTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFAsFYSDYIVALKDGAIESEGKTENIIQS-NVLRG 231
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEILNNkEILEK 238
|
250
....*....|....*....
gi 261284556 232 -------IYDMDIEIEEIN 243
Cdd:PRK13632 239 akidspfIYKLSKKLKGID 257
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
2-196 |
2.34e-25 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 99.71 E-value: 2.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVY------GG---------------KKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITV 60
Cdd:cd03267 1 IEVSNLSKSYrvyskePGligslkslfkrkyreVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 61 DGKEVSQWKSGDLAKKVSILKQSNHISLRLTVRELVSFGRFPYsqgrlNAEDEKF---VDEAISYMELEDMQHKYLHQLS 137
Cdd:cd03267 81 AGLVPWKRRKKFLRRIGVVFGQKTQLWWDLPVIDSFYLLAAIY-----DLPPARFkkrLDELSELLDLEELLDTPVRQLS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 261284556 138 GGQTQRAFIAMVIAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDI 196
Cdd:cd03267 156 LGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYM 214
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-227 |
2.56e-25 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 99.61 E-value: 2.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKK-VVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSIL 80
Cdd:cd03254 3 IEFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 81 KQSNHIsLRLTVRELVSFgrfpysqGRLNAEDEKFV--------DEAIsyMELEDMQHKYL----HQLSGGQTQRAFIAM 148
Cdd:cd03254 83 LQDTFL-FSGTIMENIRL-------GRPNATDEEVIeaakeagaHDFI--MKLPNGYDTVLgengGNLSQGERQLLAIAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 261284556 149 VIAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTdlNKTIVIVIHDINFASFySDYIVALKDGAIESEGKTENIIQSN 227
Cdd:cd03254 153 AMLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLAKK 228
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-233 |
2.81e-25 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 99.72 E-value: 2.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQW------KSGdla 74
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLpmhkraRLG--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 75 kkVSILKQSNHISLRLTVR-------ELVSFGRfpysqgrlnAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIA 147
Cdd:COG1137 80 --IGYLPQEASIFRKLTVEdnilavlELRKLSK---------KEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 148 MVIAQNTEYILLDEPLNNLDMKhSVQ-IMKILRKLVtdlNKTIVIVIHD---------INFAsfysdYIvaLKDGAIESE 217
Cdd:COG1137 149 RALATNPKFILLDEPFAGVDPI-AVAdIQKIIRHLK---ERGIGVLITDhnvretlgiCDRA-----YI--ISEGKVLAE 217
|
250
....*....|....*.
gi 261284556 218 GKTENIIQSNVLRGIY 233
Cdd:COG1137 218 GTPEEILNNPLVRKVY 233
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-195 |
4.49e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 103.22 E-value: 4.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 4 VTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMIsrltgkdSGLITVDGKEVsqWKSGDLakKVSILKQS 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKIL-------AGELEPDSGEV--SIPKGL--RIGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 84 NHISLRLTVRELVSFGRFPYSQ--GRLNAEDEKFVDEAISYMELEDMQHKY----------------------------- 132
Cdd:COG0488 70 PPLDDDLTVLDTVLDGDAELRAleAELEELEAKLAEPDEDLERLAELQEEFealggweaearaeeilsglgfpeedldrp 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 261284556 133 LHQLSGGQTQRAFIAMVIAQNTEYILLDEPLNNLDMkHSVQimkILRKLVTDLNKTIVIVIHD 195
Cdd:COG0488 150 VSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL-ESIE---WLEEFLKNYPGTVLVVSHD 208
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-228 |
6.57e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 100.26 E-value: 6.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQwKSGDLAKKVSILK 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 82 QSNHISLRLTVRE-LVSFGRFpysQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILLD 160
Cdd:PRK13537 87 QFDNLDPDFTVREnLLVFGRY---FGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 261284556 161 EPLNNLDMKHSVQIMKILRKLVTDlNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENIIQSNV 228
Cdd:PRK13537 164 EPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEI 230
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-223 |
6.79e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 99.08 E-value: 6.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKD-----SGLITVDGKEVSQWKSG--DL 73
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIYSPRTDtvDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 74 AKKVS-ILKQSNhiSLRLTVRELVSFGRfpysqgRLNAEDEKFV-DEAIS--------YMELEDMQHKYLHQLSGGQTQR 143
Cdd:PRK14239 85 RKEIGmVFQQPN--PFPMSIYENVVYGL------RLKGIKDKQVlDEAVEkslkgasiWDEVKDRLHDSALGLSGGQQQR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 144 AFIAMVIAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLnkTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENI 223
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-234 |
9.11e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 99.09 E-value: 9.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRL-----TGKDSGLITVDGKEV--SQWKSGDLA 74
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndlipGFRVEGKVTFHGKNLyaPDVDPVEVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 75 KKVSILKQSNHiSLRLTVRELVSFG-RFPYSQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQN 153
Cdd:PRK14243 91 RRIGMVFQKPN-PFPKSIYDNIAYGaRINGYKGDMDELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 154 TEYILLDEPLNNLDMKHSVQIMKILRKLVTDLnkTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENIIQSNVLRGIY 233
Cdd:PRK14243 170 PEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTAFFNVELTEGGGRYGYLVEFDRTEKIF 247
|
.
gi 261284556 234 D 234
Cdd:PRK14243 248 N 248
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1-220 |
1.15e-24 |
|
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: 98.72 E-value: 1.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVY---------GGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSG 71
Cdd:TIGR02769 2 LLEVRDVTHTYrtgglfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 72 D---LAKKVSILKQSNHISL--RLTVRELVsfgRFPYSQ-GRLN-AEDEKFVDEAISYMEL--EDMQhKYLHQLSGGQTQ 142
Cdd:TIGR02769 82 QrraFRRDVQLVFQDSPSAVnpRMTVRQII---GEPLRHlTSLDeSEQKARIAELLDMVGLrsEDAD-KLPRQLSGGQLQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 261284556 143 RAFIAMVIAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKT 220
Cdd:TIGR02769 158 RINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDV 235
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-226 |
1.81e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 98.28 E-value: 1.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKK--VVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVS 78
Cdd:PRK13648 7 IIVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 79 ILKQS-NHISLRLTVRELVSFG----RFPYSqgrlnaEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQN 153
Cdd:PRK13648 87 IVFQNpDNQFVGSIVKYDVAFGlenhAVPYD------EMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 261284556 154 TEYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFAsFYSDYIVALKDGAIESEGKTENIIQS 226
Cdd:PRK13648 161 PSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEA-MEADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
6-233 |
2.32e-24 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 97.27 E-value: 2.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 6 NVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKK-VSILKQSN 84
Cdd:PRK10895 8 NLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgIGYLPQEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 85 HISLRLTVRELVsfgrFPYSQGRLNAEDEKFVDEAISYME---LEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILLDE 161
Cdd:PRK10895 88 SIFRRLSVYDNL----MAVLQIRDDLSAEQREDRANELMEefhIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 261284556 162 PLNNLDMKHSVQIMKILRKLvTDLNKTIVIVIHDI--NFASFYSDYIVAlkDGAIESEGKTENIIQSNVLRGIY 233
Cdd:PRK10895 164 PFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVreTLAVCERAYIVS--QGHLIAHGTPTEILQDEHVKRVY 234
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
20-229 |
2.63e-24 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 99.42 E-value: 2.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 20 VSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEV-SQWKSGDLA---KKVSILKQSNHISLRLTVREL 95
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfDSRKGIFLPpekRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 96 VSFGRfpysqGRLNAEDEKFVDEAISYM-ELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILLDEPLNNLDMKHSVQI 174
Cdd:TIGR02142 96 LRYGM-----KRARPSERRISFERVIELlGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEI 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 261284556 175 MKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENIIQSNVL 229
Cdd:TIGR02142 171 LPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDL 225
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-214 |
3.24e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 97.46 E-value: 3.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYG-G----KKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSgdlak 75
Cdd:COG1101 1 MLELKNLSKTFNpGtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPE----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 76 kvsiLKQSNHISL-----------RLTVRE--LVSFGR---FPYSQGRLNAEDEKFVDE-AISYMELEDMQHKYLHQLSG 138
Cdd:COG1101 76 ----YKRAKYIGRvfqdpmmgtapSMTIEEnlALAYRRgkrRGLRRGLTKKRRELFRELlATLGLGLENRLDTKVGLLSG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 261284556 139 GQTQRAFIAMVIAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAI 214
Cdd:COG1101 152 GQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-227 |
4.12e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 97.85 E-value: 4.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGK-----KVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKK 76
Cdd:PRK13651 3 IKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 77 VSI-----------LKQSNHISLRL--------------TVRELVSFGrfPYSQGRLNAEDEKfvdEAISYMELEDMQHK 131
Cdd:PRK13651 83 VLEklviqktrfkkIKKIKEIRRRVgvvfqfaeyqlfeqTIEKDIIFG--PVSMGVSKEEAKK---RAAKYIELVGLDES 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 132 YLHQ----LSGGQTQRAFIAMVIAQNTEYILLDEPLNNLDMKHSVQIMKILRKLvTDLNKTIVIVIHDINFASFYSDYIV 207
Cdd:PRK13651 158 YLQRspfeLSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNL-NKQGKTIILVTHDLDNVLEWTKRTI 236
|
250 260
....*....|....*....|
gi 261284556 208 ALKDGAIESEGKTENIIQSN 227
Cdd:PRK13651 237 FFKDGKIIKDGDTYDILSDN 256
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
9-226 |
4.22e-24 |
|
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: 100.14 E-value: 4.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 9 KVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTgKDSGLITVDGKEVSQWKSGDLA---KKVSILKQSNH 85
Cdd:COG4172 294 RTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRALRplrRRMQVVFQDPF 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 86 ISL--RLTVRELVSFG---RFPysqgRLNAED-EKFVDEAISYMEL-EDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYIL 158
Cdd:COG4172 373 GSLspRMTVGQIIAEGlrvHGP----GLSAAErRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLV 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 159 LDEPLNNLDMkhSVQ--IMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENIIQS 226
Cdd:COG4172 449 LDEPTSALDV--SVQaqILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
12-212 |
4.96e-24 |
|
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: 95.31 E-value: 4.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 12 GGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMIS--RLTGKDSGLITVDGKEVSQWKsgdLAKKVSILKQSNHISLR 89
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLDKRS---FRKIIGYVPQDDILHPT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 90 LTVRELVSFgrfpysqgrlNAEdekfvdeaisymeledmqhkyLHQLSGGQTQRAFIAMVIAQNTEYILLDEPLNNLDMK 169
Cdd:cd03213 97 LTVRETLMF----------AAK---------------------LRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSS 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 261284556 170 HSVQIMKILRKLVtDLNKTIVIVIH---DINFASFysDYIVALKDG 212
Cdd:cd03213 146 SALQVMSLLRRLA-DTGRTIICSIHqpsSEIFELF--DKLLLLSQG 188
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-215 |
6.08e-24 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 98.38 E-value: 6.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGK-KVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDlaKKVSI 79
Cdd:PRK11650 3 GLKLQAVRKSYDGKtQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD--RDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 80 LKQsN-----HislrLTVRELVSFG----RFPysqgrlNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRafIAM-- 148
Cdd:PRK11650 81 VFQ-NyalypH----MSVRENMAYGlkirGMP------KAEIEERVAEAARILELEPLLDRKPRELSGGQRQR--VAMgr 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 261284556 149 VIAQNTEYILLDEPLNNLDMKHSVQiMKI-LRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIE 215
Cdd:PRK11650 148 AIVREPAVFLFDEPLSNLDAKLRVQ-MRLeIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAE 214
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-219 |
7.40e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 97.04 E-value: 7.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYG-----GKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVS--QWKSGDLA 74
Cdd:PRK13637 3 IKIENLTHIYMegtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 75 KKVSILKQ-SNHISLRLTVRELVSFGrfPYSQGRLNAEDEKFVDEAISYMEL--EDMQHKYLHQLSGGQTQRAFIAMVIA 151
Cdd:PRK13637 83 KKVGLVFQyPEYQLFEETIEKDIAFG--PINLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 261284556 152 QNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGK 219
Cdd:PRK13637 161 MEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGT 228
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-227 |
8.49e-24 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 96.37 E-value: 8.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDL---AKKV 77
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 78 SILKQSNHISLRLTVRELVSFGRFPYSQgrLNAEdekfVDEAISYMELEDM-----QHKYLHQLSGGQTQRAFIAMVIAQ 152
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVAYPLREHTQ--LPAP----LLHSTVMMKLEAVglrgaAKLMPSELSGGMARRAALARAIAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 261284556 153 NTEYILLDEPLNNLDmkhsVQIMKILRKLVTDLNK----TIVIVIHDINFASFYSDYIVALKDGAIESEGKTENiIQSN 227
Cdd:PRK11831 161 EPDLIMFDEPFVGQD----PITMGVLVKLISELNSalgvTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQA-LQAN 234
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-228 |
1.07e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 95.42 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVvdNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSqwKSGDLAKKVSIL 80
Cdd:PRK10771 1 MLKLTDITWLYHHLPM--RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHT--TTPPSRRPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 81 KQSNHISLRLTVRELVSFGRFPysqG-RLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILL 159
Cdd:PRK10771 77 FQENNLFSHLTVAQNIGLGLNP---GlKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 261284556 160 DEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENIIQSNV 228
Cdd:PRK10771 154 DEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKA 222
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-212 |
1.53e-23 |
|
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: 92.51 E-value: 1.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKevsqwksgdlakkvsilk 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 82 qsnhislrltvrelVSFGrfpysqgrlnaedekfvdeaisymeledmqhkYLHQLSGGQTQRAFIAMVIAQNTEYILLDE 161
Cdd:cd03221 63 --------------VKIG--------------------------------YFEQLSGGEKMRLALAKLLLENPNLLLLDE 96
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 261284556 162 PLNNLDMKhSVQimkILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDG 212
Cdd:cd03221 97 PTNHLDLE-SIE---ALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-216 |
2.12e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 95.57 E-value: 2.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGG---KKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKV 77
Cdd:PRK13650 4 IIEVKNLTFKYKEdqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 78 SILKQS-NHISLRLTVRELVSFGRfpYSQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEY 156
Cdd:PRK13650 84 GMVFQNpDNQFVGATVEDDVAFGL--ENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 157 ILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFySDYIVALKDGAIES 216
Cdd:PRK13650 162 IILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVAL-SDRVLVMKNGQVES 220
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-225 |
2.51e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 98.36 E-value: 2.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVY--GGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSI 79
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 80 LKQSNHIsLRLTVRELVSFGRFpysqgrlNAEDEKFVdEAISYMELEDM--QHKYL--------HQLSGGQTQRAFIAMV 149
Cdd:PRK11160 419 VSQRVHL-FSATLRDNLLLAAP-------NASDEALI-EVLQQVGLEKLleDDKGLnawlgeggRQLSGGEQRRLGIARA 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 261284556 150 IAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDlnKTIVIVIHD-INFASFysDYIVALKDGAIESEGKTENIIQ 225
Cdd:PRK11160 490 LLHDAPLLLLDEPTEGLDAETERQILELLAEHAQN--KTVLMITHRlTGLEQF--DRICVMDNGQIIEQGTHQELLA 562
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-226 |
4.24e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 94.85 E-value: 4.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGG-----KKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQwKSGD---- 72
Cdd:PRK13646 3 IRFDNVSYTYQKgtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITH-KTKDkyir 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 73 -LAKKVSILKQSNHISL-RLTVRELVSFGRFPYSQGRLNAEDEKFVdeaiSYMEL---EDMQHKYLHQLSGGQTQRAFIA 147
Cdd:PRK13646 82 pVRKRIGMVFQFPESQLfEDTVEREIIFGPKNFKMNLDEVKNYAHR----LLMDLgfsRDVMSQSPFQMSGGQMRKIAIV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 261284556 148 MVIAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENIIQS 226
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-226 |
4.60e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 94.14 E-value: 4.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRL-----TGKDSGLITVDGKEVSQWKSG--DLA 74
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDpiEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 75 KKVSILKQSNHISLRLTVRELVSFG----RFPYSQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVI 150
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIGvklnGLVKSKKELDERVEWALKKAALWDEVKDRLNDYPSNLSGGQRQRLVIARAL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 261284556 151 AQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLnkTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENIIQS 226
Cdd:PRK14267 165 AMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFEN 238
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-218 |
6.07e-23 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 93.66 E-value: 6.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSgdLAKKVSIL 80
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARS--LSQQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 81 KQsnhisLRLTVRELV-SFGRFPYS-------------QGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFI 146
Cdd:PRK11264 81 RQ-----LRQHVGFVFqNFNLFPHRtvleniiegpvivKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 261284556 147 AMVIAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDlNKTIVIVIHDINFASFYSDYIVALKDGAIESEG 218
Cdd:PRK11264 156 ARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
17-227 |
1.05e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 93.62 E-value: 1.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 17 VDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSILKQS-NHISLRLTVREL 95
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNpDNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 96 VSFGRfpYSQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILLDEPLNNLDMKHSVQIM 175
Cdd:PRK13642 103 VAFGM--ENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIM 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 261284556 176 KILRKLVTDLNKTIVIVIHDINFASfYSDYIVALKDGAIESEGKTENIIQSN 227
Cdd:PRK13642 181 RVIHEIKEKYQLTVLSITHDLDEAA-SSDRILVMKAGEIIKEAAPSELFATS 231
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-218 |
1.21e-22 |
|
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: 91.22 E-value: 1.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGG--KKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKsGDLAKKVSI 79
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 80 LKQSNHIsLRLTVRElvSFGRfpysqgrlnaedekfvdeaisymeledmqhkylhQLSGGQTQRAFIAMVIAQNTEYILL 159
Cdd:cd03247 80 LNQRPYL-FDTTLRN--NLGR----------------------------------RFSGGERQRLALARILLQDAPIVLL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 261284556 160 DEPLNNLDMKHSVQIMKILRKLVTDlnKTIVIVIHDINFASfYSDYIVALKDGAIESEG 218
Cdd:cd03247 123 DEPTVGLDPITERQLLSLIFEVLKD--KTLIWITHHLTGIE-HMDKILFLENGKIIMQG 178
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-197 |
1.49e-22 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 94.03 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGK-----------KVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKS 70
Cdd:COG4608 8 LEVRDLKKHFPVRgglfgrtvgvvKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 71 GDLA---KKVSILKQSNHISL--RLTVRELVSFGrfPYSQGRLNAEDEKfvDEAISYMEL----EDMQHKYLHQLSGGQT 141
Cdd:COG4608 88 RELRplrRRMQMVFQDPYASLnpRMTVGDIIAEP--LRIHGLASKAERR--ERVAELLELvglrPEHADRYPHEFSGGQR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 261284556 142 QRAFIAMVIAQNTEYILLDEPLNNLDMkhSV--QIMKILRKLVTDLNKTIVIVIHDIN 197
Cdd:COG4608 164 QRIGIARALALNPKLIVCDEPVSALDV--SIqaQVLNLLEDLQDELGLTYLFISHDLS 219
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-230 |
2.03e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 92.74 E-value: 2.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVY-GGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQW-KSGDLAKKVS 78
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFsKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 79 ILKQSNHIS-LRLTVRELVSFGrfPYSQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYI 157
Cdd:PRK13644 81 IVFQNPETQfVGRTVEEDLAFG--PENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 261284556 158 LLDEPLNNLDMKHSVQIMKILRKLvTDLNKTIVIVIHdiNFASFY-SDYIVALKDGAIESEGKTENIIQSNVLR 230
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIKKL-HEKGKTIVYITH--NLEELHdADRIIVMDRGKIVLEGEPENVLSDVSLQ 229
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-218 |
2.82e-22 |
|
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: 91.11 E-value: 2.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGG--KKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSI 79
Cdd:cd03245 3 IEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 80 LKQSNHIsLRLTVRELVSFgrfpysqGRLNAEDEKFVdEAISYMELEDMQHKYLH-----------QLSGGQTQRAFIAM 148
Cdd:cd03245 83 VPQDVTL-FYGTLRDNITL-------GAPLADDERIL-RAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 149 VIAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDlnKTIVIVIHDINFASFySDYIVALKDGAIESEG 218
Cdd:cd03245 154 ALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGD--KTLIIITHRPSLLDL-VDRIIVMDSGRIVADG 220
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-205 |
3.06e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 92.02 E-value: 3.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTgKDSGLITVDGKeVSQWKSGDLAKKVSILK 81
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMN-ELESEVRVEGR-VEFFNQNIYERRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 82 QSNHISL--------RLTVRELVSFGrFPYSQGRLNAEDEKFVDEAISYMELEDMQHKYLHQ----LSGGQTQRAFIAMV 149
Cdd:PRK14258 86 LRRQVSMvhpkpnlfPMSVYDNVAYG-VKIVGWRPKLEIDDIVESALKDADLWDEIKHKIHKsaldLSGGQQQRLCIARA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 261284556 150 IAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDY 205
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDF 220
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-195 |
3.47e-22 |
|
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: 95.00 E-value: 3.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVdGKEVsqwksgdlakKVSILK 81
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------KLAYVD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 82 QS-NHISLRLTVRELVSFG---------RFPYSQ--GRLNAedeKFVDeaisymeledmQHKYLHQLSGGQTQRAFIAMV 149
Cdd:TIGR03719 392 QSrDALDPNKTVWEEISGGldiiklgkrEIPSRAyvGRFNF---KGSD-----------QQKKVGQLSGGERNRVHLAKT 457
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 261284556 150 IAQNTEYILLDEPLNNLDmkhsVQIMKILRKLVTDLNKTIVIVIHD 195
Cdd:TIGR03719 458 LKSGGNVLLLDEPTNDLD----VETLRALEEALLNFAGCAVVISHD 499
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
2-227 |
5.32e-22 |
|
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: 94.55 E-value: 5.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGG--KKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSI 79
Cdd:TIGR03375 464 IEFRNVSFAYPGqeTPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNIGY 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 80 LKQSNhislRL---TVRELVSFGRfPYsqgrlnAEDEKFVDEA-----ISYMELE----DMQhkyLHQ----LSGGQTQR 143
Cdd:TIGR03375 544 VPQDP----RLfygTLRDNIALGA-PY------ADDEEILRAAelagvTEFVRRHpdglDMQ---IGErgrsLSGGQRQA 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 144 AFIAMVIAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDlnKTIVIVIHDINFASFySDYIVALKDGAIESEGKTENI 223
Cdd:TIGR03375 610 VALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAG--KTLVLVTHRTSLLDL-VDRIIVMDNGRIVADGPKDQV 686
|
....
gi 261284556 224 IQSN 227
Cdd:TIGR03375 687 LEAL 690
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-212 |
5.74e-22 |
|
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: 89.84 E-value: 5.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVS-----KVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKE--VSQ--W-KSG 71
Cdd:cd03250 1 ISVEDASftwdsGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIayVSQepWiQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 72 dlakkvsilkqsnhislrlTVRELVSFGRfPYsqgrlnaeDEKFVDEAISYMELE-DMqhKYLHQ------------LSG 138
Cdd:cd03250 81 -------------------TIRENILFGK-PF--------DEERYEKVIKACALEpDL--EILPDgdlteigekginLSG 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 261284556 139 GQTQRAFIAMVIAQNTEYILLDEPLNNLDMKHSVQIMK--ILRKLVtdLNKTIVIVIHDINFASfYSDYIVALKDG 212
Cdd:cd03250 131 GQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLL--NNKTRILVTHQLQLLP-HADQIVVLDNG 203
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
6-212 |
6.39e-22 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 93.82 E-value: 6.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 6 NVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGD-LAKKVSILKQSN 84
Cdd:PRK11288 9 GIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAaLAAGVAIIYQEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 85 HISLRLTVRELVSFGRFPYSQGRLNAED-EKFVDEAISYMELE---DMQHKYlhqLSGGQTQRAFIAMVIAQNTEYILLD 160
Cdd:PRK11288 89 HLVPEMTVAENLYLGQLPHKGGIVNRRLlNYEAREQLEHLGVDidpDTPLKY---LSIGQRQMVEIAKALARNARVIAFD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 261284556 161 EPLNNLDMKHSVQIMKILRKLVTDlNKTIVIVIH--DINFAsfYSDYIVALKDG 212
Cdd:PRK11288 166 EPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHrmEEIFA--LCDAITVFKDG 216
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-221 |
7.34e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 93.94 E-value: 7.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGD-LAKKVSI 79
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaIALGIGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 80 LKQsnHISL--RLTVRELVSFGRFPYSQGRLN-AEDEKFVDEAISYMELE-DMqHKYLHQLSGGQTQRAFIAMVIAQNTE 155
Cdd:COG3845 85 VHQ--HFMLvpNLTVAENIVLGLEPTKGGRLDrKAARARIRELSERYGLDvDP-DAKVEDLSVGEQQRVEILKALYRGAR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 261284556 156 YILLDEPLNNLDMKHSVQIMKILRKLvTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTE 221
Cdd:COG3845 162 ILILDEPTAVLTPQEADELFEILRRL-AAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTA 226
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-225 |
7.82e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 91.34 E-value: 7.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 19 NVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEV-SQWKSGDLA---KKVSILKQSNHISL-RLTVR 93
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItSTSKNKDIKqirKKVGLVFQFPESQLfEETVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 94 ELVSFGrfPYSQGRLNAEDEKFVDEAISYMEL-EDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILLDEPLNNLDMKHSV 172
Cdd:PRK13649 105 KDVAFG--PQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRK 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 261284556 173 QIMKILRKLVTDlNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENIIQ 225
Cdd:PRK13649 183 ELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQ 234
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-223 |
9.09e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 93.54 E-value: 9.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVsQWKSGDLAKK--VS 78
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPV-RFRSPRDAQAagIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 79 ILKQsnHISL--RLTVRELVSFGRFPYSQGRLN-AEDEKFVDEAISYMELE---DMQhkyLHQLSGGQTQRAFIAMVIAQ 152
Cdd:COG1129 83 IIHQ--ELNLvpNLSVAENIFLGREPRRGGLIDwRAMRRRARELLARLGLDidpDTP---VGDLSVAQQQLVEIARALSR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 261284556 153 NTEYILLDEPLNNLDMKHSVQIMKILRKLvTDLNKTIVIVIHDIN--FAsfYSDYIVALKDGAIESEGKTENI 223
Cdd:COG1129 158 DARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLDevFE--IADRVTVLRDGRLVGTGPVAEL 227
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-223 |
1.24e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 91.04 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYG-----GKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSG----D 72
Cdd:PRK13641 3 IKFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNknlkK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 73 LAKKVSILKQSNHISL-RLTVRELVSFGrfPYSQGrlnAEDEKFVDEAISYMEL----EDMQHKYLHQLSGGQTQRAFIA 147
Cdd:PRK13641 83 LRKKVSLVFQFPEAQLfENTVLKDVEFG--PKNFG---FSEDEAKEKALKWLKKvglsEDLISKSPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 261284556 148 MVIAQNTEYILLDEPLNNLDMKHSVQIMKILRklvtDLNK---TIVIVIHDINFASFYSDYIVALKDGAIESEGKTENI 223
Cdd:PRK13641 158 GVMAYEPEILCLDEPAAGLDPEGRKEMMQLFK----DYQKaghTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-235 |
1.65e-21 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 92.86 E-value: 1.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGG--KKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSI 79
Cdd:TIGR02203 331 VEFRNVTFRYPGrdRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 80 LKQSNHIsLRLTVRELVSFGRfPYSQGRLNAEDekfVDEAISYMELEDMQHKYLHQ--------LSGGQTQRAFIAMVIA 151
Cdd:TIGR02203 411 VSQDVVL-FNDTIANNIAYGR-TEQADRAEIER---ALAAAYAQDFVDKLPLGLDTpigengvlLSGGQRQRLAIARALL 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 152 QNTEYILLDEPLNNLDMKHSVQIMKILRKLVTdlNKTIVIVIHDINFASfYSDYIVALKDGAIESEGKTENIIQSNvlrG 231
Cdd:TIGR02203 486 KDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIE-KADRIVVMDDGRIVERGTHNELLARN---G 559
|
....
gi 261284556 232 IYDM 235
Cdd:TIGR02203 560 LYAQ 563
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
15-233 |
1.71e-21 |
|
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: 89.52 E-value: 1.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 15 KVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSILKQSNHIsLRLTVRE 94
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVL-FDGTIAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 95 LVSFGRFPYSQgrlnAEDEKFVDEAISYMELEDMQHKYL-------HQLSGGQTQRAFIAMVIAQNTEYILLDEPLNNLD 167
Cdd:cd03249 96 NIRYGKPDATD----EEVEEAAKKANIHDFIMSLPDGYDtlvgergSQLSGGQKQRIAIARALLRNPKILLLDEATSALD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 261284556 168 MKHSVQIMKILRKLVtdLNKTIVIVIHDINFASfYSDYIVALKDGAIESEGKTENIIQsnvLRGIY 233
Cdd:cd03249 172 AESEKLVQEALDRAM--KGRTTIVIAHRLSTIR-NADLIAVLQNGQVVEQGTHDELMA---QKGVY 231
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-218 |
1.97e-21 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 89.13 E-value: 1.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVY----------------------GGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLIT 59
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 60 VDGKeVSqwksgdlakkvSILKQSNHISLRLTVRELVSF-GRFpysQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSG 138
Cdd:cd03220 81 VRGR-VS-----------SLLGLGGGFNPELTGRENIYLnGRL---LGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 139 GQTQR-AFiAMVIAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDlNKTIVIVIHDINFASFYSDYIVALKDGAIESE 217
Cdd:cd03220 146 GMKARlAF-AIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
.
gi 261284556 218 G 218
Cdd:cd03220 224 G 224
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-225 |
3.24e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 89.79 E-value: 3.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYG-----GKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVS----QWKSG 71
Cdd:PRK13643 1 MIKFEKVNYTYQpnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSstskQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 72 DLAKKVSILKQSNHISL-RLTVRELVSFGrfPYSQGRLNAEDEKFVDEAISYMEL-EDMQHKYLHQLSGGQTQRAFIAMV 149
Cdd:PRK13643 81 PVRKKVGVVFQFPESQLfEETVLKDVAFG--PQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 261284556 150 IAQNTEYILLDEPLNNLDMKHSVQIMKILRKlVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENIIQ 225
Cdd:PRK13643 159 LAMEPEVLVLDEPTAGLDPKARIEMMQLFES-IHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
12-195 |
3.84e-21 |
|
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: 92.04 E-value: 3.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 12 GGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSILKQSNHIsLRLT 91
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHL-FDTT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 92 VRELVSFGRfPysqgrlNAEDEKF------VDEAISYMELEDMQHKYLHQ----LSGGQTQRAFIAMVIAQNTEYILLDE 161
Cdd:TIGR02868 425 VRENLRLAR-P------DATDEELwaalerVGLADWLRALPDGLDTVLGEggarLSGGERQRLALARALLADAPILLLDE 497
|
170 180 190
....*....|....*....|....*....|....
gi 261284556 162 PLNNLDMKHSVQIMKILRKlvTDLNKTIVIVIHD 195
Cdd:TIGR02868 498 PTEHLDAETADELLEDLLA--ALSGRTVVLITHH 529
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-217 |
5.71e-21 |
|
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: 87.87 E-value: 5.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKK----VVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAK- 75
Cdd:COG4181 8 IIELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 76 ---KVSILKQSNHISLRLTVRELVSFgrfPYS-QGRLNAEDEkfVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIA 151
Cdd:COG4181 88 rarHVGFVFQSFQLLPTLTALENVML---PLElAGRRDARAR--ARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 261284556 152 QNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASfYSDYIVALKDGAIESE 217
Cdd:COG4181 163 TEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAA-RCDRVLRLRAGRLVED 227
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-233 |
6.84e-21 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 88.01 E-value: 6.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKK-VSI 79
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREaVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 80 LKQSNHISLRLTVRELVSFGRFPYSQGRLNAEDEKFVDeaiSYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILL 159
Cdd:PRK11614 85 VPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYE---LFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 261284556 160 DEPLNNLDMKHSVQIMKILRKLVTDlNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENIIQSNVLRGIY 233
Cdd:PRK11614 162 DEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAY 234
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-167 |
7.94e-21 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 90.95 E-value: 7.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMIsrlTGK---DSGLITVdGKEVsqwksgdlakKVS 78
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMI---TGQeqpDSGTIKI-GETV----------KLA 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 79 ILKQSnhislrltvrelvsfgrfpysqgRLNAEDEKFVDEAIS----YMELEDM-----------------QHKYLHQLS 137
Cdd:PRK11819 391 YVDQS-----------------------RDALDPNKTVWEEISggldIIKVGNReipsrayvgrfnfkggdQQKKVGVLS 447
|
170 180 190
....*....|....*....|....*....|
gi 261284556 138 GGQTQRAFIAMVIAQNTEYILLDEPLNNLD 167
Cdd:PRK11819 448 GGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
16-214 |
1.04e-20 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 87.14 E-value: 1.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 16 VVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSILKQSNHISLRlTVREL 95
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVLFAR-SLQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 96 VSFGRFPYSQGRLNAEDEKF-VDEAISYMEL---EDMQHKYlHQLSGGQTQRAFIAMVIAQNTEYILLDEPLNNLDMKHS 171
Cdd:cd03248 108 IAYGLQSCSFECVKEAAQKAhAHSFISELASgydTEVGEKG-SQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESE 186
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 261284556 172 VQIMKILRKLVTdlNKTIVIVIHDINFASfYSDYIVALKDGAI 214
Cdd:cd03248 187 QQVQQALYDWPE--RRTVLVIAHRLSTVE-RADQILVLDGGRI 226
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-226 |
1.43e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 87.41 E-value: 1.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 4 VTNVSKVY---GGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVD------GKEVSQWKSGDLA 74
Cdd:PRK14246 10 VFNISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDgkvlyfGKDIFQIDAIKLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 75 KKVSILKQSNHISLRLTVRELVSfgrFPYSQGRLNAEDE--KFVDEAIS----YMELEDMQHKYLHQLSGGQTQRAFIAM 148
Cdd:PRK14246 90 KEVGMVFQQPNPFPHLSIYDNIA---YPLKSHGIKEKREikKIVEECLRkvglWKEVYDRLNSPASQLSGGQQQRLTIAR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 261284556 149 VIAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLnkTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENIIQS 226
Cdd:PRK14246 167 ALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTS 242
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-218 |
1.43e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 88.14 E-value: 1.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGK-----KVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDG-------KEVSQWK 69
Cdd:PRK13645 7 IILDNVSYTYAKKtpfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 70 sgDLAKKVSILKQSNHISL-RLTVRELVSFGrfPYSQGRLNAEDEKFVDEAISYMEL-EDMQHKYLHQLSGGQTQRAFIA 147
Cdd:PRK13645 87 --RLRKEIGLVFQFPEYQLfQETIEKDIAFG--PVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 261284556 148 MVIAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEG 218
Cdd:PRK13645 163 GIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIG 233
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-212 |
1.62e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 86.47 E-value: 1.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVY-GGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGD---LAKK 76
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 77 VSILKQSNHISLRLTVRELVSFgrfPYSQGRLNAED-EKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTE 155
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAI---PLIIAGASGDDiRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 261284556 156 YILLDEPLNNLDMKHSVQIMKILRKLvTDLNKTIVIVIHDINFASFYSDYIVALKDG 212
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGILRLFEEF-NRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-223 |
1.75e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 87.84 E-value: 1.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGG------KKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKS-GDL 73
Cdd:PRK13633 4 MIKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENlWDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 74 AKKVSILKQS--NHIsLRLTVRELVSFGrfPYSQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIA 151
Cdd:PRK13633 84 RNKAGMVFQNpdNQI-VATIVEEDVAFG--PENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 261284556 152 QNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASfYSDYIVALKDGAIESEGKTENI 223
Cdd:PRK13633 161 MRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAV-EADRIIVMDSGKVVMEGTPKEI 231
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-219 |
2.16e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 87.37 E-value: 2.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLA--KKVS 78
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLAlrQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 79 ILKQSNHISLRLT-VRELVSFGRfpYSQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYI 157
Cdd:PRK13638 81 TVFQDPEQQIFYTdIDSDIAFSL--RNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 261284556 158 LLDEPLNNLDMKHSVQIMKILRKLVTDLNKtIVIVIHDINFASFYSDYIVALKDGAIESEGK 219
Cdd:PRK13638 159 LLDEPTAGLDPAGRTQMIAIIRRIVAQGNH-VIISSHDIDLIYEISDAVYVLRQGQILTHGA 219
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-225 |
2.54e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 86.67 E-value: 2.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVY----------------------GGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLI 58
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 59 TVDGkevsqwksgdlakKVSILkqsnhISL------RLTVRELVSF-GRFpysQGRLNAEDEKFVDEAISYMELEDmqhk 131
Cdd:COG1134 84 EVNG-------------RVSAL-----LELgagfhpELTGRENIYLnGRL---LGLSRKEIDEKFDEIVEFAELGD---- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 132 YLHQ----LSGGQTQR-AFiAMVIAQNTEYILLDEPLnnldmkhSV-------QIMKILRKLVTDlNKTIVIVIHDINFA 199
Cdd:COG1134 139 FIDQpvktYSSGMRARlAF-AVATAVDPDILLVDEVL-------AVgdaafqkKCLARIRELRES-GRTVIFVSHSMGAV 209
|
250 260
....*....|....*....|....*.
gi 261284556 200 SFYSDYIVALKDGAIESEGKTENIIQ 225
Cdd:COG1134 210 RRLCDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-172 |
3.09e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 85.31 E-value: 3.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSqwkSGDLAKKVSIL 80
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID---DPDVAEACHYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 81 KQSNHISLRLTVRELVSFGRfpysqgRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILLD 160
Cdd:PRK13539 79 GHRNAMKPALTVAENLEFWA------AFLGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILD 152
|
170
....*....|..
gi 261284556 161 EPLNNLDmKHSV 172
Cdd:PRK13539 153 EPTAALD-AAAV 163
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-226 |
4.29e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 86.69 E-value: 4.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGL-----ITVDGKEVSQWKSG-DLAK 75
Cdd:PRK14271 22 MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRSIFNYRDVlEFRR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 76 KVSILKQS---------NHISLRLTVRELVSFGRFP-YSQGRLNaedekfvdEAISYMELEDMQHKYLHQLSGGQTQRAF 145
Cdd:PRK14271 102 RVGMLFQRpnpfpmsimDNVLAGVRAHKLVPRKEFRgVAQARLT--------EVGLWDAVKDRLSDSPFRLSGGQQQLLC 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 146 IAMVIAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLnkTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENIIQ 225
Cdd:PRK14271 174 LARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFS 251
|
.
gi 261284556 226 S 226
Cdd:PRK14271 252 S 252
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-224 |
5.00e-20 |
|
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: 88.71 E-value: 5.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTG--KDSGLI----------------TVDGK 63
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyhvalcekcgyverpSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 64 EVSQWKSGDLAKKVSILKQSNHISLRLTVRELVSFGR-FP-YSQGR-----LNA------EDEKFVDEAISYMELEDMQH 130
Cdd:TIGR03269 81 PCPVCGGTLEPEEVDFWNLSDKLRRRIRKRIAIMLQRtFAlYGDDTvldnvLEAleeigyEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 131 KYLH---QLSGGQTQRAFIAMVIAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIV 207
Cdd:TIGR03269 161 RITHiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240
|
250
....*....|....*..
gi 261284556 208 ALKDGAIESEGKTENII 224
Cdd:TIGR03269 241 WLENGEIKEEGTPDEVV 257
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-214 |
5.23e-20 |
|
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: 84.19 E-value: 5.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKK--VVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSI 79
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 80 LKQsnhislrltvrelvsfgrfpysqgrlnaEDEKF---VDEAIsymeledmqhkylhqLSGGQTQRAFIAMVIAQNTEY 156
Cdd:cd03246 81 LPQ----------------------------DDELFsgsIAENI---------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 261284556 157 ILLDEPLNNLDMKHSVQIMKILRKLvTDLNKTIVIVIHDINFASfYSDYIVALKDGAI 214
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-222 |
6.52e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 88.63 E-value: 6.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVY----GGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAK- 75
Cdd:PRK10535 4 LLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 76 ---KVSILKQSNHISLRLTVRELVSFGRFPYSQGRlnAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQ 152
Cdd:PRK10535 84 rreHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLER--KQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMN 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 153 NTEYILLDEPLNNLDMKHSVQIMKILRKLvTDLNKTIVIVIHDINFASfYSDYIVALKDGAIESEGKTEN 222
Cdd:PRK10535 162 GGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAA-QAERVIEIRDGEIVRNPPAQE 229
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-197 |
1.08e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 86.29 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVY---------GG------------KKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMisrLTG---KDSG 56
Cdd:COG4586 1 IIEVENLSKTYrvyekepglKGalkglfrreyreVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKM---LTGilvPTSG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 57 LITVDGKEVSQwKSGDLAKKVS-ILKQSNHISLRLTVRElvSFgrfpysqgRLNAE-----DEKF---VDEAISYMELED 127
Cdd:COG4586 78 EVRVLGYVPFK-RRKEFARRIGvVFGQRSQLWWDLPAID--SF--------RLLKAiyripDAEYkkrLDELVELLDLGE 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 128 MQHKYLHQLSGGQTQRAFIAMVIAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDIN 197
Cdd:COG4586 147 LLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMD 216
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-226 |
1.12e-19 |
|
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: 87.50 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKK--VVDNVSVTIPKGQITSFIGPNGAGKSTLLSMisrLTG---KDSGLITVDGKEVSQWKSGDLAKK 76
Cdd:COG4618 331 LSVENLTVVPPGSKrpILRGVSFSLEPGEVLGVIGPSGSGKSTLARL---LVGvwpPTAGSVRLDGADLSQWDREELGRH 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 77 VSILKQSnhISL-RLTVRELVSfgRFPysqgrlNAEDEKFVD--------EAISYM------ELEDMqhkyLHQLSGGQT 141
Cdd:COG4618 408 IGYLPQD--VELfDGTIAENIA--RFG------DADPEKVVAaaklagvhEMILRLpdgydtRIGEG----GARLSGGQR 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 142 QRAFIAMVIAQNTEYILLDEPLNNLDmkhsVQIMKILRKLVTDL---NKTIVIVIHDINFASfYSDYIVALKDGAIESEG 218
Cdd:COG4618 474 QRIGLARALYGDPRLVVLDEPNSNLD----DEGEAALAAAIRALkarGATVVVITHRPSLLA-AVDKLLVLRDGRVQAFG 548
|
....*...
gi 261284556 219 KTENIIQS 226
Cdd:COG4618 549 PRDEVLAR 556
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
2-213 |
1.13e-19 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 84.30 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYG-GKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKK---- 76
Cdd:cd03290 1 VQVTNGYFSWGsGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrys 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 77 VSILKQSNHIsLRLTVRELVSFGRfPYSQGRLnaedeKFVDEAISYM-ELEDMQHKYLHQ-------LSGGQTQRAFIAM 148
Cdd:cd03290 81 VAYAAQKPWL-LNATVEENITFGS-PFNKQRY-----KAVTDACSLQpDIDLLPFGDQTEigerginLSGGQRQRICVAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 261284556 149 VIAQNTEYILLDEPLNNLDMKHSVQIMK--ILrKLVTDLNKTIVIVIHDINFASfYSDYIVALKDGA 213
Cdd:cd03290 154 ALYQNTNIVFLDDPFSALDIHLSDHLMQegIL-KFLQDDKRTLVLVTHKLQYLP-HADWIIAMKDGS 218
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
17-226 |
1.22e-19 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 87.01 E-value: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 17 VDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLA----KKVSILKQSNHISLRLTV 92
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 93 RELVSFGRfpYSQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILLDEPLNNLDMKHSV 172
Cdd:PRK10070 124 LDNTAFGM--ELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 261284556 173 QIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENIIQS 226
Cdd:PRK10070 202 EMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-224 |
3.21e-19 |
|
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: 86.39 E-value: 3.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVY-----GGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLIT-------VDGKEVSQW 68
Cdd:TIGR03269 279 IIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 69 KSGDLAKKVSILKQS----NHISLRLTVRELVSFgRFPYSQGRLNA----EDEKFVDEaisymELEDMQHKYLHQLSGGQ 140
Cdd:TIGR03269 359 GRGRAKRYIGILHQEydlyPHRTVLDNLTEAIGL-ELPDELARMKAvitlKMVGFDEE-----KAEEILDKYPDELSEGE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 141 TQRAFIAMVIAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKT 220
Cdd:TIGR03269 433 RHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDP 512
|
....
gi 261284556 221 ENII 224
Cdd:TIGR03269 513 EEIV 516
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-227 |
3.99e-19 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 86.33 E-value: 3.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYG-GKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSIL 80
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 81 KQSNHISLRLTVRELVSfgrfpysQGRLNAEDEKfVDEAISYMEL----EDMQHKYLHQL-------SGGQTQRAFIAMV 149
Cdd:TIGR01193 554 PQEPYIFSGSILENLLL-------GAKENVSQDE-IWAACEIAEIkddiENMPLGYQTELseegssiSGGQKQRIALARA 625
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 261284556 150 IAQNTEYILLDEPLNNLDMkhsVQIMKILRKLVTDLNKTIVIVIHDINFASfYSDYIVALKDGAIESEGKTENIIQSN 227
Cdd:TIGR01193 626 LLTDSKVLILDESTSNLDT---ITEKKIVNNLLNLQDKTIIFVAHRLSVAK-QSDKIIVLDHGKIIEQGSHDELLDRN 699
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
2-225 |
6.26e-19 |
|
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: 85.48 E-value: 6.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVY-GGKK-VVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSI 79
Cdd:TIGR01842 317 LSVENVTIVPpGGKKpTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGY 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 80 LKQSnhISL-RLTVRELVSfgRFpysqgRLNAEDEKFVDEAIS------YMELEDMQHKYLHQ----LSGGQTQRAFIAM 148
Cdd:TIGR01842 397 LPQD--VELfPGTVAENIA--RF-----GENADPEKIIEAAKLagvhelILRLPDGYDTVIGPggatLSGGQRQRIALAR 467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 261284556 149 VIAQNTEYILLDEPLNNLDMKHSVQIMKILRKLvtDLNKTIVIVI-HDINFASFySDYIVALKDGAIESEGKTENIIQ 225
Cdd:TIGR01842 468 ALYGDPKLVVLDEPNSNLDEEGEQALANAIKAL--KARGITVVVItHRPSLLGC-VDKILVLQDGRIARFGERDEVLA 542
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-238 |
8.19e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 85.22 E-value: 8.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAK-KVSI 79
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQlGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 80 LKQSNHISLRLTVRELVSFGRFPYSQ-GRLNAEDEKFVDEAISYMELE-----DMQHKyLHQLSGGQTQRAFIAMVIAQN 153
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIGRHLTKKvCGVNIIDWREMRVRAAMMLLRvglkvDLDEK-VANLSISHKQMLEIAKTLMLD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 154 TEYILLDEPLNNLDMKHSVQIMKILRKLVTDlNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENIIQSNVLRGIY 233
Cdd:PRK09700 164 AKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVRLMV 242
|
....*
gi 261284556 234 DMDIE 238
Cdd:PRK09700 243 GRELQ 247
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-217 |
1.16e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 81.79 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKK----VVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAK- 75
Cdd:PRK11629 5 LLQCDNLCKRYQEGSvqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAEl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 76 ---KVSILKQSNHISLRLTVRELVSFgrfPYSQGRLN-AEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIA 151
Cdd:PRK11629 85 rnqKLGFIYQFHHLLPDFTALENVAM---PLLIGKKKpAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 261284556 152 QNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYiVALKDGAIESE 217
Cdd:PRK11629 162 NNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQ-LEMRDGRLTAE 226
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-227 |
1.60e-18 |
|
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: 81.76 E-value: 1.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYG--GKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSI 79
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 80 LKQSNhISLRLTVRELVSFGRFPYSQGRLnAEDEKFVDEAISYMELEDMQHKYLHQ----LSGGQTQRAFIAMVIAQNTE 155
Cdd:cd03252 81 VLQEN-VLFNRSIRDNIALADPGMSMERV-IEAAKLAGAHDFISELPEGYDTIVGEqgagLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 261284556 156 YILLDEPLNNLDMKHSVQIMKILRKLVTdlNKTIVIVIHDINfASFYSDYIVALKDGAIESEGKTENIIQSN 227
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDELLAEN 227
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
23-207 |
1.83e-18 |
|
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: 81.69 E-value: 1.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 23 TIPKGQITSFIGPNGAGKSTLLSMISrltgkdsGLITVDGKEVsqwksGDLAKKVSILKQSNHISLRLTVRELVS----- 97
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLA-------GVLKPDEGDI-----EIELDTVSYKPQYIKADYEGTVRDLLSsitkd 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 98 FGRFPYsqgrlnaedekFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILLDEPLNNLDMKHSVQIMKI 177
Cdd:cd03237 89 FYTHPY-----------FKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKV 157
|
170 180 190
....*....|....*....|....*....|
gi 261284556 178 LRKLVTDLNKTIVIVIHDINFASFYSDYIV 207
Cdd:cd03237 158 IRRFAENNEKTAFVVEHDIIMIDYLADRLI 187
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-214 |
2.26e-18 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 81.66 E-value: 2.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGG---------KKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKS- 70
Cdd:PRK10419 3 LLNVSGLSHHYAHgglsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRa 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 71 --GDLAKKVSILKQS--NHISLRLTVRELVsfgRFPYSQ-GRLN-AEDEKFVDEAISYMEL--EDMQhKYLHQLSGGQTQ 142
Cdd:PRK10419 83 qrKAFRRDIQMVFQDsiSAVNPRKTVREII---REPLRHlLSLDkAERLARASEMLRAVDLddSVLD-KRPPQLSGGQLQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 261284556 143 RAFIAMVIAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAI 214
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-209 |
2.64e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 81.31 E-value: 2.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLItvdgKEVSQWKSGDLAKKVSIl 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI----KRNGKLRIGYVPQKLYL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 81 kqsnHISLRLTVrelvsfGRFPYSQGRLNAEDekfVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILLD 160
Cdd:PRK09544 79 ----DTTLPLTV------NRFLRLRPGTKKED---ILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLD 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 261284556 161 EPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVAL 209
Cdd:PRK09544 146 EPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL 194
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-218 |
4.13e-18 |
|
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: 83.52 E-value: 4.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 4 VTNVSKVY--GGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSqwKSGDLAKK-VSIL 80
Cdd:TIGR01257 931 VKNLVKIFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE--TNLDAVRQsLGMC 1008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 81 KQSNHISLRLTVRELVSFgrfpYSQGRLNAEDEKFVD-EAIsymeLED--MQHKY---LHQLSGGQTQRAFIAMVIAQNT 154
Cdd:TIGR01257 1009 PQHNILFHHLTVAEHILF----YAQLKGRSWEEAQLEmEAM----LEDtgLHHKRneeAQDLSGGMQRKLSVAIAFVGDA 1080
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 261284556 155 EYILLDEPLNNLDMKHSVQIMKILRKLVTdlNKTIVIVIHDINFASFYSDYIVALKDGAIESEG 218
Cdd:TIGR01257 1081 KVVVLDEPTSGVDPYSRRSIWDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
12-179 |
8.66e-18 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 78.69 E-value: 8.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 12 GGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKsGDLAKKVSILKQSNHISLRLT 91
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQR-DSIARGLLYLGHAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 92 VRELVSFGRfpysqgRLNAEDEkfVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILLDEPLNNLDMKHS 171
Cdd:cd03231 90 VLENLRFWH------ADHSDEQ--VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
....*...
gi 261284556 172 VQIMKILR 179
Cdd:cd03231 162 ARFAEAMA 169
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-223 |
1.41e-17 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 79.26 E-value: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKvSIL 80
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM-GVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 81 KQSNHISL--RLTVRE--LVSFGRF---PYSQGRLN------AEDEKfVDEAISYME---LEDMQHKYLHQLSGGQTQRA 144
Cdd:PRK11300 84 RTFQHVRLfrEMTVIEnlLVAQHQQlktGLFSGLLKtpafrrAESEA-LDRAATWLErvgLLEHANRQAGNLAYGQQRRL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 261284556 145 FIAMVIAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENI 223
Cdd:PRK11300 163 EIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 241
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
24-206 |
1.54e-17 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 79.33 E-value: 1.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 24 IPK-GQITSFIGPNGAGKSTLLSMIS--------RLTGKDSGLITVD---GKEVSQWKSGDLAKKVSILKQSNHISL--- 88
Cdd:cd03236 22 VPReGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWDEILDefrGSELQNYFTKLLEGDVKVIVKPQYVDLipk 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 89 --RLTVRELvsfgrfpysqgrLNAEDEK-FVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILLDEPLNN 165
Cdd:cd03236 102 avKGKVGEL------------LKKKDERgKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSY 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 261284556 166 LDMKHSVQIMKILRKLVTDlNKTIVIVIHDINFASFYSDYI 206
Cdd:cd03236 170 LDIKQRLNAARLIRELAED-DNYVLVVEHDLAVLDYLSDYI 209
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
13-227 |
1.62e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 81.43 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 13 GKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMisrLTG--KDSGLITVDGKEVSQWKSGDLAKKVSILKQSNHIsLRL 90
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNA---LLGflPYQGSLKINGIELRELDPESWRKHLSWVGQNPQL-PHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 91 TVRELVSFGRFPYSQGRLNAEDEK-FVDEAIsymelEDMQHKYLHQ-------LSGGQTQRAFIAMVIAQNTEYILLDEP 162
Cdd:PRK11174 438 TLRDNVLLGNPDASDEQLQQALENaWVSEFL-----PLLPQGLDTPigdqaagLSVGQAQRLALARALLQPCQLLLLDEP 512
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 261284556 163 LNNLDMKHSVQIMKILRKLVTDlnKTIVIVIHDINFASFYsDYIVALKDGAIESEGKTENIIQSN 227
Cdd:PRK11174 513 TASLDAHSEQLVMQALNAASRR--QTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
12-197 |
3.39e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 77.83 E-value: 3.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 12 GGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSILKQSNhislrlt 91
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTP------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 92 vrelVSFGR-------FPYsQGRLNAEDEKFVDEAISYMEL-EDMQHKYLHQLSGGQTQRafIAMViaQNTEY----ILL 159
Cdd:PRK10247 91 ----TLFGDtvydnliFPW-QIRNQQPDPAIFLDDLERFALpDTILTKNIAELSGGEKQR--ISLI--RNLQFmpkvLLL 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 261284556 160 DEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDIN 197
Cdd:PRK10247 162 DEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKD 199
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-219 |
4.35e-17 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 80.15 E-value: 4.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVY---GGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVS 78
Cdd:TIGR00958 479 IEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 79 ILKQSNhISLRLTVRELVSFG-RFPYSQGRLNAEDEKFVDEAIsyMELEDMQHKYL----HQLSGGQTQRAFIAMVIAQN 153
Cdd:TIGR00958 559 LVGQEP-VLFSGSVRENIAYGlTDTPDEEIMAAAKAANAHDFI--MEFPNGYDTEVgekgSQLSGGQKQRIAIARALVRK 635
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 261284556 154 TEYILLDEPLNNLDmkhsVQIMKILRKLVTDLNKTIVIVIHDINFASfYSDYIVALKDGAIESEGK 219
Cdd:TIGR00958 636 PRVLILDEATSALD----AECEQLLQESRSRASRTVLLIAHRLSTVE-RADQILVLKKGSVVEMGT 696
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
5-212 |
9.43e-17 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 79.00 E-value: 9.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 5 TNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVsQWKSGD--LAKKVSILKQ 82
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-DFKSSKeaLENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 83 SNHISLRLTVRELVSFGRFPySQGRLNAEDEKFVDEAISYMELE---DMQHKyLHQLSGGQTQRAFIAMVIAQNTEYILL 159
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLGRYP-TKGMFVDQDKMYRDTKAIFDELDidiDPRAK-VATLSVSQMQMIEIAKAFSYNAKIVIM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 261284556 160 DEPLNNLDMKHSVQIMKILRKLvTDLNKTIVIVIHDINFASFYSDYIVALKDG 212
Cdd:PRK10982 159 DEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-223 |
2.16e-16 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 76.12 E-value: 2.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEvSQWKsgDLAKKVS-- 78
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRD-GQLR--DLYALSEae 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 79 ----------ILKQSNHISLRLTV-------RELVSFGRFPYsqGRLNAEDEKFVDEA-ISYMELEDMQHKYlhqlSGGQ 140
Cdd:PRK11701 83 rrrllrtewgFVHQHPRDGLRMQVsaggnigERLMAVGARHY--GDIRATAGDWLERVeIDAARIDDLPTTF----SGGM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 141 TQRAFIAMVIAQNTEYILLDEPLNNLDMkhSVQ--IMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEG 218
Cdd:PRK11701 157 QQRLQIARNLVTHPRLVFMDEPTGGLDV--SVQarLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
....*
gi 261284556 219 KTENI 223
Cdd:PRK11701 235 LTDQV 239
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
19-230 |
4.53e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 76.45 E-value: 4.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 19 NVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSqwksgDLAKKVSILKQSNHISL-----RLtvr 93
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLF-----DAEKGICLPPEKRRIGYvfqdaRL--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 94 elvsfgrFP-YS-QGRL-----NAEDEKFvDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILLDEPLNNL 166
Cdd:PRK11144 88 -------FPhYKvRGNLrygmaKSMVAQF-DKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 261284556 167 DMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENIIQSNVLR 230
Cdd:PRK11144 160 DLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAMR 223
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
6-179 |
4.69e-16 |
|
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: 73.93 E-value: 4.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 6 NVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQwKSGDLAKKVSILKQSNH 85
Cdd:TIGR01189 5 NLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAE-QRDEPHENILYLGHLPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 86 ISLRLTVRELVSFGRfpysqgRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQR-AFIAMVIAQNTEYIlLDEPLN 164
Cdd:TIGR01189 84 LKPELSALENLHFWA------AIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRlALARLWLSRRPLWI-LDEPTT 156
|
170
....*....|....*
gi 261284556 165 NLDMKHSVQIMKILR 179
Cdd:TIGR01189 157 ALDKAGVALLAGLLR 171
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-233 |
8.19e-16 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 76.21 E-value: 8.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKKV--VDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSI 79
Cdd:PRK11176 342 IEFRNVTFTYPGKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 80 LKQSNHIsLRLTVRELVSFGRFP-YSQGRL-NAEDEKFVDEAISYME--LEDMQHKYLHQLSGGQTQRAFIAMVIAQNTE 155
Cdd:PRK11176 422 VSQNVHL-FNDTIANNIAYARTEqYSREQIeEAARMAYAMDFINKMDngLDTVIGENGVLLSGGQRQRIAIARALLRDSP 500
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 261284556 156 YILLDEPLNNLDMKHSVQIMKILRKLvtDLNKTIVIVIHDINFASfYSDYIVALKDGAIESEGKTENIIQSNvlrGIY 233
Cdd:PRK11176 501 ILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIE-KADEILVVEDGEIVERGTHAELLAQN---GVY 572
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
12-220 |
1.14e-15 |
|
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: 72.66 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 12 GGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMIS--RLTGKDSGLITVDGKEVSQwksgDLAKKVSILKQSN-HISL 88
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAgrKTAGVITGEILINGRPLDK----NFQRSTGYVEQQDvHSPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 89 rLTVRELVSFgrfpysqgrlnaedekfvdeaisymeledmqHKYLHQLSGGQTQRAFIAMVIAQNTEYILLDEPLNNLDM 168
Cdd:cd03232 94 -LTVREALRF-------------------------------SALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 261284556 169 KHSVQIMKILRKLVtDLNKTIVIVIH----DInFASFysDYIVALKDGaieseGKT 220
Cdd:cd03232 142 QAAYNIVRFLKKLA-DSGQAILCTIHqpsaSI-FEKF--DRLLLLKRG-----GKT 188
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-223 |
2.15e-15 |
|
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: 75.11 E-value: 2.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 12 GGKKVVDNVSVTIPKGQITSFIGPNGAGKS-TLLSmISRL----TGKDSGLITVDGKEVSQWKSGDLAK----KVSILKQ 82
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvTALS-ILRLlpdpAAHPSGSILFDGQDLLGLSERELRRirgnRIAMIFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 83 SNHISLR--LTVrelvsfGRfpysQ--------GRLNAEDEKfvDEAISYMEL------EDMQHKYLHQLSGGQTQRAFI 146
Cdd:COG4172 100 EPMTSLNplHTI------GK----QiaevlrlhRGLSGAAAR--ARALELLERvgipdpERRLDAYPHQLSGGQRQRVMI 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 261284556 147 AMVIAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENI 223
Cdd:COG4172 168 AMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAEL 244
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
9-223 |
4.02e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 74.36 E-value: 4.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 9 KVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKST----LLSMISrltgkDSGLITVDGKEVSQWKSGDL---AKKVSILK 81
Cdd:PRK15134 294 RTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQLlpvRHRIQVVF 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 82 QSNHISL--RLTVRELVSFGrFPYSQGRLNA-EDEKFVDEAISYMELE-DMQHKYLHQLSGGQTQRAFIAMVIAQNTEYI 157
Cdd:PRK15134 369 QDPNSSLnpRLNVLQIIEEG-LRVHQPTLSAaQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLI 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 261284556 158 LLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENI 223
Cdd:PRK15134 448 ILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERV 513
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
5-207 |
5.38e-15 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 74.05 E-value: 5.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 5 TNVSKVYGGKKV-VDnvSVTIPKGQITSFIGPNGAGKSTLLSMISrltgkdsGLITVDGKEVsqwksgDLAKKVSILKQS 83
Cdd:COG1245 345 PDLTKSYGGFSLeVE--GGEIREGEVLGIVGPNGIGKTTFAKILA-------GVLKPDEGEV------DEDLKISYKPQY 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 84 NHISLRLTVREL---VSFGRFPYSqgrlnaedeKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILLD 160
Cdd:COG1245 410 ISPDYDGTVEEFlrsANTDDFGSS---------YYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLD 480
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 261284556 161 EPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIV 207
Cdd:COG1245 481 EPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLM 527
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-214 |
1.37e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 71.25 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 4 VTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLsmisRLTgkdSGLITVDGKEVsqwksgdLAKKVSILKQS 83
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLL----RLL---AGLETPSAGEL-------LAGTAPLAEAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 84 NHISL-----RL----TVRELVSFGRfpYSQGRLNAEdekfvdEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNT 154
Cdd:PRK11247 81 EDTRLmfqdaRLlpwkKVIDNVGLGL--KGQWRDAAL------QALAAVGLADRANEWPAALSGGQKQRVALARALIHRP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 155 EYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAI 214
Cdd:PRK11247 153 GLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
17-225 |
1.94e-14 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 70.50 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 17 VDNVSVTIPKGQITSFIGPNGAGKS----TLLSMISRLTGKDSGLITVDGKEVSqwkSGDL-AKKVSILKQsNHISLRLT 91
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVA---PCALrGRKIATIMQ-NPRSAFNP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 92 VRELVSFGRFPYSQGRLNAEDEKFVdEAISYMELEDMQ---HKYLHQLSGGQTQRAFIAMVIAQNTEYILLDEPLNNLDM 168
Cdd:PRK10418 95 LHTMHTHARETCLALGKPADDATLT-AALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 261284556 169 KHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENIIQ 225
Cdd:PRK10418 174 VAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFN 230
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
9-220 |
2.33e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 72.45 E-value: 2.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 9 KVYGGKKVV-DNVSVTIPKGQITSFIGPNGAGKSTLLSMIS-RLTGkdsGLITvDGKEVSQWKSGDLAKKVSI---LKQS 83
Cdd:TIGR00956 770 KIKKEKRVIlNNVDGWVKPGTLTALMGASGAGKTTLLNVLAeRVTT---GVIT-GGDRLVNGRPLDSSFQRSIgyvQQQD 845
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 84 NHISlRLTVRELVSFG---RFPYSQGRlnAEDEKFVDEAISYMELEDmqhkYLHQLSG--------GQTQRAFIAMVIAQ 152
Cdd:TIGR00956 846 LHLP-TSTVRESLRFSaylRQPKSVSK--SEKMEYVEEVIKLLEMES----YADAVVGvpgeglnvEQRKRLTIGVELVA 918
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 261284556 153 NTEYIL-LDEPLNNLDMKHSVQIMKILRKLVtDLNKTIVIVIHD---INFASFysDYIVALKDGaieseGKT 220
Cdd:TIGR00956 919 KPKLLLfLDEPTSGLDSQTAWSICKLMRKLA-DHGQAILCTIHQpsaILFEEF--DRLLLLQKG-----GQT 982
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-226 |
4.09e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 69.82 E-value: 4.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGK---------KVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSG 71
Cdd:PRK15112 4 LLEVRNLSKTFRYRtgwfrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 72 DLAKKVSILKQ--SNHISLRLTVRELVSfgrFPYsqgRLN-----AEDEKFVDEAISYMEL-EDMQHKYLHQLSGGQTQR 143
Cdd:PRK15112 84 YRSQRIRMIFQdpSTSLNPRQRISQILD---FPL---RLNtdlepEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 144 AFIAMVIAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENI 223
Cdd:PRK15112 158 LGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADV 237
|
...
gi 261284556 224 IQS 226
Cdd:PRK15112 238 LAS 240
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
24-207 |
5.11e-14 |
|
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: 70.97 E-value: 5.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 24 IPK-GQITSFIGPNGAGKSTLLSMISrltgkdsGLIT---------VDGKEVSQWKSG--------DLAK---KVSILKQ 82
Cdd:COG1245 95 VPKkGKVTGILGPNGIGKSTALKILS-------GELKpnlgdydeePSWDEVLKRFRGtelqdyfkKLANgeiKVAHKPQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 83 snHI-----SLRLTVRELvsfgrfpysqgrLNAEDEK-FVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEY 156
Cdd:COG1245 168 --YVdlipkVFKGTVREL------------LEKVDERgKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADF 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 261284556 157 ILLDEPLNNLDMKHSVQIMKILRKLVTDlNKTIVIVIHDINFASFYSDYIV 207
Cdd:COG1245 234 YFFDEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDLAILDYLADYVH 283
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-226 |
6.42e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 70.16 E-value: 6.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKV----VDNVSVTIPKGQITSFIGPNGAGKST-------LLS-----MISRLTGKDSGLITVDGKE 64
Cdd:PRK11022 3 LLNVDKLSVHFGDESApfraVDRISYSVKQGEVVGIVGESGSGKSVsslaimgLIDypgrvMAEKLEFNGQDLQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 65 VSQWKSGDLA---------------------KKVSILKQSNHISLRLTVRELVSFGRFPYSQGRLNAedekfvdeaisym 123
Cdd:PRK11022 83 RRNLVGAEVAmifqdpmtslnpcytvgfqimEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDV------------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 124 eledmqhkYLHQLSGGQTQRAFIAMVIAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYS 203
Cdd:PRK11022 150 --------YPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAA 221
|
250 260
....*....|....*....|...
gi 261284556 204 DYIVALKDGAIESEGKTENIIQS 226
Cdd:PRK11022 222 HKIIVMYAGQVVETGKAHDIFRA 244
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
15-204 |
8.00e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 69.74 E-value: 8.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 15 KVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEV-----SQWKsgDLAKKVSILKQSNHISL- 88
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlgmkdDEWR--AVRSDIQMIFQDPLASLn 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 89 -RLTVRELVSFGRFPYsQGRLNAEDEKfvDEAISYME----LEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILLDEPL 163
Cdd:PRK15079 113 pRMTIGEIIAEPLRTY-HPKLSRQEVK--DRVKAMMLkvglLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPV 189
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 261284556 164 NNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSD 204
Cdd:PRK15079 190 SALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISD 230
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-212 |
8.59e-14 |
|
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: 70.24 E-value: 8.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRL--TGKDSGLITVDGKE-VSQWKSGDLAKKV 77
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPlKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 78 SILKQSNHISLRLTVRELVSFGRFPYSQGRLNAEDEKF--VDEAISYMELEDMQH-KYLHQLSGGQTQRAFIAMVIAQNT 154
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNEITLPGGRMAYNAMYlrAKNLLRELQLDADNVtRPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 261284556 155 EYILLDEPLNNLDMKHSVQIMKILRKLVTDlNKTIVIVIHDINFASFYSDYIVALKDG 212
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-218 |
9.91e-14 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 67.82 E-value: 9.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGK--KVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSI 79
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 80 LKQsNHISLRLTVR-ELVSFGRFpysqgrlnaeDEKFVDEAISYMELEDmqhkylhQLSGGQTQRAFIAMVIAQNTEYIL 158
Cdd:cd03369 87 IPQ-DPTLFSGTIRsNLDPFDEY----------SDEEIYGALRVSEGGL-------NLSQGQRQLLCLARALLKRPRVLV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 159 LDEPLNNLDMKHSVQIMKILRKLVTdlNKTIVIVIHDINFASFYsDYIVALKDGAIESEG 218
Cdd:cd03369 149 LDEATASIDYATDALIQKTIREEFT--NSTILTIAHRLRTIIDY-DKILVMDAGEVKEYD 205
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
14-226 |
1.56e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 69.81 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 14 KKVVDNVSVTIPKGQITSFIGPNGAGKSTLL-SMISRLtgkdsglitvdgkEVSqwkSGDLAKKVSI--LKQSNHIsLRL 90
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLqSLLSQF-------------EIS---EGRVWAERSIayVPQQAWI-MNA 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 91 TVRELVSFgrfpysqgrLNAEDEKFVDEAISYMELE-DMQH-----------KYLHqLSGGQTQRAFIAMVIAQNTEYIL 158
Cdd:PTZ00243 736 TVRGNILF---------FDEEDAARLADAVRVSQLEaDLAQlgggleteigeKGVN-LSGGQKARVSLARAVYANRDVYL 805
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 159 LDEPLNNLDMKHSVQIMK--ILRKLVtdlNKTIVIVIHDINFASfYSDYIVALKDGAIESEGKTENIIQS 226
Cdd:PTZ00243 806 LDDPLSALDAHVGERVVEecFLGALA---GKTRVLATHQVHVVP-RADYVVALGDGRVEFSGSSADFMRT 871
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-232 |
1.67e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 69.31 E-value: 1.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGdLAKKVSI- 79
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQLGIy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 80 -LKQSNHISLRLTVRELVSFGrFPYSQGRLNAEDEKF--------VDEAISYMELEDMQhkylhqlsggqtqrafiaMV- 149
Cdd:PRK15439 90 lVPQEPLLFPNLSVKENILFG-LPKRQASMQKMKQLLaalgcqldLDSSAGSLEVADRQ------------------IVe 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 150 ----IAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVtDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENIIQ 225
Cdd:PRK15439 151 ilrgLMRDSRILILDEPTASLTPAETERLFSRIRELL-AQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLST 229
|
....*..
gi 261284556 226 SNVLRGI 232
Cdd:PRK15439 230 DDIIQAI 236
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
14-225 |
1.92e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 69.36 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 14 KKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSILKQS---------N 84
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTpflfsdtvaN 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 85 HISLrltvrelvsfgrfpysqGRLNAEDEKfVDEAISYMELED----MQHKYLHQ-------LSGGQTQRAFIAMVIAQN 153
Cdd:PRK10789 408 NIAL-----------------GRPDATQQE-IEHVARLASVHDdilrLPQGYDTEvgergvmLSGGQKQRISIARALLLN 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 261284556 154 TEYILLDEPLNNLDMKHSVQIMKILRKLVTdlNKTIVIVIHDINfASFYSDYIVALKDGAIESEGKTENIIQ 225
Cdd:PRK10789 470 AEILILDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLS-ALTEASEILVMQHGHIAQRGNHDQLAQ 538
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-212 |
2.39e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 68.80 E-value: 2.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRL--TGKDSGLITVDGKEVSQWKSGDLAKK-V 77
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEELQASNIRDTERAgI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 78 SILKQSNHISLRLTVRELVSFGRFPYSQGRLNaeDEKFVDEAISYME---LEDMQHKYLHQLSGGQTQRAFIAMVIAQNT 154
Cdd:PRK13549 85 AIIHQELALVKELSVLENIFLGNEITPGGIMD--YDAMYLRAQKLLAqlkLDINPATPVGNLGLGQQQLVEIAKALNKQA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 261284556 155 EYILLDEPLNNLDMKHSVQIMKILRKLvTDLNKTIVIVIHDINFASFYSDYIVALKDG 212
Cdd:PRK13549 163 RLLILDEPTASLTESETAVLLDIIRDL-KAHGIACIYISHKLNEVKAISDTICVIRDG 219
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
14-211 |
2.70e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 66.91 E-value: 2.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 14 KKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISR--LTGKDSGLITVDGKEVSQwksgdlakKVSILkqsNHISLRLT 91
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVPDNQFGR--------EASLI---DAIGRKGD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 92 VRELVsfgrfpysqgrlnaedekfvdEAISYMELED---MQHKYlHQLSGGQTQRAFIAMVIAQNTEYILLDEPLNNLDM 168
Cdd:COG2401 112 FKDAV---------------------ELLNAVGLSDavlWLRRF-KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 261284556 169 KHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKD 211
Cdd:COG2401 170 QTAKRVARNLQKLARRAGITLVVATHHYDVIDDLQPDLLIFVG 212
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1-207 |
4.49e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 68.30 E-value: 4.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVvdNVSV-TIPKGQITSFIGPNGAGKSTLLSMISrltgkdsGLITVDGKEVsqwksgDLAKKVSI 79
Cdd:PRK13409 340 LVEYPDLTKKLGDFSL--EVEGgEIYEGEVIGIVGPNGIGKTTFAKLLA-------GVLKPDEGEV------DPELKISY 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 80 LKQSNHISLRLTVRELVSFGRFPYSqgrlnaeDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILL 159
Cdd:PRK13409 405 KPQYIKPDYDGTVEDLLRSITDDLG-------SSYYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLL 477
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 261284556 160 DEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIV 207
Cdd:PRK13409 478 DEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLM 525
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
14-194 |
5.27e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 68.15 E-value: 5.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 14 KKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMIS--RLTG-KDSGLITVDGKEVSQWKsgdlAKKVSILKQSNHISL-R 89
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAfrSPKGvKGSGSVLLNGMPIDAKE----MRAISAYVQQDDLFIpT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 90 LTVRELVSF------GRFPYSQGRLNAedekfVDEAISYMELEDMQHKYLHQ------LSGGQTQRAFIAMVIAQNTEYI 157
Cdd:TIGR00955 114 LTVREHLMFqahlrmPRRVTKKEKRER-----VDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLL 188
|
170 180 190
....*....|....*....|....*....|....*....
gi 261284556 158 LLDEPLNNLD--MKHSVqiMKILRKLVTDlNKTIVIVIH 194
Cdd:TIGR00955 189 FCDEPTSGLDsfMAYSV--VQVLKGLAQK-GKTIICTIH 224
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-213 |
5.98e-13 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 65.92 E-value: 5.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVY-----GGKK--VVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEvsQWksgdl 73
Cdd:COG4778 4 LLEVENLSKTFtlhlqGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDG--GW----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 74 akkVSILKQSNHISLRLTVREL--VS-FGRF-PysqgRLNAED-------EKFVDEAISYMELEDMqhkyLHQL------ 136
Cdd:COG4778 77 ---VDLAQASPREILALRRRTIgyVSqFLRViP----RVSALDvvaepllERGVDREEARARAREL----LARLnlperl 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 137 --------SGGQTQRAFIAMVIAQNTEYILLDEPLNNLDMKHSVQIMKILRKLvtdlnK----TIVIVIHDINFASFYSD 204
Cdd:COG4778 146 wdlppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-----KargtAIIGIFHDEEVREAVAD 220
|
....*....
gi 261284556 205 YIVALKDGA 213
Cdd:COG4778 221 RVVDVTPFS 229
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
27-212 |
7.94e-13 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 67.95 E-value: 7.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 27 GQITSFIGPNGAGKSTLLSMIS-RLTGkdsGLITVDGKEVSQWKSGDLAKKVSILKQSNHI-SLRLTVRELVSFGRFPys 104
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAgRKTG---GYIEGDIRISGFPKKQETFARISGYCEQNDIhSPQVTVRESLIYSAFL-- 980
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 105 qgRLNAE---DEK--FVDEAISYMELEDMQHKY-----LHQLSGGQTQRAFIAMVIAQNTEYILLDEPLNNLDMKHSVQI 174
Cdd:PLN03140 981 --RLPKEvskEEKmmFVDEVMELVELDNLKDAIvglpgVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIV 1058
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 261284556 175 MKILRKLVtDLNKTIVIVIH----DInFASFysDYIVALKDG 212
Cdd:PLN03140 1059 MRTVRNTV-DTGRTVVCTIHqpsiDI-FEAF--DELLLMKRG 1096
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
14-212 |
8.41e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 67.42 E-value: 8.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 14 KKVVDNVSVTIPKGQITSFIGPNGAGKS-TLLSMISRLTGKD----SGLITVDGKEV----SQWKSGDLAKKVSILKQSN 84
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLlhasEQTLRGVRGNKIAMIFQEP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 85 HISL------RLTVRELVSFGRfpySQGRLNAEDEkfvdeAISYME----------LEDmqhkYLHQLSGGQTQRAFIAM 148
Cdd:PRK15134 102 MVSLnplhtlEKQLYEVLSLHR---GMRREAARGE-----ILNCLDrvgirqaakrLTD----YPHQLSGGERQRVMIAM 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 261284556 149 VIAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDG 212
Cdd:PRK15134 170 ALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNG 233
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-226 |
8.49e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 67.57 E-value: 8.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 17 VDNVSVTIPKGQITSFIGPNGAGKS-TLLSMIsRLTGKDSGLITVDG------------------KEVSQWKSGDLAkkv 77
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSvTALALM-RLLEQAGGLVQCDKmllrrrsrqvielseqsaAQMRHVRGADMA--- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 78 sILKQSNHISLR--LTVRELVSFG-RFPYSQGRLNAEDE-KFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQN 153
Cdd:PRK10261 108 -MIFQEPMTSLNpvFTVGEQIAESiRLHQGASREEAMVEaKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCR 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 261284556 154 TEYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENIIQS 226
Cdd:PRK10261 187 PAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHA 259
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
20-217 |
1.04e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 65.57 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 20 VSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQW----KSGDLAKKVSILKQSNHISLRLTVREL 95
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeeaRAKLRAKHVGFVFQSFMLIPTLNALEN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 96 VsfgRFPysqGRLNAEDEKFV-DEAISYMELEDMQHKYLH---QLSGGQTQRAFIAMVIAQNTEYILLDEPLNNLDMKHS 171
Cdd:PRK10584 109 V---ELP---ALLRGESSRQSrNGAKALLEQLGLGKRLDHlpaQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTG 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 261284556 172 VQIMKILRKLVTDLNKTIVIVIHDINFASfYSDYIVALKDGAIESE 217
Cdd:PRK10584 183 DKIADLLFSLNREHGTTLILVTHDLQLAA-RCDRRLRLVNGQLQEE 227
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-218 |
1.51e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 66.03 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGK-----KVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITV--------------- 60
Cdd:PRK13631 21 ILRVKNLYCVFDEKqenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknnheli 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 61 ---DGKEVSQWKsgDLAKKVSILKQSNHISL-RLTVRELVSFGrfPYSQGRLNAEDEKfvdEAISYMELEDMQHKYLH-- 134
Cdd:PRK13631 101 tnpYSKKIKNFK--ELRRRVSMVFQFPEYQLfKDTIEKDIMFG--PVALGVKKSEAKK---LAKFYLNKMGLDDSYLErs 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 135 --QLSGGQTQRAFIAMVIAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDlNKTIVIVIHDINFASFYSDYIVALKDG 212
Cdd:PRK13631 174 pfGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKG 252
|
....*.
gi 261284556 213 AIESEG 218
Cdd:PRK13631 253 KILKTG 258
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
15-226 |
1.59e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 66.08 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 15 KVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTgKDSGLITVDGkevSQWKSGDLakkvsiLKQSNHISLRLTVRE 94
Cdd:COG4170 21 KAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGIT-KDNWHVTADR---FRWNGIDL------LKLSPRERRKIIGRE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 95 LVSFGRFPYSQGRLNAEDEKFVDEAISYMELEDM----------------------QHK-----YLHQLSGGQTQRAFIA 147
Cdd:COG4170 91 IAMIFQEPSSCLDPSAKIGDQLIEAIPSWTFKGKwwqrfkwrkkraiellhrvgikDHKdimnsYPHELTEGECQKVMIA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 148 MVIAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDG-AIESeGKTENIIQS 226
Cdd:COG4170 171 MAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGqTVES-GPTEQILKS 249
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
24-207 |
1.79e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 66.37 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 24 IPK-GQITSFIGPNGAGKSTLLSMISRLT----GKDSGLITVD-------GKEVSQWKSGDLAKKVSILKQSNHI----- 86
Cdd:PRK13409 95 IPKeGKVTGILGPNGIGKTTAVKILSGELipnlGDYEEEPSWDevlkrfrGTELQNYFKKLYNGEIKVVHKPQYVdlipk 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 87 SLRLTVRELvsfgrfpysqgrLNAEDEKFV-DEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILLDEPLNN 165
Cdd:PRK13409 175 VFKGKVREL------------LKKVDERGKlDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSY 242
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 261284556 166 LDMKHSVQIMKILRKLVTdlNKTIVIVIHDINFASFYSDYIV 207
Cdd:PRK13409 243 LDIRQRLNVARLIRELAE--GKYVLVVEHDLAVLDYLADNVH 282
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-227 |
2.00e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 66.51 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 17 VDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKevsqwksgdlakkVSILKQSNHISlRLTVRELV 96
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAYVPQQAWIQ-NDSLRENI 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 97 SFGRfpysqgRLNAEDEKFVDEAISYM-ELE--------DMQHKYLHqLSGGQTQRAFIAMVIAQNTEYILLDEPLNNLD 167
Cdd:TIGR00957 720 LFGK------ALNEKYYQQVLEACALLpDLEilpsgdrtEIGEKGVN-LSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 261284556 168 -------MKHSVQIMKILRklvtdlNKTIVIVIHDINFASfYSDYIVALKDGAIESEGKTENIIQSN 227
Cdd:TIGR00957 793 ahvgkhiFEHVIGPEGVLK------NKTRILVTHGISYLP-QVDVIIVMSGGKISEMGSYQELLQRD 852
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-167 |
3.49e-12 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 65.75 E-value: 3.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKK-VVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSIL 80
Cdd:PRK13657 335 VEFDDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 81 KQSNHISLRlTVRELVSFGRfPysqgrlNAEDEKFVD-----EAISYMELEDMQHKYL-----HQLSGGQTQRAFIAMVI 150
Cdd:PRK13657 415 FQDAGLFNR-SIEDNIRVGR-P------DATDEEMRAaaeraQAHDFIERKPDGYDTVvgergRQLSGGERQRLAIARAL 486
|
170
....*....|....*..
gi 261284556 151 AQNTEYILLDEPLNNLD 167
Cdd:PRK13657 487 LKDPPILILDEATSALD 503
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-197 |
7.94e-12 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 62.90 E-value: 7.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVY--GGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSI 79
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 80 LKQSNHIsLRLTVRE-LVSFGRfpYSQGRL-NAEDEKFVDEAISYME--LEDMQHKYLHQLSGGQTQRAFIAMVIAQNTE 155
Cdd:cd03244 83 IPQDPVL-FSGTIRSnLDPFGE--YSDEELwQALERVGLKEFVESLPggLDTVVEEGGENLSVGQRQLLCLARALLRKSK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 261284556 156 YILLDEPLNNLDMKHSVQIMKILRKLVTDlnKTIVIVIHDIN 197
Cdd:cd03244 160 ILVLDEATASVDPETDALIQKTIREAFKD--CTVLTIAHRLD 199
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-221 |
8.16e-12 |
|
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: 64.57 E-value: 8.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 6 NVSKVYGGKK-VVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTgKDSglitvDGKEVSQwksgdLAKKVSILKQSN 84
Cdd:TIGR03719 9 RVSKVVPPKKeILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVD-KDF-----NGEARPQ-----PGIKVGYLPQEP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 85 HISLRLTVRELVSFG--RFPYSQGRLNAEDEKFVDEAISYMEL--------EDMQHKYLHQ------------------- 135
Cdd:TIGR03719 78 QLDPTKTVRENVEEGvaEIKDALDRFNEISAKYAEPDADFDKLaaeqaelqEIIDAADAWDldsqleiamdalrcppwda 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 136 ----LSGGQTQRAFIAMVIAQNTEYILLDEPLNNLDMKhSVQimkILRKLVTDLNKTIVIVIHD---------------- 195
Cdd:TIGR03719 158 dvtkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAE-SVA---WLERHLQEYPGTVVAVTHDryfldnvagwileldr 233
|
250 260
....*....|....*....|....*....
gi 261284556 196 ---INFASFYSDYIVAlKDGAIESEGKTE 221
Cdd:TIGR03719 234 grgIPWEGNYSSWLEQ-KQKRLEQEEKEE 261
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
14-194 |
1.52e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 63.75 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 14 KKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMIS-RLTGKD-SGLITVDGKEVSQwksgDLAKKVSILKQSNHISLRLT 91
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANNRKPTK----QILKRTGFVTQDDILYPHLT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 92 VRE---LVSFGRFPYS---QGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILLDEPLNN 165
Cdd:PLN03211 157 VREtlvFCSLLRLPKSltkQEKILVAESVISELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSG 236
|
170 180
....*....|....*....|....*....
gi 261284556 166 LDMKHSVQIMKILRKLVTDlNKTIVIVIH 194
Cdd:PLN03211 237 LDATAAYRLVLTLGSLAQK-GKTIVTSMH 264
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-175 |
1.55e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 61.89 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQwksgDLA---KKV 77
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK----DLCtyqKQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 78 SILKQSNHISLRLTVRELVSFGrFPYSQGRLNaedekfVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYI 157
Cdd:PRK13540 77 CFVGHRSGINPYLTLRENCLYD-IHFSPGAVG------ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLW 149
|
170
....*....|....*...
gi 261284556 158 LLDEPLNNLDMKHSVQIM 175
Cdd:PRK13540 150 LLDEPLVALDELSLLTII 167
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-218 |
1.84e-11 |
|
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: 61.39 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMI-----SRLTGkdsGLITVDGKevsqwksgdlakk 76
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImghpkYEVTE---GEILFKGE------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 77 vSILKQSNHISLRLTVreLVSFGRFPYSQGRLNAEDEKFVDEAisymeledmqhkylhqLSGGQTQRAFIAMVIAQNTEY 156
Cdd:cd03217 65 -DITDLPPEERARLGI--FLAFQYPPEIPGVKNADFLRYVNEG----------------FSGGEKKRNEILQLLLLEPDL 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 261284556 157 ILLDEPLNNLDMKHSVQIMKILRKLVTDlNKTIVIVIHDINFASFY-SDYIVALKDGAIESEG 218
Cdd:cd03217 126 AILDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG 187
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
12-224 |
1.86e-11 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 62.90 E-value: 1.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 12 GGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTgKDSGLITVDG-----------------KEVSQWKSGDLA 74
Cdd:PRK15093 18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVT-KDNWRVTADRmrfddidllrlsprerrKLVGHNVSMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 75 KKVSILKQSNHISLRLtvreLVSFGRFPYS---QGRLNAEDEKFVD--EAISYMELEDMQHKYLHQLSGGQTQRAFIAMV 149
Cdd:PRK15093 97 EPQSCLDPSERVGRQL----MQNIPGWTYKgrwWQRFGWRKRRAIEllHRVGIKDHKDAMRSFPYELTEGECQKVMIAIA 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 261284556 150 IAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENII 224
Cdd:PRK15093 173 LANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELV 247
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-196 |
2.11e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 63.34 E-value: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 17 VDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEV---SQWKSGDLAKKVSILKQSNHISL--RLT 91
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlSPGKLQALRRDIQFIFQDPYASLdpRQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 92 VrelvsfgrfPYS-------QGRLNAED-EKFVDEAISYMELEDmQH--KYLHQLSGGQTQRAFIAMVIAQNTEYILLDE 161
Cdd:PRK10261 420 V---------GDSimeplrvHGLLPGKAaAARVAWLLERVGLLP-EHawRYPHEFSGGQRQRICIARALALNPKVIIADE 489
|
170 180 190
....*....|....*....|....*....|....*
gi 261284556 162 PLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDI 196
Cdd:PRK10261 490 AVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDM 524
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-233 |
2.60e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 63.20 E-value: 2.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVY-GGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSIL 80
Cdd:PRK10790 341 IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 81 KQsNHISLRLTVRELVSFGRfpysqgrlNAEDEKfVDEAISYMELEDMQHKY---LH--------QLSGGQTQRAFIAMV 149
Cdd:PRK10790 421 QQ-DPVVLADTFLANVTLGR--------DISEEQ-VWQALETVQLAELARSLpdgLYtplgeqgnNLSVGQKQLLALARV 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 150 IAQNTEYILLDEPLNNLDMKHSVQIMKILRkLVTDlNKTIVIVIHDINfASFYSDYIVALKDGAIESEGKTENIIQSnvl 229
Cdd:PRK10790 491 LVQTPQILILDEATANIDSGTEQAIQQALA-AVRE-HTTLVVIAHRLS-TIVEADTILVLHRGQAVEQGTHQQLLAA--- 564
|
....
gi 261284556 230 RGIY 233
Cdd:PRK10790 565 QGRY 568
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
12-221 |
3.23e-11 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 61.51 E-value: 3.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 12 GGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMIS-----RLTgkdSGLITVDGKEVSQWKSGDLAKKvSILKQSNH- 85
Cdd:TIGR01978 11 EDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAghpsyEVT---SGTILFKGQDLLELEPDERARA-GLFLAFQYp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 86 -----ISLRLTVRELVSFGRFPYSQGRLNAEDekFVDEAISYMELEDMQHKYLHQ-----LSGGQTQRAFIAMVIAQNTE 155
Cdd:TIGR01978 87 eeipgVSNLEFLRSALNARRSARGEEPLDLLD--FEKLLKEKLALLDMDEEFLNRsvnegFSGGEKKRNEILQMALLEPK 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 156 YILLDEPLNNLDmkhsVQIMKILRKLVTDL---NKTIVIVIHDIN-FASFYSDYIVALKDGAIESEGKTE 221
Cdd:TIGR01978 165 LAILDEIDSGLD----IDALKIVAEGINRLrepDRSFLIITHYQRlLNYIKPDYVHVLLDGRIVKSGDVE 230
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
13-212 |
4.29e-11 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 60.35 E-value: 4.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 13 GKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKD---SGLITVDGKEVSQWKSGDLAKKVSILKQSNHISLr 89
Cdd:cd03233 19 KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPT- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 90 LTVRELVSFGRfpysqgRLNAedekfvdeaisymeledmqHKYLHQLSGGQTQRAFIAMVIAQNTEYILLDEPLNNLDMK 169
Cdd:cd03233 98 LTVRETLDFAL------RCKG-------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSS 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 261284556 170 HSVQIMKILRKLVTDLNKTIVIVIH---DINFASFysDYIVALKDG 212
Cdd:cd03233 153 TALEILKCIRTMADVLKTTTFVSLYqasDEIYDLF--DKVLVLYEG 196
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-48 |
5.08e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 62.45 E-value: 5.08e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 261284556 2 IQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMIS 48
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIA 48
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-167 |
5.36e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 61.95 E-value: 5.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMIsrlTGKD----SGLITVDGKevsQWKSG----DL 73
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI---TGDHpqgySNDLTLFGR---RRGSGetiwDI 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 74 AKKVSILKQSNHISLRL--TVRELVSFGRFPySQGRLNA---EDEKFVDEAISYMELED-MQHKYLHQLSGGQTQRAFIA 147
Cdd:PRK10938 335 KKHIGYVSSSLHLDYRVstSVRNVILSGFFD-SIGIYQAvsdRQQKLAQQWLDILGIDKrTADAPFHSLSWGQQRLALIV 413
|
170 180
....*....|....*....|
gi 261284556 148 MVIAQNTEYILLDEPLNNLD 167
Cdd:PRK10938 414 RALVKHPTLLILDEPLQGLD 433
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
12-218 |
8.75e-11 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 60.08 E-value: 8.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 12 GGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISrltGKD-----SGLITVDGKEVSQWKSGDLAKKvsilkqsnHI 86
Cdd:COG0396 11 EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLM---GHPkyevtSGSILLDGEDILELSPDERARA--------GI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 87 SLR---------LTVRELVsfgRFPYSQGRLNAED-EKFVDEAISYMELEDMQHKYLHQ-----LSGGQTQRAFIAMVIA 151
Cdd:COG0396 80 FLAfqypveipgVSVSNFL---RTALNARRGEELSaREFLKLLKEKMKELGLDEDFLDRyvnegFSGGEKKRNEILQMLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 261284556 152 QNTEYILLDEPLNNLDmkhsVQIMKILRKLVTDL---NKTIVIVIHdinfasfYS---DYIVA-----LKDGAIESEG 218
Cdd:COG0396 157 LEPKLAILDETDSGLD----IDALRIVAEGVNKLrspDRGILIITH-------YQrilDYIKPdfvhvLVDGRIVKSG 223
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-214 |
9.42e-11 |
|
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: 58.98 E-value: 9.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 3 QVTNVSkvygGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGD-LAKKVSIL- 80
Cdd:cd03215 6 EVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDaIRAGIAYVp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 81 --KQSNHISLRLTVRELVSFGRFpysqgrlnaedekfvdeaisymeledmqhkylhqLSGGQTQRAFIAMVIAQNTEYIL 158
Cdd:cd03215 82 edRKREGLVLDLSVAENIALSSL----------------------------------LSGGNQQKVVLARWLARDPRVLI 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 261284556 159 LDEPLNNLDMKHSVQIMKILRKLvTDLNKTIVIVIHDINFASFYSDYIVALKDGAI 214
Cdd:cd03215 128 LDEPTRGVDVGAKAEIYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-217 |
1.13e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 60.95 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 3 QVTNVSKVYGGKkvVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKK-VSILK 81
Cdd:PRK09700 267 EVRNVTSRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKgMAYIT 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 82 QSNH---------ISLRLTVRELVSFGRFPYSQGRLNAEDEKFVDEAisymELEDMQHK------YLHQLSGGQTQRAFI 146
Cdd:PRK09700 345 ESRRdngffpnfsIAQNMAISRSLKDGGYKGAMGLFHEVDEQRTAEN----QRELLALKchsvnqNITELSGGNQQKVLI 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 261284556 147 AMVIAQNTEYILLDEPLNNLDMKHSVQIMKILRKLvTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESE 217
Cdd:PRK09700 421 SKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-198 |
1.17e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.12 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 3 QVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLS-MISRLTgKDSGLITVDGK-EVS---QWKS------- 70
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKlMLGQLQ-ADSGRIHCGTKlEVAyfdQHRAeldpekt 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 71 -----GDLAKKVSILKQSNHIslrltvrelvsfgrfpysqgrlnaedekfvdeaISYmeLEDmqhkYLHQ---------- 135
Cdd:PRK11147 400 vmdnlAEGKQEVMVNGRPRHV---------------------------------LGY--LQD----FLFHpkramtpvka 440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 261284556 136 LSGGQTQRAFIAMVIAQNTEYILLDEPLNNLDmkhsVQIMKILRKLVTDLNKTIVIVIHDINF 198
Cdd:PRK11147 441 LSGGERNRLLLARLFLKPSNLLILDEPTNDLD----VETLELLEELLDSYQGTVLLVSHDRQF 499
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-181 |
1.55e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.79 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEV-------SQwKSGdl 73
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtfngpksSQ-EAG-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 74 akkVSILKQSNHISLRLTVRELVSFGR-FPYSQGRLNAedEKFVDEA---ISYMELEDMQHKYLHQLSGGQTQRAFIAMV 149
Cdd:PRK10762 81 ---IGIIHQELNLIPQLTIAENIFLGReFVNRFGRIDW--KKMYAEAdklLARLNLRFSSDKLVGELSIGEQQMVEIAKV 155
|
170 180 190
....*....|....*....|....*....|..
gi 261284556 150 IAQNTEYILLDEPLNNLDMKHSVQIMKILRKL 181
Cdd:PRK10762 156 LSFESKVIIMDEPTDALTDTETESLFRVIREL 187
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
19-229 |
3.39e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 60.14 E-value: 3.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 19 NVSVTIPKGQITSFIGPNGAGKSTLLS-MISRLTGKDSGLITVDGKevsqwksgdlakkVSILKQSNHIsLRLTVRELVS 97
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGT-------------VAYVPQVSWI-FNATVRDNIL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 98 FGRfPYSQGRLnaedEKFVDEAISYMELEDMQHKYLHQ-------LSGGQTQRAFIAMVIAQNTEYILLDEPLNNLDMKH 170
Cdd:PLN03130 701 FGS-PFDPERY----ERAIDVTALQHDLDLLPGGDLTEigergvnISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHV 775
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 171 SVQIM-KILRKLVTdlNKTIVIVIHDINFASfYSDYIVALKDGAIESEGKTENIIQSNVL 229
Cdd:PLN03130 776 GRQVFdKCIKDELR--GKTRVLVTNQLHFLS-QVDRIILVHEGMIKEEGTYEELSNNGPL 832
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
17-196 |
6.54e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 58.20 E-value: 6.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 17 VDNVSVTIPKGQITSFIGPNGAGKS-TLLSMISRLT--GKDSGLITVDGKEVSQWKSGDL----AKKVSILKQSNHISLR 89
Cdd:PRK09473 32 VNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAanGRIGGSATFNGREILNLPEKELnklrAEQISMIFQDPMTSLN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 90 LTVR---ELVSFGRFPYSQGRLNAEDE--KFVDeAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILLDEPLN 164
Cdd:PRK09473 112 PYMRvgeQLMEVLMLHKGMSKAEAFEEsvRMLD-AVKMPEARKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTT 190
|
170 180 190
....*....|....*....|....*....|..
gi 261284556 165 NLDMKHSVQIMKILRKLVTDLNKTIVIVIHDI 196
Cdd:PRK09473 191 ALDVTVQAQIMTLLNELKREFNTAIIMITHDL 222
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-195 |
1.31e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.82 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 6 NVSKVYGGKKVV-DNVSVtipkgqitSF--------IGPNGAGKSTLLSMIsrltgkdSGLITVDGKEVsqWKSGDLakK 76
Cdd:PRK11819 11 RVSKVVPPKKQIlKDISL--------SFfpgakigvLGLNGAGKSTLLRIM-------AGVDKEFEGEA--RPAPGI--K 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 77 VSILKQSNHISLRLTVRELV--SFGRFPYSQGRLN------AEDEKFVDEAISYM-ELED-MQHKYLH------------ 134
Cdd:PRK11819 72 VGYLPQEPQLDPEKTVRENVeeGVAEVKAALDRFNeiyaayAEPDADFDALAAEQgELQEiIDAADAWdldsqleiamda 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 261284556 135 -----------QLSGGQTQRAFIAMVIAQNTEYILLDEPLNNLDMKhSVQimkILRKLVTDLNKTIVIVIHD 195
Cdd:PRK11819 152 lrcppwdakvtKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE-SVA---WLEQFLHDYPGTVVAVTHD 219
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-233 |
1.85e-09 |
|
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: 57.65 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 16 VVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSILKQSNHI---SLRLTV 92
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLfsgSLRMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 93 RelvsfgrfPYSQgrlNAEDEKFVDEAISYME--LEDMQHKYLHQ-------LSGGQTQRAFIAMVIAQNTEYILLDEPL 163
Cdd:TIGR00957 1381 D--------PFSQ---YSDEEVWWALELAHLKtfVSALPDKLDHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEAT 1449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 164 NNLDMKHSVQIMKILRKLVTDLnkTIVIVIHDINFASFYSDYIVaLKDGAIESEGKTENIIQSnvlRGIY 233
Cdd:TIGR00957 1450 AAVDLETDNLIQSTIRTQFEDC--TVLTIAHRLNTIMDYTRVIV-LDKGEVAEFGAPSNLLQQ---RGIF 1513
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-223 |
2.06e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 57.27 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGK----------------E 64
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDlivarlqqdpprnvegT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 65 VSQWKSGDLAKKVSILKQSNHISLRLTV----RELVSFGRFpysQGRLNAED----EKFVDEAISYMELEdmQHKYLHQL 136
Cdd:PRK11147 83 VYDFVAEGIEEQAEYLKRYHDISHLVETdpseKNLNELAKL---QEQLDHHNlwqlENRINEVLAQLGLD--PDAALSSL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 137 SGGQTQRAFIAMVIAQNTEYILLDEPLNNLDmkhsVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIES 216
Cdd:PRK11147 158 SGGWLRKAALGRALVSNPDVLLLDEPTNHLD----IETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVS 233
|
250
....*....|....*.
gi 261284556 217 ---------EGKTENI 223
Cdd:PRK11147 234 ypgnydqylLEKEEAL 249
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
34-168 |
2.08e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 56.01 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 34 GPNGAGKSTLLSMISRLTGKDSGLITVDGKEVsqwKSGDLAKKVSILKQSNHISLRLTVRELVSF-----GRFPysqgrl 108
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQIDGKTA---TRGDRSRFMAYLGHLPGLKADLSTLENLHFlcglhGRRA------ 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 109 naedEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILLDEPLNNLDM 168
Cdd:PRK13543 115 ----KQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
14-245 |
2.17e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 57.68 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 14 KKVVDNVSVTIPKGQITSFIGPNGAGKSTLLS-MISRLTGKDSGLITVDGKevsqwksgdlakkVSILKQSNHIsLRLTV 92
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGS-------------VAYVPQVSWI-FNATV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 93 RELVSFGRFPYSQGRLNAEDEKFVDEAISYMELEDMQH--KYLHQLSGGQTQRAFIAMVIAQNTEYILLDEPLNNLDMKH 170
Cdd:PLN03232 696 RENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEigERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHV 775
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 171 SVQIMKILRKlvTDLN-KTIVIVIHDINFASFYsDYIVALKDGAIESEGKTENIIQSNVL-------RGIYDMDIEIEEI 242
Cdd:PLN03232 776 AHQVFDSCMK--DELKgKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELSKSGSLfkklmenAGKMDATQEVNTN 852
|
...
gi 261284556 243 NDN 245
Cdd:PLN03232 853 DEN 855
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
15-196 |
2.20e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 56.90 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 15 KVVDNVSVTIPKGQITSFIGPNGAGKSTL---LSMISRLTgkdSGLITVDGKEV-----SQWKsgDLAKKVSILKQSNHI 86
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLarlLTMIETPT---GGELYYQGQDLlkadpEAQK--LLRQKIQIVFQNPYG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 87 SL--RLTVRELVSFgrfPYS-QGRLNAEDEKfvDEAISYMELEDMQ----HKYLHQLSGGQTQRAFIAMVIAQNTEYILL 159
Cdd:PRK11308 104 SLnpRKKVGQILEE---PLLiNTSLSAAERR--EKALAMMAKVGLRpehyDRYPHMFSGGQRQRIAIARALMLDPDVVVA 178
|
170 180 190
....*....|....*....|....*....|....*..
gi 261284556 160 DEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDI 196
Cdd:PRK11308 179 DEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDL 215
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
17-162 |
3.29e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 56.67 E-value: 3.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 17 VDNVSVTIPKGQITSFIGPNGAGKSTLLSMisrLTG---KDSGLITVDGKEVsqwKSGDLA--KKVSILKQSnhISL--R 89
Cdd:NF033858 282 VDHVSFRIRRGEIFGFLGSNGCGKSTTMKM---LTGllpASEGEAWLFGQPV---DAGDIAtrRRVGYMSQA--FSLygE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 90 LTVRE-LVSFGR-FpysqgRLNAED-EKFVDEAISYMELEDmqhkYLHQLSG----GQTQRAFIAMVIAQNTEYILLDEP 162
Cdd:NF033858 354 LTVRQnLELHARlF-----HLPAAEiAARVAEMLERFDLAD----VADALPDslplGIRQRLSLAVAVIHKPELLILDEP 424
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-223 |
4.14e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 56.95 E-value: 4.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKK--VVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSgDLAKKVS 78
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNIS-DVHQNMG 2015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 79 ILKQSNHISLRLTVRE-LVSFGRFpysQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYI 157
Cdd:TIGR01257 2016 YCPQFDAIDDLLTGREhLYLYARL---RGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLV 2092
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 261284556 158 LLDEPLNNLDMKHSVQIMKILRKLVTDlNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENI 223
Cdd:TIGR01257 2093 LLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-195 |
6.51e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 55.75 E-value: 6.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKKV-VDNVSVTIPKGQITSFIGPNGAGKSTlLSMIsrLTG---KDSGLITVDGKEVSQWKSGDLAKKV 77
Cdd:PRK10522 323 LELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKST-LAML--LTGlyqPQSGEILLDGKPVTAEQPEDYRKLF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 78 SILKQSNHIslrltvrelvsFGRFPYSQGRlnAEDEKFVDeaiSYMELEDMQHKYLH--------QLSGGQTQRAFIAMV 149
Cdd:PRK10522 400 SAVFTDFHL-----------FDQLLGPEGK--PANPALVE---KWLERLKMAHKLELedgrisnlKLSKGQKKRLALLLA 463
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 261284556 150 IAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHD 195
Cdd:PRK10522 464 LAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD 509
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-172 |
1.98e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 52.88 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKsGDLAKKVSIL 80
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQR-DEYHQDLLYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 81 KQSNHISLRLTVRELVSFgrfpYSQGRLNAEDEKFVDeAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILLD 160
Cdd:PRK13538 80 GHQPGIKTELTALENLRF----YQRLHGPGDDEALWE-ALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILD 154
|
170
....*....|..
gi 261284556 161 EPLNNLDmKHSV 172
Cdd:PRK13538 155 EPFTAID-KQGV 165
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
136-207 |
2.01e-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: 52.57 E-value: 2.01e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 261284556 136 LSGGQTQRAFIAMVIAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIV 207
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIH 143
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
6-214 |
2.08e-08 |
|
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: 54.44 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 6 NVSKVY-GGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQwksgdlakkvsiLKQSn 84
Cdd:COG5265 362 NVSFGYdPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRD------------VTQA- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 85 hiSLR-----------L---TVRELVSFgrfpysqGRLNAEDEKfVDEAIsymeledmQHKYLHQ--------------- 135
Cdd:COG5265 429 --SLRaaigivpqdtvLfndTIAYNIAY-------GRPDASEEE-VEAAA--------RAAQIHDfieslpdgydtrvge 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 136 ----LSGGQTQRAFIAMVIAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDlNKTIVI------VIHdinfasfySDY 205
Cdd:COG5265 491 rglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARG-RTTLVIahrlstIVD--------ADE 561
|
....*....
gi 261284556 206 IVALKDGAI 214
Cdd:COG5265 562 ILVLEAGRI 570
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
19-213 |
2.57e-08 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 53.03 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 19 NVSVTIPKGQITSFIGPNGAGKSTL----------------LSMISRltgkdSGLITVDGKEVsQWKSGdLAKKVSILKQ 82
Cdd:cd03270 13 NVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryvesLSAYAR-----QFLGQMDKPDV-DSIEG-LSPAIAIDQK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 83 SNHISLRLTV---RELVSFGRFPYSQGRLNAEDEKFVDEAISYMELEdmqhKYLHQLSGGQTQRAFIAMVIAQNTEYIL- 158
Cdd:cd03270 86 TTSRNPRSTVgtvTEIYDYLRLLFARVGIRERLGFLVDVGLGYLTLS----RSAPTLSGGEAQRIRLATQIGSGLTGVLy 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 261284556 159 -LDEPLNNLDMKHSVQIMKILRKLvTDLNKTIVIVIHD---INFAsfysDYIVALKDGA 213
Cdd:cd03270 162 vLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDedtIRAA----DHVIDIGPGA 215
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-215 |
3.13e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.02 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISrltgkdsglitvdgkevsqwksGDLAKkvsil 80
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLA----------------------GELAP----- 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 81 kQSNHISLRLTVRelvsFGRFPYSQGRLNAEDEKFVDEA--ISYMELEDMQHKYL--------------HQLSGGQTQRA 144
Cdd:PRK10636 365 -VSGEIGLAKGIK----LGYFAQHQLEFLRADESPLQHLarLAPQELEQKLRDYLggfgfqgdkvteetRRFSGGEKARL 439
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 261284556 145 FIAMVIAQNTEYILLDEPLNNLDMkhsvQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDGAIE 215
Cdd:PRK10636 440 VLALIVWQRPNLLLLDEPTNHLDL----DMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVE 506
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-225 |
3.77e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 53.47 E-value: 3.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 17 VDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGD-LAKK---VSILKQSNHISLRLTV 92
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDgLANGivyISEDRKRDGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 93 RE---LVSFGRFPYSQGRLNAEDEKfvdEAIS-YMELEDMQHKYLHQ----LSGGQTQRAFIAMVIAQNTEYILLDEPLN 164
Cdd:PRK10762 348 KEnmsLTALRYFSRAGGSLKHADEQ---QAVSdFIRLFNIKTPSMEQaiglLSGGNQQKVAIARGLMTRPKVLILDEPTR 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 261284556 165 NLDMKHSVQIMKILRKLVTDlNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENIIQ 225
Cdd:PRK10762 425 GVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTREQATQ 484
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-214 |
4.60e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 52.34 E-value: 4.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKD--SGLITVDGKEVSQWKSGDLAKK-- 76
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGESILDLEPEERAHLgi 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 77 -------VSILKQSNHISLRLtvrelvSFGRFPYSQGRLNAEDEKFVDEAISYMELEDMQHKYLHQ-----LSGGQTQRA 144
Cdd:CHL00131 87 flafqypIEIPGVSNADFLRL------AYNSKRKFQGLPELDPLEFLEIINEKLKLVGMDPSFLSRnvnegFSGGEKKRN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 261284556 145 FIAMVIAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDlNKTIVIVIHDINFASFYS-DYIVALKDGAI 214
Cdd:CHL00131 161 EILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTS-ENSIILITHYQRLLDYIKpDYVHVMQNGKI 230
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
19-219 |
4.99e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 51.17 E-value: 4.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 19 NVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKdsglitvdgkevsqwksgdlakkvsilkqsnhislRLTVRELVSF 98
Cdd:cd03238 13 NLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYASGK-----------------------------------ARLISFLPKF 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 99 GRFP-YSQGRLNAedekFVDEAISYMELEdmqhKYLHQLSGGQTQRAFIAMVIAQNTEYIL--LDEPLNNLDMKHSVQIM 175
Cdd:cd03238 58 SRNKlIFIDQLQF----LIDVGLGYLTLG----QKLSTLSGGELQRVKLASELFSEPPGTLfiLDEPSTGLHQQDINQLL 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 261284556 176 KILRKLVtDLNKTIVIVIHDINFASfYSDYIVALKDGAIESEGK 219
Cdd:cd03238 130 EVIKGLI-DLGNTVILIEHNLDVLS-SADWIIDFGPGSGKSGGK 171
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-194 |
7.20e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.11 E-value: 7.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKKVVD---NVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDG----KEVS--QWKSgd 72
Cdd:PTZ00265 383 IQFKNVRFHYDTRKDVEiykDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDINlkWWRS-- 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 73 lakKVSILKQ-----SNHISLRLTVrELVSFGRFPYSQGRLN--------------------AEDEKFVDEAISYMELED 127
Cdd:PTZ00265 461 ---KIGVVSQdpllfSNSIKNNIKY-SLYSLKDLEALSNYYNedgndsqenknkrnscrakcAGDLNDMSNTTDSNELIE 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 128 MQHKY----------------LH-------------------QLSGGQTQRAFIAMVIAQNTEYILLDEPLNNLDMKHSV 172
Cdd:PTZ00265 537 MRKNYqtikdsevvdvskkvlIHdfvsalpdkyetlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEY 616
|
250 260
....*....|....*....|..
gi 261284556 173 QIMKILRKLVTDLNKTIVIVIH 194
Cdd:PTZ00265 617 LVQKTINNLKGNENRITIIIAH 638
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
14-229 |
8.63e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 52.52 E-value: 8.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 14 KKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMI-SRLTGKDSGLITVDGKEVSQWKSGD-LAKKVSIL---KQSNHISL 88
Cdd:TIGR02633 273 RKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPVDIRNPAQaIRAGIAMVpedRKRHGIVP 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 89 RLTVRE---LVSFGRFPYsQGRLNAEDE-KFVDEAISYMELEdMQHKYL--HQLSGGQTQRAFIAMVIAQNTEYILLDEP 162
Cdd:TIGR02633 353 ILGVGKnitLSVLKSFCF-KMRIDAAAElQIIGSAIQRLKVK-TASPFLpiGRLSGGNQQKAVLAKMLLTNPRVLILDEP 430
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 261284556 163 LNNLDMKHSVQIMKILRKLVTDlNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENIIQSNVL 229
Cdd:TIGR02633 431 TRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLKGDFVNHALTQEQVL 496
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1-167 |
9.15e-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: 52.61 E-value: 9.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDsGLITVDGKE-----VSQWKS--GDL 73
Cdd:TIGR01271 1219 DVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSwnsvtLQTWRKafGVI 1297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 74 AKKVSILKQSNHISLRltvrelvsfgrfPYSQGRlNAEDEKFVDEAISYMELEDMQHKYLHQ-------LSGGQTQRAFI 146
Cdd:TIGR01271 1298 PQKVFIFSGTFRKNLD------------PYEQWS-DEEIWKVAEEVGLKSVIEQFPDKLDFVlvdggyvLSNGHKQLMCL 1364
|
170 180
....*....|....*....|.
gi 261284556 147 AMVIAQNTEYILLDEPLNNLD 167
Cdd:TIGR01271 1365 ARSILSKAKILLLDEPSAHLD 1385
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
53-233 |
9.74e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 52.72 E-value: 9.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 53 KDSGLITVDGKEVSQWKSGDLAKKVSILKQSNhISLRLTVRELVSFGRFPYSQgrlnaEDEKFVDEAISYME-LEDMQHK 131
Cdd:PTZ00265 1274 KNSGKILLDGVDICDYNLKDLRNLFSIVSQEP-MLFNMSIYENIKFGKEDATR-----EDVKRACKFAAIDEfIESLPNK 1347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 132 YL-------HQLSGGQTQRAFIAMVIAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIHDInfASF-YS 203
Cdd:PTZ00265 1348 YDtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI--ASIkRS 1425
|
170 180 190
....*....|....*....|....*....|....*
gi 261284556 204 DYIVAL----KDGA-IESEGKTENIIqsNVLRGIY 233
Cdd:PTZ00265 1426 DKIVVFnnpdRTGSfVQAHGTHEELL--SVQDGVY 1458
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-230 |
1.45e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 51.56 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 3 QVTNVSkvygGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGD-LAKKVSIL- 80
Cdd:COG1129 258 EVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRAGIAYVp 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 81 --KQSNHISLRLTVRE---LVSFGRFPySQGRLNAEDE-KFVDEAIsymelEDMQHKY--LHQ----LSGGQTQRAFIAM 148
Cdd:COG1129 334 edRKGEGLVLDLSIREnitLASLDRLS-RGGLLDRRRErALAEEYI-----KRLRIKTpsPEQpvgnLSGGNQQKVVLAK 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 149 VIAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDlNKTIVIV-------IHdinfasfYSDYIVALKDGAIESEGKTE 221
Cdd:COG1129 408 WLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVIsselpelLG-------LSDRILVMREGRIVGELDRE 479
|
....*....
gi 261284556 222 NIIQSNVLR 230
Cdd:COG1129 480 EATEEAIMA 488
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-198 |
1.90e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.40 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLsmisrltgKDSGLITVDG-------KEVSQWKSGDLA 74
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFL--------RYMAMHAIDGipkncqiLHVEQEVVGDDT 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 75 KKVSILKQSN---------HISLRLTVRELVSFGRFPYSQGRLNAEDEKfvdEAIS------YMELE------------- 126
Cdd:PLN03073 250 TALQCVLNTDiertqlleeEAQLVAQQRELEFETETGKGKGANKDGVDK---DAVSqrleeiYKRLElidaytaearaas 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 127 ---------DMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILLDEPLNNLDMkHSVQimkILRKLVTDLNKTIVIVIHDIN 197
Cdd:PLN03073 327 ilaglsftpEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL-HAVL---WLETYLLKWPKTFIVVSHARE 402
|
.
gi 261284556 198 F 198
Cdd:PLN03073 403 F 403
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-198 |
2.05e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 51.32 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAkkvsil 80
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETP------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 81 kqsnhiSLRLTVRELVSFGRFPYSQ--GRLNAEDEKFVDEAISYM--ELEDMQ--------HKYLHQL------------ 136
Cdd:PRK10636 75 ------ALPQPALEYVIDGDREYRQleAQLHDANERNDGHAIATIhgKLDAIDawtirsraASLLHGLgfsneqlerpvs 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 261284556 137 --SGGQTQRAFIAMVIAQNTEYILLDEPLNNLDMKHSVQIMKILRklvtDLNKTIVIVIHDINF 198
Cdd:PRK10636 149 dfSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLK----SYQGTLILISHDRDF 208
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-214 |
2.06e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.52 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVY--GGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVS 78
Cdd:PLN03232 1234 SIKFEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLS 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 79 ILKQSNhISLRLTVRelvsFGRFPYSQ----GRLNAEDEKFVDEAI--SYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQ 152
Cdd:PLN03232 1314 IIPQSP-VLFSGTVR----FNIDPFSEhndaDLWEALERAHIKDVIdrNPFGLDAEVSEGGENFSVGQRQLLSLARALLR 1388
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 261284556 153 NTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLnkTIVIVIHDINfASFYSDYIVALKDGAI 214
Cdd:PLN03232 1389 RSKILVLDEATASVDVRTDSLIQRTIREEFKSC--TMLVIAHRLN-TIIDCDKILVLSSGQV 1447
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
13-203 |
2.07e-07 |
|
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: 49.46 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 13 GKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLtgkdsglitvdgkevsqWKSGDlaKKVSILKQSNhiSLRLTV 92
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGL-----------------WPWGS--GRIGMPEGED--LLFLPQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 93 RelvsfgrfPY-SQGRLNaedekfvdEAISYmeledmqhKYLHQLSGGQTQRAFIAMVIAQNTEYILLDEPLNNLDMKHS 171
Cdd:cd03223 72 R--------PYlPLGTLR--------EQLIY--------PWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESE 127
|
170 180 190
....*....|....*....|....*....|..
gi 261284556 172 VQIMKILRKLVTdlnkTIVIVIHDINFASFYS 203
Cdd:cd03223 128 DRLYQLLKELGI----TVISVGHRPSLWKFHD 155
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-196 |
3.15e-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: 3.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVY--GGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDsGLITVDGKE-----VSQWKS--GD 72
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSwnsvpLQKWRKafGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 73 LAKKVSILKQSNHISLRltvrelvsfgrfPYSQGRlNAEDEKFVDEAISYMELEDMQHKYLHQ-------LSGGQTQRAF 145
Cdd:cd03289 82 IPQKVFIFSGTFRKNLD------------PYGKWS-DEEIWKVAEEVGLKSVIEQFPGQLDFVlvdggcvLSHGHKQLMC 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 261284556 146 IAMVIAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTDLnkTIVIVIHDI 196
Cdd:cd03289 149 LARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADC--TVILSEHRI 197
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-214 |
5.62e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.89 E-value: 5.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLIT-VDGKEV---SQWKSGDLAKKV 77
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKwSENANIgyyAQDHAYDFENDL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 78 SIL------KQSNHisLRLTVRELVsfGRFPYSQgrlnaedekfvDEAisymeledmqHKYLHQLSGGQTQRAFIAMVIA 151
Cdd:PRK15064 400 TLFdwmsqwRQEGD--DEQAVRGTL--GRLLFSQ-----------DDI----------KKSVKVLSGGEKGRMLFGKLMM 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 261284556 152 QNTEYILLDEPLNNLDMKhSVQimkilrKLVTDLNK---TIVIVIHDINFASFYSDYIVALKDGAI 214
Cdd:PRK15064 455 QKPNVLVMDEPTNHMDME-SIE------SLNMALEKyegTLIFVSHDREFVSSLATRIIEITPDGV 513
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-217 |
5.73e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.91 E-value: 5.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSkvygGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDlAKKVSIL- 80
Cdd:PRK11288 258 LRLDGLK----GPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRD-AIRAGIMl 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 81 -----KQSNHISLRlTVRELVSFG-RFPYSQGRLNAEDEKFVDEAISYMELEDMQHKYLHQ----LSGGQTQRAFIAMVI 150
Cdd:PRK11288 333 cpedrKAEGIIPVH-SVADNINISaRRHHLRAGCLINNRWEAENADRFIRSLNIKTPSREQlimnLSGGNQQKAILGRWL 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 261284556 151 AQNTEYILLDEPLNNLDMKHSVQIMKILRKLvTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESE 217
Cdd:PRK11288 412 SEDMKVILLDEPTRGIDVGAKHEIYNVIYEL-AAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGE 477
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
13-193 |
9.84e-07 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 49.04 E-value: 9.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 13 GKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMIsrltgkdSGLitvdgkevsqWKSGD------LAKKVSILKQSNHI 86
Cdd:COG4178 375 GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAI-------AGL----------WPYGSgriarpAGARVLFLPQRPYL 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 87 SLrLTVRELVSfgrfpYSQGRLNAEDEKfVDEAISYMELEDMQHKyLHQ-------LSGGQTQR-AFiAMVIAQNTEYIL 158
Cdd:COG4178 438 PL-GTLREALL-----YPATAEAFSDAE-LREALEAVGLGHLAER-LDEeadwdqvLSLGEQQRlAF-ARLLLHKPDWLF 508
|
170 180 190
....*....|....*....|....*....|....*
gi 261284556 159 LDEPLNNLDMKHSVQIMKILRKLvtdLNKTIVIVI 193
Cdd:COG4178 509 LDEATSALDEENEAALYQLLREE---LPGTTVISV 540
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
14-194 |
1.24e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.56 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 14 KKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSqwksgDLAKK-VSILKQSNHISLRLTV 92
Cdd:PRK13541 13 QKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNIN-----NIAKPyCTYIGHNLGLKLEMTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 93 RELVSFGRFPYSQGRLnaedekfVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILLDEPLNNLDMKHsv 172
Cdd:PRK13541 88 FENLKFWSEIYNSAET-------LYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKEN-- 158
|
170 180
....*....|....*....|..
gi 261284556 173 qimkilRKLVTDLnktivIVIH 194
Cdd:PRK13541 159 ------RDLLNNL-----IVMK 169
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-194 |
1.31e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 48.25 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMisrLTGKD-----SGLITVDGKEVSQWKSGDLAK 75
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSAT---LAGREdyevtGGTVEFKGKDLLELSPEDRAG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 76 K---------VSILKQSNHISLRLTVRELVSFgRFPYSQGRLNAEDekFVDEAIsymELEDMQHKYLHQ-----LSGGQT 141
Cdd:PRK09580 78 EgifmafqypVEIPGVSNQFFLQTALNAVRSY-RGQEPLDRFDFQD--LMEEKI---ALLKMPEDLLTRsvnvgFSGGEK 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 261284556 142 QRAFIAMVIAQNTEYILLDEPLNNLDmkhsVQIMKILRKLVTDL---NKTIVIVIH 194
Cdd:PRK09580 152 KRNDILQMAVLEPELCILDESDSGLD----IDALKIVADGVNSLrdgKRSFIIVTH 203
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
18-202 |
1.74e-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: 46.58 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 18 DNVSVTIPKGQITSFIGPNGAGKSTLLSMISrltgkdsglitvdgkevsqwksgdlakkvsilkqsnhislrltvreLVS 97
Cdd:cd03227 12 VPNDVTFGEGSLTIITGPNGSGKSTILDAIG----------------------------------------------LAL 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 98 FGRFPysqgRLNAEDEKFVDEAISYMELEDMQhkYLHQLSGGQTQRAFIAMVIA----QNTEYILLDEPLNNLDMKHSVQ 173
Cdd:cd03227 46 GGAQS----ATRRRSGVKAGCIVAAVSAELIF--TRLQLSGGEKELSALALILAlaslKPRPLYILDEIDRGLDPRDGQA 119
|
170 180 190
....*....|....*....|....*....|
gi 261284556 174 IMKILRKLVtdLNKTIVIVI-HDINFASFY 202
Cdd:cd03227 120 LAEAILEHL--VKGAQVIVItHLPELAELA 147
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
14-194 |
2.16e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.57 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 14 KKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLT----GKDSGLITVDG---KEVSQWKSGDLakkVSILKQSNHI 86
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTdgfhIGVEGVITYDGitpEEIKKHYRGDV---VYNAETDVHF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 87 SlRLTVRELVSFG---RFPYSQGRLNAEDEKFVDEAISYMELEDMQHKY--------LHQLSGGQTQRAFIAMVIAQNTE 155
Cdd:TIGR00956 151 P-HLTVGETLDFAarcKTPQNRPDGVSREEYAKHIADVYMATYGLSHTRntkvgndfVRGVSGGERKRVSIAEASLGGAK 229
|
170 180 190
....*....|....*....|....*....|....*....
gi 261284556 156 YILLDEPLNNLDMKHSVQIMKILRKLVTDLNKTIVIVIH 194
Cdd:TIGR00956 230 IQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIY 268
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-223 |
2.40e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 47.81 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLlSMISRLTGKDSGLitvdgkevSQWKSGDLAKKVSILK 81
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGR--------RPWRF*TWCANRRALR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 82 QS--NHISLRLTVRELVSFGRFPYSQGR---LNAEDEKF-VDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTE 155
Cdd:NF000106 85 RTig*HRPVR*GRRESFSGRENLYMIGR*ldLSRKDARArADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 261284556 156 YILLDEPLNNLDMKHSVQIMKILRKLVTDlNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENI 223
Cdd:NF000106 165 VLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
17-224 |
4.07e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 46.73 E-value: 4.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 17 VDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGkevsqwksgdlakKVSILKQSNHISLRLTVRELV 96
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-------------EVSVIAISAGLSGQLTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 97 SFGRFpySQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILLDEPLNNLDMKHSvqiMK 176
Cdd:PRK13546 107 EFKML--CMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFA---QK 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 261284556 177 ILRKL--VTDLNKTIVIVIHDINFASFYSDYIVALKDGAIESEGKTENII 224
Cdd:PRK13546 182 CLDKIyeFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL 231
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
6-65 |
9.77e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.94 E-value: 9.77e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 261284556 6 NVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRL--TGKDSGLITVDGKEV 65
Cdd:NF040905 6 GITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVypHGSYEGEILFDGEVC 67
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-182 |
1.20e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 45.69 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVS---KVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMI-SRLTGKDSGLITVDGKEVSQWKSGDLAKK 76
Cdd:PRK13549 259 ILEVRNLTawdPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLfGAYPGRWEGEIFIDGKPVKIRNPQQAIAQ 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 77 ----VSILKQSNHISLRLTVRE---LVSFGRFpYSQGRLNAEDE-KFVDEAISYMELEdMQHKYLH--QLSGGQTQRAFI 146
Cdd:PRK13549 339 giamVPEDRKRDGIVPVMGVGKnitLAALDRF-TGGSRIDDAAElKTILESIQRLKVK-TASPELAiaRLSGGNQQKAVL 416
|
170 180 190
....*....|....*....|....*....|....*.
gi 261284556 147 AMVIAQNTEYILLDEPLNNLDMKHSVQIMKILRKLV 182
Cdd:PRK13549 417 AKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLV 452
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
16-83 |
1.26e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 46.27 E-value: 1.26e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 261284556 16 VVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSILKQS 83
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQA 1321
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
18-144 |
2.30e-05 |
|
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that maintains replication in the presence of DNA damage. When replication is prematurely disrupted by DNA damage, several recF pathway gene products play critical roles processing the arrested replication fork, allowing it to resume and complete its task. This CD represents the nucleotide binding domain of RecF. RecF belongs to a large superfamily of ABC transporters 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 with 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: 213209 [Multi-domain] Cd Length: 270 Bit Score: 44.60 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 18 DNVSVTIPKGqITSFIGPNGAGKSTLLSMISRL-TGKdsGLITVDGKEVSQWK------SGDLAKKVSILKQS------- 83
Cdd:cd03242 13 AELELEFEPG-VTVLVGENAQGKTNLLEAISLLaTGK--SHRTSRDKELIRWGaeeakiSAVLERQGGELALEltirsgg 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 261284556 84 ------NHISLRlTVRELVsfgrfpysqGRLNA-----EDEKFVDEAISY------MELEDMQHKYLHQLSggQTQRA 144
Cdd:cd03242 90 grkarlNGIKVR-RLSDLL---------GVLNAvwfapEDLELVKGSPADrrrfldRLLGQLEPAYAHVLS--EYQKA 155
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
13-192 |
2.38e-05 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 44.46 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 13 GKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKevsqwksgdlakkVSILKQSNHIsLRLTV 92
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWI-MPGTI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 93 RELVSFGrFPYSQGRLNAedekfvdeAISYMELEDMQHKYLHQ-----------LSGGQTQRAFIAMVIAQNTEYILLDE 161
Cdd:cd03291 115 KENIIFG-VSYDEYRYKS--------VVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDS 185
|
170 180 190
....*....|....*....|....*....|..
gi 261284556 162 PLNNLDMKHSVQIM-KILRKLVTdlNKTIVIV 192
Cdd:cd03291 186 PFGYLDVFTEKEIFeSCVCKLMA--NKTRILV 215
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-196 |
2.43e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 43.85 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVsKVYGGKKVVDnvsvtIPKGqITSFIGPNGAGKSTLLSMI--------SRLTGKDSGLITVDGKEVS------- 66
Cdd:COG0419 5 LRLENF-RSYRDTETID-----FDDG-LNLIVGPNGAGKSTILEAIryalygkaRSRSKLRSDLINVGSEEASvelefeh 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 67 -------QWKSGDLAKkvsiLKQSNHISLRLTVRELVSFGRFPYSQGRLNAEDEKFVDEAISYMELEDMQHKYLHQ---- 135
Cdd:COG0419 78 ggkryriERRQGEFAE----FLEAKPSERKEALKRLLGLEIYEELKERLKELEEALESALEELAELQKLKQEILAQlsgl 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 261284556 136 -----LSGGQTQRAFIAMVIAqnteyILLDepLNNLDMKHSVQIMKILRKLvtdlnktiVIVIHDI 196
Cdd:COG0419 154 dpietLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEEL--------AIITHVI 204
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
21-225 |
4.96e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.85 E-value: 4.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 21 SVTIPKGQITSFIGPNGAGKSTLlsmiSR-LTGKdsgLITVDGKEVSQWKSG------DLAKKVSILKQSNHISLrLTVR 93
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSAL----ARaLAGE---LPLLSGERQSQFSHItrlsfeQLQKLVSDEWQRNNTDM-LSPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 94 ElVSFGRFPYSQGRLNAEDEKFVDEAISYMELEDMQHKYLHQLSGGQTQRAFIAMVIAQNTEYILLDEPLNNLDmkhsVQ 173
Cdd:PRK10938 95 E-DDTGRTTAEIIQDEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLD----VA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 261284556 174 IMKILRKLVTDLNK---TIVIVI---HDI-NFAsfysDYIVALKDGAIESEGKTENIIQ 225
Cdd:PRK10938 170 SRQQLAELLASLHQsgiTLVLVLnrfDEIpDFV----QFAGVLADCTLAETGEREEILQ 224
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
29-212 |
6.58e-05 |
|
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: 42.59 E-value: 6.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 29 ITSFIGPNGAGKSTLLSMIS-RLTG-KDSGLITVDGKEvsqwksgDLAKKVSILKQsnhISLRLT---------VRELVS 97
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEALKyALTGeLPPNSKGGAHDP-------KLIREGEVRAQ---VKLAFEnangkkytiTRSLAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 98 FGRFPY-SQGRLNAEdekfvdeaisymeLEDMqhkyLHQLSGGQTQ------RAFIAMVIAQNTEYILLDEPLNNLDMKH 170
Cdd:cd03240 94 LENVIFcHQGESNWP-------------LLDM----RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEN 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 261284556 171 -SVQIMKILRKLVTDLNKTIVIVIHDINFASFYSDYIVALKDG 212
Cdd:cd03240 157 iEESLAEIIEERKSQKNFQLIVITHDEELVDAADHIYRVEKDG 199
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
17-62 |
7.07e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 43.73 E-value: 7.07e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 261284556 17 VDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDG 62
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG 85
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
2-224 |
1.33e-04 |
|
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: 42.20 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 2 IQVTNVSKVYGG--KKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAKKVSI 79
Cdd:cd03288 20 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 80 LKQsNHISLRLTVrelvsfgrfpysqgRLNAEDEKFVDEAISYMELEDMQHKYL----------------HQLSGGQTQR 143
Cdd:cd03288 100 ILQ-DPILFSGSI--------------RFNLDPECKCTDDRLWEALEIAQLKNMvkslpggldavvteggENFSVGQRQL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 144 AFIAMVIAQNTEYILLDEPLNNLDMKHSvqimKILRKLVTD--LNKTIVIVIHDINfASFYSDYIVALKDGAIESEGKTE 221
Cdd:cd03288 165 FCLARAFVRKSSILIMDEATASIDMATE----NILQKVVMTafADRTVVTIAHRVS-TILDADLVLVLSRGILVECDTPE 239
|
...
gi 261284556 222 NII 224
Cdd:cd03288 240 NLL 242
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
13-65 |
2.56e-04 |
|
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.
Pssm-ID: 410880 [Multi-domain] Cd Length: 265 Bit Score: 41.39 E-value: 2.56e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 261284556 13 GKKVVDNVsVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDS---GLITVDGKEV 65
Cdd:cd01136 54 GVRAIDGL-LTCGEGQRIGIFAGSGVGKSTLLGMIARNTDADVnviALIGERGREV 108
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
18-50 |
3.72e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 37.58 E-value: 3.72e-04
10 20 30
....*....|....*....|....*....|...
gi 261284556 18 DNVSVTIPKGQITSFIGPNGAGKSTLLSMISRL 50
Cdd:pfam13555 13 DGHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTL 45
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
25-65 |
4.39e-04 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 40.75 E-value: 4.39e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 261284556 25 PKGQITSFIGPNGAGKSTLLSMISR-LTGKDSGLITVDGKEV 65
Cdd:COG3950 23 NPPRLTVLVGENGSGKTTLLEAIALaLSGLLSRLDDVKFRKL 64
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
13-67 |
5.16e-04 |
|
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho.
Pssm-ID: 425417 [Multi-domain] Cd Length: 212 Bit Score: 40.03 E-value: 5.16e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 261284556 13 GKKVVDNVsVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDS---GLITVDGKEVSQ 67
Cdd:pfam00006 1 GIRAIDGL-LPIGRGQRIGIFGGSGVGKTVLAGMIARQASADVvvyALIGERGREVRE 57
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
21-45 |
6.42e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 40.30 E-value: 6.42e-04
10 20
....*....|....*....|....*
gi 261284556 21 SVTIPKGQITSFIGPNGAGKSTLLS 45
Cdd:COG4637 15 DLELPLGPLTVLIGANGSGKSNLLD 39
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
26-198 |
7.32e-04 |
|
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: 38.89 E-value: 7.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 26 KGQITSFIGPNGAGKSTLLSMISRLTGKDS-GLITVDGkevsqwksgdlakkvsilkqsnhislrltvrelvsfgrfpys 104
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGgGVIYIDG------------------------------------------ 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 105 qgrlnaedEKFVDEAISYMELEDMQHKYlHQLSGGQTQRAFIAMVIAQNTEYILLDEPLNNLDMKHSVQIMKILRKLVTD 184
Cdd:smart00382 39 --------EDILEEVLDQLLLIIVGGKK-ASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLL 109
|
170
....*....|....*....
gi 261284556 185 L-----NKTIVIVIHDINF 198
Cdd:smart00382 110 LlksekNLTVILTTNDEKD 128
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-162 |
7.55e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 40.40 E-value: 7.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 3 QVTNVS-KVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDL-AKKVSil 80
Cdd:COG3845 259 EVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERrRLGVA-- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 81 kqsnHI---------SLRLTVRE---LVSFGRFPYSQG--------RLNAED--EKF------VDEAISymeledmqhky 132
Cdd:COG3845 337 ----YIpedrlgrglVPDMSVAEnliLGRYRRPPFSRGgfldrkaiRAFAEEliEEFdvrtpgPDTPAR----------- 401
|
170 180 190
....*....|....*....|....*....|
gi 261284556 133 lhQLSGGQTQRAFIAMVIAQNTEYILLDEP 162
Cdd:COG3845 402 --SLSGGNQQKVILARELSRDPKLLIAAQP 429
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
13-73 |
9.09e-04 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 40.09 E-value: 9.09e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 261284556 13 GKKVVDNVsVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITV---DGKEVSQWKSGDL 73
Cdd:PRK07721 145 GVRAIDSL-LTVGKGQRVGIFAGSGVGKSTLMGMIARNTSADLNVIALigeRGREVREFIERDL 207
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
19-95 |
9.82e-04 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 39.87 E-value: 9.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 19 NVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKD---SGLITVDGKEVSQW-----KSGDLAKKVSILKQSNHISL-R 89
Cdd:PRK07196 147 NGLLTIGKGQRVGLMAGSGVGKSVLLGMITRYTQADvvvVGLIGERGREVKEFiehslQAAGMAKSVVVAAPADESPLmR 226
|
....*.
gi 261284556 90 LTVREL 95
Cdd:PRK07196 227 IKATEL 232
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-198 |
1.06e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.88 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 1 MIQVTNVSKVYGGKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEvsqwksgdlakKVSIL 80
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNE-----------RLGKL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 81 KQSNHISLRLTVRELVSFGRFP-----------YSQGRLNAEDekfvdeaisYMELEDMQHKY----------------- 132
Cdd:PRK15064 70 RQDQFAFEEFTVLDTVIMGHTElwevkqerdriYALPEMSEED---------GMKVADLEVKFaemdgytaearagelll 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 133 -------LH-----QLSGGQTQRAFIAMVIAQNTEYILLDEPLNNLDMkHSVqimkilRKLVTDLNK---TIVIVIHDIN 197
Cdd:PRK15064 141 gvgipeeQHyglmsEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDI-NTI------RWLEDVLNErnsTMIIISHDRH 213
|
.
gi 261284556 198 F 198
Cdd:PRK15064 214 F 214
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
19-44 |
1.38e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.61 E-value: 1.38e-03
10 20
....*....|....*....|....*.
gi 261284556 19 NVSVTIPKGQITSFIGPNGAGKSTLL 44
Cdd:TIGR00630 626 NITVSIPLGLFTCITGVSGSGKSTLI 651
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
158-219 |
1.89e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.43 E-value: 1.89e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 261284556 158 LLDEPLNNLDMKHSVQIMKILRKLVTdLNKTIVIVIHDINFaSFYSDYIVALKDGAIESEGK 219
Cdd:PRK00635 1725 LLDEIATSLDNQQKSALLVQLRTLVS-LGHSVIYIDHDPAL-LKQADYLIEMGPGSGKTGGK 1784
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
19-209 |
2.16e-03 |
|
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: 38.36 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 19 NVSVTIPKGQITSFIGPNGAGKSTLLSMI------SRLTGKDsgliTVDGKEVSQWKSGDLAKKVSILK-------QSN- 84
Cdd:cd03271 13 NIDVDIPLGVLTCVTGVSGSGKSSLINDTlypalaRRLHLKK----EQPGNHDRIEGLEHIDKVIVIDQspigrtpRSNp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 85 --HISLRLTVREL---VSFGRfpysqgRLNAE--DEKF------------VDEAISYME-----------LEDMQHKYLH 134
Cdd:cd03271 89 atYTGVFDEIRELfceVCKGK------RYNREtlEVRYkgksiadvldmtVEEALEFFEnipkiarklqtLCDVGLGYIK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 135 ------QLSGGQTQR----AFIAMVIAQNTEYIlLDEPLNNLDMKHSVQIMKILRKLVtDLNKTIVIVIHDINFASfYSD 204
Cdd:cd03271 163 lgqpatTLSGGEAQRiklaKELSKRSTGKTLYI-LDEPTTGLHFHDVKKLLEVLQRLV-DKGNTVVVIEHNLDVIK-CAD 239
|
....*
gi 261284556 205 YIVAL 209
Cdd:cd03271 240 WIIDL 244
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
13-161 |
2.75e-03 |
|
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: 38.58 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 13 GKKVVDNVSVTIPKGQITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKevsqwksgdlaKKVSILKQSNHISLRlTV 92
Cdd:TIGR00954 464 GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAK-----------GKLFYVPQRPYMTLG-TL 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 93 RELVSfgrfpYSQGRLNAEDEKFVD-EAISYMELEDMQH------------KYLHQLSGGQTQRAFIAMVIAQNTEYILL 159
Cdd:TIGR00954 532 RDQII-----YPDSSEDMKRRGLSDkDLEQILDNVQLTHilereggwsavqDWMDVLSGGEKQRIAMARLFYHKPQFAIL 606
|
..
gi 261284556 160 DE 161
Cdd:TIGR00954 607 DE 608
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
13-66 |
3.27e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 38.23 E-value: 3.27e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 261284556 13 GKKVVDNVSVTIPKGQITSFIGPNGAGKSTL-LSMISRLTGKD-SGLITVDGKEVS 66
Cdd:NF040905 272 ERKVVDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGRSYGRNiSGTVFKDGKEVD 327
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
29-212 |
4.72e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 37.75 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 29 ITSFIGPNGAGKSTLLSMISRLTGKDSGLITVDGKEVSQWKSGDLAkkVSILKQSNHISLRLTVRELVSFG---RFPYSQ 105
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTDERSRNGGIGGIP--SLLNGIDPKEPIEFEISEFLEDGvryRYGLDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 261284556 106 GRLNAEDEKF-VDEAISYMELEDMQHKYLHQLSG--GQTQRAFIAMVIAQNTEYILLDEPLNNLDMKHSVQIMKILRKLV 182
Cdd:pfam13304 79 EREDVEEKLSsKPTLLEKRLLLREDSEEREPKFPpeAEELRLGLDVEERIELSLSELSDLISGLLLLSIISPLSFLLLLD 158
|
170 180 190
....*....|....*....|....*....|
gi 261284556 183 TDLNKTIVIVIHDINFASFYSDYIVALKDG 212
Cdd:pfam13304 159 EGLLLEDWAVLDLAADLALFPDLKELLQRL 188
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
19-43 |
4.79e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.08 E-value: 4.79e-03
10 20
....*....|....*....|....*
gi 261284556 19 NVSVTIPKGQITSFIGPNGAGKSTL 43
Cdd:COG0178 18 NIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| |
