|
Name |
Accession |
Description |
Interval |
E-value |
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-252 |
1.14e-124 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 355.12 E-value: 1.14e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 1 MISVNKVFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAML 80
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 81 PQMHDHQLDLTVKELIEFGRGPHKLWRGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLL 160
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGRYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 161 LDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVLCHEMFQHVFGIEVD 240
Cdd:COG1120 161 LDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVYGVEAR 240
|
250
....*....|....
gi 446549187 241 IFQ--GSDKPFFTP 252
Cdd:COG1120 241 VIEdpVTGRPLVLP 254
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-249 |
1.02e-99 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 291.60 E-value: 1.02e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 1 MISVNKVFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAML 80
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 81 PQMHDHQLDLTVKELIEFGRGPHKlwRGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLL 160
Cdd:COG4604 81 RQENHINSRLTVRELVAFGRFPYS--KGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 161 LDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVLCHEMFQHVFGIEVD 240
Cdd:COG4604 159 LDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEVLSDIYDTDIE 238
|
....*....
gi 446549187 241 IFQGSDKPF 249
Cdd:COG4604 239 VEEIDGKRI 247
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-250 |
4.62e-92 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 272.27 E-value: 4.62e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 1 MISVNKVFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAML 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 81 PQMHDHQLDLTVKELIEFGRGPH-KLWrGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVL 159
Cdd:PRK11231 82 PQHHLTPEGITVRELVAYGRSPWlSLW-GRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 160 LLDEPTTFLDIVHQLEVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVLCHEMFQHVFGIEV 239
Cdd:PRK11231 161 LLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVFDVEA 239
|
250
....*....|...
gi 446549187 240 DIFQG--SDKPFF 250
Cdd:PRK11231 240 EIHPEpvSGTPMC 252
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-243 |
7.00e-84 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 251.61 E-value: 7.00e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 1 MISVNKVFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAML 80
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 81 PQMHDHQLDLTVKELIEFGRGPHklwrGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTN--- 157
Cdd:PRK13548 82 PQHSSLSFPFTVEEVVAMGRAPH----GLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQLWEpdg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 158 ---VLLLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVLCHEMFQHV 234
Cdd:PRK13548 158 pprWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPETLRRV 237
|
....*....
gi 446549187 235 FGIEVDIFQ 243
Cdd:PRK13548 238 YGADVLVQP 246
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-254 |
1.06e-82 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 248.88 E-value: 1.06e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 1 MISVNKVFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAML 80
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 81 PQMHDHQLDLTVKELIEFGRGPHklwrGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQ------ 154
Cdd:COG4559 81 PQHSSLAFPFTVEEVVALGRAPH----GSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQlwepvd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 155 -RTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVLCHEMFQH 233
Cdd:COG4559 157 gGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELLER 235
|
250 260
....*....|....*....|...
gi 446549187 234 VFGIEVDIFQ--GSDKPFFTPKR 254
Cdd:COG4559 236 VYGADLRVLAhpEGGCPQVLPRA 258
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-220 |
2.65e-79 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 237.33 E-value: 2.65e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 3 SVNKVFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAMLPQ 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 83 mhdhqldltvkeliefgrgphklwrgrlnkedeeivdwALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLD 162
Cdd:cd03214 81 --------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446549187 163 EPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDG 220
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
3-242 |
3.71e-74 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 227.36 E-value: 3.71e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 3 SVNKVFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAMLPQ 82
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 83 MHDHQLDLTVKELIEFGRGPHKLWRGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLD 162
Cdd:PRK10575 93 QLPAAEGMTVRELVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 163 EPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVLCHEMFQHVFGIEVDIF 242
Cdd:PRK10575 173 EPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIYGIPMGIL 252
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-243 |
7.25e-74 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 225.74 E-value: 7.25e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 1 MISVNKVFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHtmksaDVAKQLAML 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR-----RARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 81 PQMHDHQLD--LTVKELIEFGRGPHKLWRGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNV 158
Cdd:COG1121 81 PQRAEVDWDfpITVRDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 159 LLLDEPTTFLDIVHQLEVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKLqYDGIPEEVLCHEMFQHVFGIE 238
Cdd:COG1121 161 LLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLV-AHGPPEEVLTPENLSRAYGGP 238
|
....*
gi 446549187 239 VDIFQ 243
Cdd:COG1121 239 VALLA 243
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
18-241 |
3.66e-71 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 219.86 E-value: 3.66e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 18 QNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAMLPQMHDHQLDLTVKELIE 97
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQELVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 98 FGRGPHKLWRGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVHQLEVM 177
Cdd:PRK10253 104 RGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446549187 178 ELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVLCHEMFQHVFGIEVDI 241
Cdd:PRK10253 184 ELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYGLRCMI 247
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-229 |
5.35e-66 |
|
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: 205.26 E-value: 5.35e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 2 ISVNKVFYA-HSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAML 80
Cdd:COG1122 1 IELENLSFSyPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 81 PQMHDHQL-DLTVKELIEFgrGPHKLwrgRLNKED-EEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNV 158
Cdd:COG1122 81 FQNPDDQLfAPTVEEDVAF--GPENL---GLPREEiRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446549187 159 LLLDEPTTFLDIVHQLEVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVLCHE 229
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-216 |
3.32e-61 |
|
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: 192.36 E-value: 3.32e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 3 SVNKVFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIhtmksADVAKQLAMLPQ 82
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL-----EKERKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 83 MH--DHQLDLTVKELIEFGRGPHKLWRGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLL 160
Cdd:cd03235 76 RRsiDRDFPISVRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446549187 161 LDEPTTFLDIVHQLEVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKL 216
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
9-215 |
2.80e-60 |
|
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: 189.99 E-value: 2.80e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 9 YAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAMLPQMHDHQL 88
Cdd:cd03225 9 YPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQNPDDQF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 89 -DLTVKELIEFGRGPhklwRGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTF 167
Cdd:cd03225 89 fGPTVEEEVAFGLEN----LGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAG 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446549187 168 LDIVHQLEVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGK 215
Cdd:cd03225 165 LDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-239 |
4.53e-56 |
|
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 upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 181.09 E-value: 4.53e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 2 ISVNKVF--YAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGksIHTMKSA---DVAKQ 76
Cdd:TIGR04520 1 IEVENVSfsYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEEnlwEIRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 77 LAMLPQMHDHQL-DLTVKELIEFG---RG-PHklwrgrlnKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMT 151
Cdd:TIGR04520 79 VGMVFQNPDNQFvGATVEDDVAFGlenLGvPR--------EEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 152 LAQRTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQySDRLLVLKRGKLQYDGIPEEVLCHEMF 231
Cdd:TIGR04520 151 LAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFSQVEL 229
|
....*...
gi 446549187 232 QHVFGIEV 239
Cdd:TIGR04520 230 LKEIGLDV 237
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
18-226 |
5.37e-56 |
|
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: 187.42 E-value: 5.37e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 18 QNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADV---AKQLAMLPQMHDHQLD--LTV 92
Cdd:COG1123 282 DDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLrelRRRVQMVFQDPYSSLNprMTV 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 93 KELIEFGRGPHKLWRGrlnKEDEEIVDWALSVTNL-EGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIV 171
Cdd:COG1123 362 GDIIAEPLRLHGLLSR---AERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVS 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446549187 172 HQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVL 226
Cdd:COG1123 439 VQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVF 493
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
24-252 |
6.85e-56 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 184.66 E-value: 6.85e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 24 IKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAMLPQMHDHQLDLTVKELIEFGRGPH 103
Cdd:PRK09536 26 VREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLSFEFDVRQVVEMGRTPH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 104 KLWRGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVHQLEVMELVKRL 183
Cdd:PRK09536 106 RSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRL 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446549187 184 NEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVLCHEMFQHVFGIEVDIFQ--GSDKPFFTP 252
Cdd:PRK09536 186 VDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFDARTAVGTdpATGAPTVTP 255
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
19-235 |
1.44e-54 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 176.02 E-value: 1.44e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 19 NMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTmKSADVAKQLAMLPQMHDHQLDLTVKELIEF 98
Cdd:COG1131 18 GVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGYVPQEPALYPDLTVRENLRF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 99 grgpHKLWRGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVHQLEVME 178
Cdd:COG1131 97 ----FARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446549187 179 LVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVLcHEMFQHVF 235
Cdd:COG1131 173 LLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELK-ARLLEDVF 227
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-225 |
1.65e-53 |
|
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: 173.52 E-value: 1.65e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 2 ISVNKVFYAHSERFQ-MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSAD---VAKQL 77
Cdd:cd03256 1 IEVENLSKTYPNGKKaLKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 78 AMLPQmhDHQL--DLTVKELIEFGR-GPHKLWR---GRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMT 151
Cdd:cd03256 81 GMIFQ--QFNLieRLSVLENVLSGRlGRRSTWRslfGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446549187 152 LAQRTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEV 225
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
7-226 |
7.45e-53 |
|
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: 179.33 E-value: 7.45e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 7 VFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQS---EGDIVLDGKSIHTMKSADVAKQLAMLPQM 83
Cdd:COG1123 12 VRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRRIGMVFQD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 84 HDHQLD-LTVKELIEFGrgphkLWRGRLNKED-EEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLL 161
Cdd:COG1123 92 PMTQLNpVTVGDQIAEA-----LENLGLSRAEaRARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446549187 162 DEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVL 226
Cdd:COG1123 167 DEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEIL 231
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-237 |
7.42e-52 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 169.17 E-value: 7.42e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 1 MISVNKVFYAHsERFQMqNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADvaKQLAML 80
Cdd:COG3840 1 MLRLDDLTYRY-GDFPL-RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--RPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 81 PQmhDHQL--DLTVKELIEFGRGPhklwRGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNV 158
Cdd:COG3840 77 FQ--ENNLfpHLTVAQNIGLGLRP----GLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 159 LLLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVLC---HEMFQHVF 235
Cdd:COG3840 151 LLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDgepPPALAAYL 230
|
..
gi 446549187 236 GI 237
Cdd:COG3840 231 GI 232
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-216 |
1.38e-50 |
|
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: 165.36 E-value: 1.38e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 4 VNKVFYAHSERFQ-MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVA----KQLA 78
Cdd:cd03255 6 LSKTYGGGGEKVQaLKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafrrRHIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 79 MLPQmhDHQL--DLTVKELIEFGrgphKLWRGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRT 156
Cdd:cd03255 86 FVFQ--SFNLlpDLTALENVELP----LLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 157 NVLLLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDiNQAAQYSDRLLVLKRGKL 216
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
4-219 |
2.55e-50 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 164.83 E-value: 2.55e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 4 VNKVFYAHSERFQ-MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAK----QLA 78
Cdd:COG1136 10 LTKSYGTGEGEVTaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARlrrrHIG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 79 MLPQmhDHQL--DLTVKELIEFgrgPHKLwRGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRT 156
Cdd:COG1136 90 FVFQ--FFNLlpELTALENVAL---PLLL-AGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446549187 157 NVLLLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDiNQAAQYSDRLLVLKRGKLQYD 219
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRIVSD 225
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-220 |
6.54e-49 |
|
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: 161.52 E-value: 6.54e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 4 VNKVFYAHSERFQ-MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVA---KQLAM 79
Cdd:cd03257 7 LSVSFPTGGGSVKaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKirrKEIQM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 80 LPQMHDHQLD--LTVKELIEFgrgPHKLWRGRLNKEDEEIVDWAL--SVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQR 155
Cdd:cd03257 87 VFQDPMSSLNprMTIGEQIAE---PLRIHGKLSKKEARKEAVLLLlvGVGLPEEVLNRYPHELSGGQRQRVAIARALALN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446549187 156 TNVLLLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDG 220
Cdd:cd03257 164 PKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-226 |
4.81e-48 |
|
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: 159.64 E-value: 4.81e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 1 MISVNKVFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTmKSADVAKQLAML 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK-EPREARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 81 PQMHDHQLDLTVKELIEFGRGPHKLWRGRLNKEDEEIVDWalsvTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLL 160
Cdd:COG4555 80 PDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIEL----LGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446549187 161 LDEPTTFLDIVHQLEVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVL 226
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELR 220
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
19-220 |
7.21e-48 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 158.07 E-value: 7.21e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 19 NMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSAD-----VAKQLAMLPQMhdhqldlTVK 93
Cdd:cd03259 18 DLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERrnigmVFQDYALFPHL-------TVA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 94 ELIEFGrgphkLWRGRLNKEDEEI-VDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVH 172
Cdd:cd03259 91 ENIAFG-----LKLRGVPKAEIRArVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446549187 173 QLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDG 220
Cdd:cd03259 166 REELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-216 |
1.67e-47 |
|
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: 158.43 E-value: 1.67e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 1 MISV---NKVFYAHSERFQM-QNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQ 76
Cdd:COG1124 1 MLEVrnlSVSYGQGGRRVPVlKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 77 LAMLPQ-----MHDHQldlTVKELIefgRGPhkLWRGRLNKEDEEIVDWALSVtNL-EGYEYRLLQSLSGGERQRAWIAM 150
Cdd:COG1124 81 VQMVFQdpyasLHPRH---TVDRIL---AEP--LRIHGLPDREERIAELLEQV-GLpPSFLDRYPHQLSGGQRQRVAIAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446549187 151 TLAQRTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKL 216
Cdd:COG1124 152 ALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
4-214 |
3.33e-47 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 157.94 E-value: 3.33e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 4 VNKVFYAHSERFQ-MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIhTMKSADVakqlAMLPQ 82
Cdd:COG1116 13 VSKRFPTGGGGVTaLDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV-TGPGPDR----GVVFQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 83 mhDHQL--DLTVKELIEFGRgphKLwRGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLL 160
Cdd:COG1116 88 --EPALlpWLTVLDNVALGL---EL-RGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446549187 161 LDEPttF--LDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRG 214
Cdd:COG1116 162 MDEP--FgaLDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-225 |
6.65e-47 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 156.51 E-value: 6.65e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 2 ISVNKVFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSAD---VAKQLA 78
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 79 MLPQmhDHQL--DLTVKELIEFGRGPHklwrGRLNKED-EEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQR 155
Cdd:cd03261 81 MLFQ--SGALfdSLTVFENVAFPLREH----TRLSEEEiREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 156 TNVLLLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEV 225
Cdd:cd03261 155 PELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-229 |
9.97e-47 |
|
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: 156.29 E-value: 9.97e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 1 MISVNKVFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSAD---VAKQL 77
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyeLRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 78 AMLPQ---MHDhqlDLTVKELIEFGrgphkLWR-GRLNKED-EEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTL 152
Cdd:COG1127 85 GMLFQggaLFD---SLTVFENVAFP-----LREhTDLSEAEiRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446549187 153 AQRTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVLCHE 229
Cdd:COG1127 157 ALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD 233
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-213 |
2.53e-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: 154.55 E-value: 2.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 4 VNKVFYAHSERFQ-MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIhtmksADVAKQLAMLPQ 82
Cdd:cd03293 6 VSKTYGGGGGAVTaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV-----TGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 83 mHDHQLD-LTVKELIEFGRgphKLwRGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLL 161
Cdd:cd03293 81 -QDALLPwLTVLDNVALGL---EL-QGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446549187 162 DEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKR 213
Cdd:cd03293 156 DEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSA 207
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-216 |
3.81e-46 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 153.82 E-value: 3.81e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 2 ISVNKVFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAMLP 81
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 82 QmhdhQLDL---TVKELIEFGrgphklWRGRLNKEDEEIVDWALSVTNL-EGYEYRLLQSLSGGERQRAWIAMTLAQRTN 157
Cdd:COG4619 81 Q----EPALwggTVRDNLPFP------FQLRERKFDRERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446549187 158 VLLLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKL 216
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
18-225 |
1.14e-45 |
|
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: 153.11 E-value: 1.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 18 QNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQ-----SEGDIVLDGKSIHTMKSADVA--KQLAMLPQmHDHQLDL 90
Cdd:cd03260 17 KDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVLElrRRVGMVFQ-KPNPFPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 91 TVKELIEFGRGPHKLWRgrlNKEDEEIVDWALSVTNLEGYEYRLLQ--SLSGGERQRAWIAMTLAQRTNVLLLDEPTTFL 168
Cdd:cd03260 96 SIYDNVAYGLRLHGIKL---KEELDERVEEALRKAALWDEVKDRLHalGLSGGQQQRLCLARALANEPEVLLLDEPTSAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446549187 169 DIVHQLEVMELVKRLNEEfgMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEV 225
Cdd:cd03260 173 DPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
18-209 |
2.32e-45 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 151.23 E-value: 2.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 18 QNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGksihtmksadvAKQLAMLPQMH--DHQLDLTVKEL 95
Cdd:NF040873 9 HGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRSevPDSLPLTVRDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 96 IEFGRGPHKLWRGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVHQLE 175
Cdd:NF040873 78 VAMGRWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRER 157
|
170 180 190
....*....|....*....|....*....|....
gi 446549187 176 VMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLL 209
Cdd:NF040873 158 IIALLAEEHAR-GATVVVVTHDLELVRRADPCVL 190
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
18-225 |
2.56e-45 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 155.64 E-value: 2.56e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 18 QNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADvaKQLAMLPQmhDHQL--DLTVKEL 95
Cdd:COG3842 22 DDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK--RNVGMVFQ--DYALfpHLTVAEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 96 IEFGrgphkLWRGRLNKED-EEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVHQL 174
Cdd:COG3842 98 VAFG-----LRMRGVPKAEiRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLRE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446549187 175 EVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEV 225
Cdd:COG3842 173 EMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
18-229 |
5.87e-45 |
|
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: 152.12 E-value: 5.87e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 18 QNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAK-------QLAMLPQmhdhqlDL 90
Cdd:COG0411 21 DDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARlgiartfQNPRLFP------EL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 91 TVKELIEFG---RGPHKLWRGRLN--------KEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVL 159
Cdd:COG0411 95 TVLENVLVAahaRLGRGLLAALLRlprarreeREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 160 LLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVLCHE 229
Cdd:COG0411 175 LLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVRADP 244
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
18-226 |
6.70e-45 |
|
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: 151.44 E-value: 6.70e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 18 QNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAK-------QLAMLPQmhdhqlDL 90
Cdd:cd03219 17 DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARlgigrtfQIPRLFP------EL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 91 TVKELIEFG---RGPHKLWRGRLNKEDEEIVDWALSV---TNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEP 164
Cdd:cd03219 91 TVLENVMVAaqaRTGSGLLLARARREEREARERAEELlerVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446549187 165 TTFLDIVHQLEVMELVKRLNeEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVL 226
Cdd:cd03219 171 AAGLNPEETEELAELIRELR-ERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVR 231
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-228 |
1.07e-44 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 152.09 E-value: 1.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 2 ISVNKVF--YAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAM 79
Cdd:PRK13635 6 IRVEHISfrYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 80 LPQMHDHQ-LDLTVKELIEFGRGPHKLWRgrlnKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNV 158
Cdd:PRK13635 86 VFQNPDNQfVGATVQDDVAFGLENIGVPR----EEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 159 LLLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQySDRLLVLKRGKLQYDGIPEEVLCH 228
Cdd:PRK13635 162 IILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-220 |
2.14e-44 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 149.43 E-value: 2.14e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 1 MISVNKVFYAHSERFQ-MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAK---Q 76
Cdd:COG2884 1 MIRFENVSKRYPGGREaLSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYlrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 77 LAMLPQmhDHQL--DLTVKELIEF-----GRgPHKLWRGRLnkedEEIVDWalsVtNLEGYEYRLLQSLSGGERQRAWIA 149
Cdd:COG2884 81 IGVVFQ--DFRLlpDRTVYENVALplrvtGK-SRKEIRRRV----REVLDL---V-GLSDKAKALPHELSGGEQQRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446549187 150 MTLAQRTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDG 220
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-246 |
5.71e-44 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 149.98 E-value: 5.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 1 MISVNKVFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQS--------EGDIVLDGKSIHTMKSAD 72
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 73 VAKQLAMLPQMHDHQLDLTVKELIEFGRGPHKLWRGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTL 152
Cdd:PRK13547 81 LARLRAVLPQAAQPAFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 153 AQ---------RTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPE 223
Cdd:PRK13547 161 AQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPA 240
|
250 260
....*....|....*....|...
gi 446549187 224 EVLCHEMFQHVFGIEVDIFQGSD 246
Cdd:PRK13547 241 DVLTPAHIARCYGFAVRLVDAGD 263
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
18-226 |
7.09e-44 |
|
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: 148.35 E-value: 7.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 18 QNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQ-LAMLPQmhDHQL--DLTVKE 94
Cdd:cd03224 17 FGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYVPE--GRRIfpELTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 95 LIEFGrgphklWRGRLNKEDEEIVDWALSV-TNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFL--DIV 171
Cdd:cd03224 95 NLLLG------AYARRRAKRKARLERVYELfPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLapKIV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446549187 172 HqlEVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVL 226
Cdd:cd03224 169 E--EIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELL 220
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
9-215 |
8.32e-44 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 145.85 E-value: 8.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 9 YAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAMLPQmhdhql 88
Cdd:cd00267 7 FRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 89 dltvkeliefgrgphklwrgrlnkedeeivdwalsvtnlegyeyrllqsLSGGERQRAWIAMTLAQRTNVLLLDEPTTFL 168
Cdd:cd00267 81 -------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGL 111
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446549187 169 DIVHQLEVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGK 215
Cdd:cd00267 112 DPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-215 |
9.71e-44 |
|
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: 146.56 E-value: 9.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 4 VNKVFyahSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVA--KQLAMLP 81
Cdd:cd03229 6 VSKRY---GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPlrRRIGMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 82 QmhDHQL--DLTVKELIEFGrgphklwrgrlnkedeeivdwalsvtnlegyeyrllqsLSGGERQRAWIAMTLAQRTNVL 159
Cdd:cd03229 83 Q--DFALfpHLTVLENIALG--------------------------------------LSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446549187 160 LLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGK 215
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
21-253 |
3.21e-43 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 147.29 E-value: 3.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 21 NVHIKAGEVVSLIGPNGSGKSTLLRLIARLLkQSEGDIVLDGKSIHTMKSADVAKQLAMLPQMHDHQLDLTVKELIEFGR 100
Cdd:COG4138 16 SAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAYLSQQQSPPFAMPVFQYLALHQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 101 gPHKLWRGRLNKEDEEIVDwALSVTNLEGyeyRLLQSLSGGERQRAWIAMTLAQ---RTN----VLLLDEPTTFLDIVHQ 173
Cdd:COG4138 95 -PAGASSEAVEQLLAQLAE-ALGLEDKLS---RPLTQLSGGEWQRVRLAAVLLQvwpTINpegqLLLLDEPMNSLDVAQQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 174 LEVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVLCHEMFQHVFGIEVDIFQGSDKPFFTPK 253
Cdd:COG4138 170 AALDRLLRELCQQ-GITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVFGVKFRRLEVEGHRWLIPT 248
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
17-225 |
4.31e-43 |
|
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: 146.61 E-value: 4.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 17 MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTM-----KSADVAKQLAMLPQMhdhqldlT 91
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLpphkrPVNTVFQNYALFPHL-------T 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 92 VKELIEFGrgphkLWRGRLNKED-EEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDI 170
Cdd:cd03300 89 VFENIAFG-----LRLKKLPKAEiKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446549187 171 VHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEV 225
Cdd:cd03300 164 KLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
2-220 |
2.66e-42 |
|
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: 143.79 E-value: 2.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 2 ISVNKVFYahseRFQMQNM--NVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADvaKQLAM 79
Cdd:cd03298 1 VRLDKIRF----SYGEQPMhfDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 80 LPQMHDHQLDLTVKELIEFGRGPhklwRGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVL 159
Cdd:cd03298 75 LFQENNLFAHLTVEQNVGLGLSP----GLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446549187 160 LLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDG 220
Cdd:cd03298 151 LLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
18-226 |
2.30e-41 |
|
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: 142.04 E-value: 2.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 18 QNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQ-LAMLPQmhDHQL--DLTVKE 94
Cdd:COG0410 20 HGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgIGYVPE--GRRIfpSLTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 95 LIEFGrgphkLWRGRLNKEDEEIVDWAlsvtnlegYEY--RLLQ-------SLSGGERQRAWIAMTLAQRTNVLLLDEPT 165
Cdd:COG0410 98 NLLLG-----AYARRDRAEVRADLERV--------YELfpRLKErrrqragTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446549187 166 TFL--DIVHqlEVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVL 226
Cdd:COG0410 165 LGLapLIVE--EIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELL 224
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
19-216 |
3.18e-41 |
|
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: 139.84 E-value: 3.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 19 NMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTmKSADVAKQLAMLPQMHDHQLDLTVKELIEf 98
Cdd:cd03230 18 DISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLPEEPSLYENLTVRENLK- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 99 grgphklwrgrlnkedeeivdwalsvtnlegyeyrllqsLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVHQLEVME 178
Cdd:cd03230 96 ---------------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWE 136
|
170 180 190
....*....|....*....|....*....|....*...
gi 446549187 179 LVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKL 216
Cdd:cd03230 137 LLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-226 |
1.43e-40 |
|
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: 148.44 E-value: 1.43e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 2 ISVNKV-F-YAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAM 79
Cdd:COG2274 474 IELENVsFrYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 80 LPQmHDHQLDLTVKELIefgrgphKLWRGRLNkeDEEIVdWALSVTNLE--------GYEYRLL---QSLSGGERQRAWI 148
Cdd:COG2274 554 VLQ-DVFLFSGTIRENI-------TLGDPDAT--DEEII-EAARLAGLHdfiealpmGYDTVVGeggSNLSGGQRQRLAI 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 149 AMTLAQRTNVLLLDEPTTFLDIVHQLEVMELVKRLNEefGMTIIMVLHD---INQAaqysDRLLVLKRGKLQYDGIPEEV 225
Cdd:COG2274 623 ARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRlstIRLA----DRIIVLDKGRIVEDGTHEEL 696
|
.
gi 446549187 226 L 226
Cdd:COG2274 697 L 697
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
13-225 |
4.38e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 140.57 E-value: 4.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 13 ERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSI--HTMKSADVAKQLAMLPQMHDHQL-D 89
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQYPEYQLfE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 90 LTVKELIEFGrgPHklwrgRLNKEDEEIVDWALSVTNLEGYEYRLLQ-----SLSGGERQRAWIAMTLAQRTNVLLLDEP 164
Cdd:PRK13637 99 ETIEKDIAFG--PI-----NLGLSEEEIENRVKRAMNIVGLDYEDYKdkspfELSGGQKRRVAIAGVVAMEPKILILDEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446549187 165 TTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEV 225
Cdd:PRK13637 172 TAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-251 |
4.87e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 140.25 E-value: 4.87e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 1 MISVNKVFYAH---SERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQL 77
Cdd:PRK13650 4 IIEVKNLTFKYkedQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 78 AMLPQMHDHQ-LDLTVKELIEFG---RG-PHKLWRGRlnkedeeiVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTL 152
Cdd:PRK13650 84 GMVFQNPDNQfVGATVEDDVAFGlenKGiPHEEMKER--------VNEALELVGMQDFKEREPARLSGGQKQRVAIAGAV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 153 AQRTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAqYSDRLLVLKRGKLQYDGIPEEvlchemfq 232
Cdd:PRK13650 156 AMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRE-------- 226
|
250 260
....*....|....*....|
gi 446549187 233 hVFGIEVDIFQ-GSDKPFFT 251
Cdd:PRK13650 227 -LFSRGNDLLQlGLDIPFTT 245
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
3-228 |
7.64e-40 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 138.59 E-value: 7.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 3 SVNKVFyaHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTM-------KSADVAK 75
Cdd:cd03295 5 NVTKRY--GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQdpvelrrKIGYVIQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 76 QLAMLPQMHDHQLDLTVKELIEFGRgphklwrgrlnKEDEEIVDWALSVTNLEGYEY--RLLQSLSGGERQRAWIAMTLA 153
Cdd:cd03295 83 QIGLFPHMTVEENIALVPKLLKWPK-----------EKIRERADELLALVGLDPAEFadRYPHELSGGQQQRVGVARALA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446549187 154 QRTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVLCH 228
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-215 |
9.28e-40 |
|
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: 135.97 E-value: 9.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 2 ISVNKVFYAHSERFQM--QNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAM 79
Cdd:cd03228 1 IEFKNVSFSYPGRPKPvlKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 80 LPQmHDHQLDLTVKEliefgrgphklwrgrlnkedeeivdwalsvtNLegyeyrllqsLSGGERQRAWIAMTLAQRTNVL 159
Cdd:cd03228 81 VPQ-DPFLFSGTIRE-------------------------------NI----------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446549187 160 LLDEPTTFLDIVHQLEVMELVKRLNEefGMTIIMVLHDINQAAQYsDRLLVLKRGK 215
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIRDA-DRIIVLDDGR 171
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
18-225 |
1.19e-39 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 140.98 E-value: 1.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 18 QNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADvaKQLAMLPQ---MHDHqldLTVKE 94
Cdd:COG3839 20 KDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD--RNIAMVFQsyaLYPH---MTVYE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 95 LIEFGrgphkLWRGRLNKED-EEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDivHQ 173
Cdd:COG3839 95 NIAFP-----LKLRKVPKAEiDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLD--AK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446549187 174 LEV---MELvKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEV 225
Cdd:COG3839 168 LRVemrAEI-KRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
15-228 |
1.54e-39 |
|
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: 137.47 E-value: 1.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 15 FQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADvaKQLAMLPQmhDHQL--DLTV 92
Cdd:cd03299 13 FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK--RDISYVPQ--NYALfpHMTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 93 KELIEFGRgphKLwRGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVH 172
Cdd:cd03299 89 YKNIAYGL---KK-RKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446549187 173 QLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVLCH 228
Cdd:cd03299 165 KEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-226 |
1.66e-39 |
|
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: 144.13 E-value: 1.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 2 ISVNKV-FYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAML 80
Cdd:COG4988 337 IELEDVsFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 81 PQmHDHQLDLTVKELIEFGRGphklwrgrlNKEDEEIVDwALSVTNL--------EGYEYRLLQS---LSGGERQRAWIA 149
Cdd:COG4988 417 PQ-NPYLFAGTIRENLRLGRP---------DASDEELEA-ALEAAGLdefvaalpDGLDTPLGEGgrgLSGGQAQRLALA 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446549187 150 MTLAQRTNVLLLDEPTTFLDIVHQLEVMELVKRLNEefGMTIIMVLHDINQAAQYsDRLLVLKRGKLQYDGIPEEVL 226
Cdd:COG4988 486 RALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQA-DRILVLDDGRIVEQGTHEELL 559
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-225 |
1.69e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 135.98 E-value: 1.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 1 MISVNKVFYAHSERFQ-MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSA--DVAKQL 77
Cdd:PRK13639 1 ILETRDLKYSYPDGTEaLKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSllEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 78 AMLPQMHDHQL-DLTVKELIEFGrgPHKLwrgRLNKED-EEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQR 155
Cdd:PRK13639 81 GIVFQNPDDQLfAPTVEEDVAFG--PLNL---GLSKEEvEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 156 TNVLLLDEPTTFLDIVHQLEVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEV 225
Cdd:PRK13639 156 PEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
17-234 |
2.50e-38 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 134.45 E-value: 2.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 17 MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSAD---------VAKQLAMLPQMhdhq 87
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlirqeagmVFQQFYLFPHL---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 88 ldlTVKELIEFgrGPHKLwRGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTF 167
Cdd:PRK09493 93 ---TALENVMF--GPLRV-RGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446549187 168 LDIVHQLEVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVL-------CHEMFQHV 234
Cdd:PRK09493 167 LDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIknppsqrLQEFLQHV 239
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
26-238 |
2.74e-38 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 133.82 E-value: 2.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 26 AGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSihtmkSADVAKQLAMLPQMHDHQLD--LTVKELIEFGRGPH 103
Cdd:TIGR03771 5 KGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGAS-----PGKGWRHIGYVPQRHEFAWDfpISVAHTVMSGRTGH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 104 KLWRGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVHQLEVMELVKRL 183
Cdd:TIGR03771 80 IGWLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFIEL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446549187 184 NEEfGMTIIMVLHDINQAAQYSDRLLVLKrGKLQYDGIPEEVLCHEMFQHVFGIE 238
Cdd:TIGR03771 160 AGA-GTAILMTTHDLAQAMATCDRVVLLN-GRVIADGTPQQLQDPAPWMTTFGVS 212
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
18-166 |
1.03e-37 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 130.08 E-value: 1.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 18 QNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAMLPQMHDHQLDLTVKELIE 97
Cdd:pfam00005 2 KNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENLR 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446549187 98 FGRGPHKLwrgrLNKEDEEIVDWALSVTNLEGYEYRLLQ----SLSGGERQRAWIAMTLAQRTNVLLLDEPTT 166
Cdd:pfam00005 82 LGLLLKGL----SKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-225 |
1.31e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 133.67 E-value: 1.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 1 MISVNKVFYAHS------ERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSA-DV 73
Cdd:PRK13633 4 MIKCKNVSYKYEsneestEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 74 AKQLAMLPQMHDHQLDLT-VKELIEFGrgPHKLwrGRLNKEDEEIVDWALSVTNLegYEYRLLQS--LSGGERQRAWIAM 150
Cdd:PRK13633 84 RNKAGMVFQNPDNQIVATiVEEDVAFG--PENL--GIPPEEIRERVDESLKKVGM--YEYRRHAPhlLSGGQKQRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446549187 151 TLAQRTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQySDRLLVLKRGKLQYDGIPEEV 225
Cdd:PRK13633 158 ILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEI 231
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
19-216 |
1.64e-37 |
|
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: 134.41 E-value: 1.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 19 NMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLK---QSEGDIVLDGKSIHTMKSADV----AKQLAMLPQmhdhqlD-- 89
Cdd:COG0444 23 GVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKELrkirGREIQMIFQ------Dpm 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 90 ------LTVKELIEFgrgPHKLWRGRLNKEDEEIVDWALSVTNLEGYEYRLLQ---SLSGGERQRAWIAMTLAQRTNVLL 160
Cdd:COG0444 97 tslnpvMTVGDQIAE---PLRIHGGLSKAEARERAIELLERVGLPDPERRLDRyphELSGGMRQRVMIARALALEPKLLI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446549187 161 LDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKL 216
Cdd:COG0444 174 ADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRI 229
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-219 |
2.00e-37 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 132.90 E-value: 2.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 1 MISVN---KVFYAHS--ERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAK 75
Cdd:COG1101 1 MLELKnlsKTFNPGTvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 76 QLAMLPQmhDHQL----DLTVKE--LIEFGRGPHKLWRGRLNKEDEEIVDWALSVTNLeGYEYRLLQ---SLSGGERQra 146
Cdd:COG1101 81 YIGRVFQ--DPMMgtapSMTIEEnlALAYRRGKRRGLRRGLTKKRRELFRELLATLGL-GLENRLDTkvgLLSGGQRQ-- 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446549187 147 wiAMTLA----QRTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYD 219
Cdd:COG1101 156 --ALSLLmatlTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIILD 230
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
18-228 |
2.64e-37 |
|
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: 132.77 E-value: 2.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 18 QNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADV----AKQLAM-------LPQMhdh 86
Cdd:cd03294 41 NDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMvfqsfalLPHR--- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 87 qldlTVKELIEFGrgphkL-WRGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPT 165
Cdd:cd03294 118 ----TVLENVAFG-----LeVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446549187 166 TFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVLCH 228
Cdd:cd03294 189 SALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
18-216 |
8.84e-37 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 129.30 E-value: 8.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 18 QNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHtmkSADVAKQLAMLPQMHDHQL-DLTVKELI 96
Cdd:cd03226 17 DDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK---AKERRKSIGYVMQDVDYQLfTDSVREEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 97 EFGRgphklwrgRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVHQLEV 176
Cdd:cd03226 94 LLGL--------KELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERV 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446549187 177 MELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKL 216
Cdd:cd03226 166 GELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
19-225 |
9.26e-37 |
|
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: 130.54 E-value: 9.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 19 NMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSAD-----VAKQLAMLPQMhdhqldlTVK 93
Cdd:cd03296 20 DVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQErnvgfVFQHYALFRHM-------TVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 94 ELIEFGRGPHKLWRGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVHQ 173
Cdd:cd03296 93 DNVAFGLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVR 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446549187 174 LEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEV 225
Cdd:cd03296 173 KELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-226 |
1.49e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 130.88 E-value: 1.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 1 MISVNKVF--YAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLA 78
Cdd:PRK13632 7 MIKVENVSfsYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 79 MLPQMHDHQ-LDLTVKELIEFGRGPHKLWRgrlnKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTN 157
Cdd:PRK13632 87 IIFQNPDNQfIGATVEDDIAFGLENKKVPP----KKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446549187 158 VLLLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQySDRLLVLKRGKLQYDGIPEEVL 226
Cdd:PRK13632 163 IIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEIL 230
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
9-226 |
1.66e-36 |
|
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: 136.05 E-value: 1.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 9 YAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAMLPQmHDHQL 88
Cdd:COG4987 343 YPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQ-RPHLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 89 DLTVKELIEFGRGphklwrgrlNKEDEEIVDwALSVTNL--------EGYEYRLL---QSLSGGERQRAWIAMTLAQRTN 157
Cdd:COG4987 422 DTTLRENLRLARP---------DATDEELWA-ALERVGLgdwlaalpDGLDTWLGeggRRLSGGERRRLALARALLRDAP 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446549187 158 VLLLDEPTTFLDIVHQLEVMELVKRLNEefGMTIIMVLHDINQAAQYsDRLLVLKRGKLQYDGIPEEVL 226
Cdd:COG4987 492 ILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLERM-DRILVLEDGRIVEQGTHEELL 557
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-239 |
3.63e-36 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 128.55 E-value: 3.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 1 MISVNKVFYahseRFQMQNM--NVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSiHTmKSADVAKQLA 78
Cdd:PRK10771 1 MLKLTDITW----LYHHLPMrfDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-HT-TTPPSRRPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 79 MLPQMHDHQLDLTVKELIEFGRGPhklwrG-RLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTN 157
Cdd:PRK10771 75 MLFQENNLFSHLTVAQNIGLGLNP-----GlKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 158 VLLLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVLCHEMFQ-HVFG 236
Cdd:PRK10771 150 ILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKASAsALLG 229
|
...
gi 446549187 237 IEV 239
Cdd:PRK10771 230 IKS 232
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
19-228 |
4.36e-36 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 131.42 E-value: 4.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 19 NMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADvAKQLAMLPQmhDHQL--DLTVKELI 96
Cdd:COG1118 20 DVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPR-ERRVGFVFQ--HYALfpHMTVAENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 97 EFG---RGPHKlwrgrlnKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPttF--LDI- 170
Cdd:COG1118 97 AFGlrvRPPSK-------AEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEP--FgaLDAk 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446549187 171 VHQlEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVLCH 228
Cdd:COG1118 168 VRK-ELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
19-224 |
1.47e-35 |
|
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: 126.72 E-value: 1.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 19 NMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIhTMKSADVAKQLAMLPQMHDHQLDLTVKElief 98
Cdd:cd03265 18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV-VREPREVRRRIGIVFQDLSVDDELTGWE---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 99 grgpHKLWRGRL----NKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVHQL 174
Cdd:cd03265 93 ----NLYIHARLygvpGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446549187 175 EVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEE 224
Cdd:cd03265 169 HVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
18-224 |
1.81e-35 |
|
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: 126.47 E-value: 1.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 18 QNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSAdVAKQLAMLPQmHDHQLD-LTVKELI 96
Cdd:cd03263 19 DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKA-ARQSLGYCPQ-FDALFDeLTVREHL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 97 EFgrgpHKLWRGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVHQLEV 176
Cdd:cd03263 97 RF----YARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAI 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446549187 177 MELVKRLNEefGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEE 224
Cdd:cd03263 173 WDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
19-228 |
3.03e-35 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 126.26 E-value: 3.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 19 NMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIhTMKSADVAK---QLAMLPQmhDHQL--DLTVK 93
Cdd:COG1126 19 GISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDINKlrrKVGMVFQ--QFNLfpHLTVL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 94 E-LIEfgrGPHKLwRGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLD--I 170
Cdd:COG1126 96 EnVTL---APIKV-KKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDpeL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446549187 171 VHqlEVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVLCH 228
Cdd:COG1126 172 VG--EVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFEN 226
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-197 |
6.09e-35 |
|
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: 124.51 E-value: 6.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 1 MISVNKVFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTmKSADVAKQLAML 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 81 PqmHDHQL--DLTVKELIEFGRgphKLWRGRLNKEDeeiVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNV 158
Cdd:COG4133 81 G--HADGLkpELTVRENLRFWA---ALYGLRADREA---IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPL 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 446549187 159 LLLDEPTTFLDIVHQLEVMELVKRLNEEfGMTIIMVLHD 197
Cdd:COG4133 153 WLLDEPFTALDAAGVALLAELIAAHLAR-GGAVLLTTHQ 190
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
17-216 |
8.22e-35 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 124.56 E-value: 8.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 17 MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIhTMKSADVA---KQLAMLPQMHDHQLDLTVK 93
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TDDKKNINelrQKVGMVFQQFNLFPHLTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 94 ELIEFgrGPHKLwRGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLD--IV 171
Cdd:cd03262 95 ENITL--APIKV-KGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDpeLV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446549187 172 HqlEVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKL 216
Cdd:cd03262 172 G--EVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-228 |
1.55e-34 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 124.23 E-value: 1.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 1 MIS---VNKVFYAHSERFQ-MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADV--- 73
Cdd:cd03258 1 MIElknVSKVFGDTGGKVTaLKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 74 AKQLAMLPQmHDHQLD-LTVKELIEFgrgPHKLWRGRlNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTL 152
Cdd:cd03258 81 RRRIGMIFQ-HFNLLSsRTVFENVAL---PLEIAGVP-KAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446549187 153 AQRTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVLCH 228
Cdd:cd03258 156 ANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
17-234 |
1.85e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 125.73 E-value: 1.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 17 MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSA--DVAKQLAMLPQMHDHQL-DLTVK 93
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGlmKLRESVGMVFQDPDNQLfSASVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 94 ELIEFGRGPHKLWRgrlnKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVHQ 173
Cdd:PRK13636 102 QDVSFGAVNLKLPE----DEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGV 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446549187 174 LEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVLC-HEMFQHV 234
Cdd:PRK13636 178 SEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAeKEMLRKV 239
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-217 |
3.35e-34 |
|
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: 122.75 E-value: 3.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 4 VNKVFyahSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSAD-----VAKQLA 78
Cdd:cd03301 6 VTKRF---GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDrdiamVFQNYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 79 MLPQMhdhqldlTVKELIEFgrgPHKLwRGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNV 158
Cdd:cd03301 83 LYPHM-------TVYDNIAF---GLKL-RKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446549187 159 LLLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQ 217
Cdd:cd03301 152 FLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
32-244 |
3.76e-34 |
|
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: 125.68 E-value: 3.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 32 LIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSI-----HTMKSADVAKQLAMLPQMhdhqldlTVKELIEFgrgPHKLw 106
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVtnvppHLRHINMVFQSYALFPHM-------TVEENVAF---GLKM- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 107 RGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDivHQL-EVMEL-VKRLN 184
Cdd:TIGR01187 70 RKVPRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALD--KKLrDQMQLeLKTIQ 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446549187 185 EEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVLCH--EMFQHVFGIEVDIFQG 244
Cdd:TIGR01187 148 EQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEpaNLFVARFIGEINVFEA 209
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
13-228 |
7.19e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 124.36 E-value: 7.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 13 ERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSA----DVAKQLAMLPQMHDHQL 88
Cdd:PRK13634 19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNkklkPLRKKVGIVFQFPEHQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 89 -DLTVKELIEFGrgPHKLwrGRLNKEDEEIVDWALSVTNLEgyEYRLLQS---LSGGERQRAWIAMTLAQRTNVLLLDEP 164
Cdd:PRK13634 99 fEETVEKDICFG--PMNF--GVSEEDAKQKAREMIELVGLP--EELLARSpfeLSGGQMRRVAIAGVLAMEPEVLVLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446549187 165 TTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVLCH 228
Cdd:PRK13634 173 TAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFAD 236
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-220 |
8.36e-34 |
|
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: 122.02 E-value: 8.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 27 GEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDG-------KSIHT----MKSADVAKQLAMLPQMhdhqldlTVKEL 95
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrKKINLppqqRKIGLVFQQYALFPHL-------NVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 96 IEFGrgphklWRGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVHQLE 175
Cdd:cd03297 96 LAFG------LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446549187 176 VMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDG 220
Cdd:cd03297 170 LLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
17-244 |
1.91e-33 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 124.95 E-value: 1.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 17 MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSAD-----VAKQLAMLPQMhdhqldlT 91
Cdd:PRK11607 35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQrpinmMFQSYALFPHM-------T 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 92 VKELIEFGRGPHKLWRGRLNKEDEEIvdwaLSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIV 171
Cdd:PRK11607 108 VEQNIAFGLKQDKLPKAEIASRVNEM----LGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446549187 172 ----HQLEVMELVKRLneefGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVLCH--EMFQHVFGIEVDIFQG 244
Cdd:PRK11607 184 lrdrMQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHptTRYSAEFIGSVNVFEG 258
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-241 |
2.83e-33 |
|
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: 121.34 E-value: 2.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 1 MISVNKVFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEG-DIVLDGK-----SIhtmksADVA 74
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGErrggeDV-----WELR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 75 KQLAML-PQMH-DHQLDLTVKELIEFGR----GphkLWRgRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWI 148
Cdd:COG1119 78 KRIGLVsPALQlRFPRDETVLDVVLSGFfdsiG---LYR-EPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 149 AMTLAQRTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVLCH 228
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLTS 233
|
250
....*....|...
gi 446549187 229 EMFQHVFGIEVDI 241
Cdd:COG1119 234 ENLSEAFGLPVEV 246
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
19-244 |
4.52e-33 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 123.68 E-value: 4.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 19 NMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDG-----KSIHTMKSADVAKQLAMLPQMhdhqldlTVK 93
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGedvthRSIQQRDICMVFQSYALFPHM-------SLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 94 ELIEFGRgphKLwRGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVHQ 173
Cdd:PRK11432 97 ENVGYGL---KM-LGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLR 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446549187 174 LEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVLCH--EMFQHVFGIEVDIFQG 244
Cdd:PRK11432 173 RSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQpaSRFMASFMGDANIFPA 245
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
21-220 |
6.63e-33 |
|
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: 119.58 E-value: 6.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 21 NVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSiHTmKSADVAKQLAMLPQMHDHQLDLTVKELIEFGR 100
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQS-HT-GLAPYQRPVSMLFQENNLFAHLTVRQNIGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 101 GPHKlwrgRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVHQLEVMELV 180
Cdd:TIGR01277 96 HPGL----KLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446549187 181 KRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDG 220
Cdd:TIGR01277 172 KQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
18-228 |
6.63e-33 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 122.12 E-value: 6.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 18 QNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSAD-------VAKQLAMLPQMhdhqldl 90
Cdd:COG1125 19 DDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrrrigyVIQQIGLFPHM------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 91 TVKELIefGRGPhklwrgRLNKEDE----EIVDWALSVTNLEGYEY--RLLQSLSGGERQRAWIAMTLAQRTNVLLLDEP 164
Cdd:COG1125 92 TVAENI--ATVP------RLLGWDKerirARVDELLELVGLDPEEYrdRYPHELSGGQQQRVGVARALAADPPILLMDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446549187 165 ttF--LD-IV-HQLEvmELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKL-QYDGiPEEVLCH 228
Cdd:COG1125 164 --FgaLDpITrEQLQ--DELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIvQYDT-PEEILAN 227
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
24-239 |
7.84e-33 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 120.42 E-value: 7.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 24 IKAGEVVSLIGPNGSGKSTLLRLIARLLkQSEGDIVLDGKSIHTMKSADVAKQLAMLPQ-------MHD-HQLDLTVKEL 95
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQqqtppfaMPVfQYLTLHQPDK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 96 IEFGRGPHKLwrgrlnkedEEIVDwALSVTNLEGyeyRLLQSLSGGERQRAWIAMTLAQ---RTN----VLLLDEPTTFL 168
Cdd:PRK03695 98 TRTEAVASAL---------NEVAE-ALGLDDKLG---RSVNQLSGGEWQRVRLAAVVLQvwpDINpagqLLLLDEPMNSL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446549187 169 DIVHQLEVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVLCHEMFQHVFGIEV 239
Cdd:PRK03695 165 DVAQQAALDRLLSELCQQ-GIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVFGVNF 234
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
9-220 |
1.16e-32 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 119.23 E-value: 1.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 9 YAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAMLPQmHDHQL 88
Cdd:cd03245 12 YPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQ-DVTLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 89 DLTVKELIEFGRGPHklwrgrlnkEDEEIVDWA--LSVTNL-----EGYEYRLL---QSLSGGERQRAWIAMTLAQRTNV 158
Cdd:cd03245 91 YGTLRDNITLGAPLA---------DDERILRAAelAGVTDFvnkhpNGLDLQIGergRGLSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446549187 159 LLLDEPTTFLDIvhQLEvMELVKRLNEEF-GMTIIMVLHDINqAAQYSDRLLVLKRGKLQYDG 220
Cdd:cd03245 162 LLLDEPTSAMDM--NSE-ERLKERLRQLLgDKTLIIITHRPS-LLDLVDRIIVMDSGRIVADG 220
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1-216 |
1.35e-32 |
|
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: 118.66 E-value: 1.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 1 MISVNKVfYAHSERfQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAK---QL 77
Cdd:cd03292 3 FINVTKT-YPNGTA-ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYlrrKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 78 AMLPQMHDHQLDLTVKELIEFG----RGPHKLWRGRlnkedeeiVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLA 153
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFAlevtGVPPREIRKR--------VPAALELVGLSHKHRALPAELSGGEQQRVAIARAIV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446549187 154 QRTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKL 216
Cdd:cd03292 153 NSPTILIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
18-226 |
1.42e-32 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 125.28 E-value: 1.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 18 QNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAMLPQmhDHQL-DLTVKELI 96
Cdd:COG1132 357 KDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQ--DTFLfSGTIRENI 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 97 EFgrgphklwrGRLNKEDEEIVDwALSVTNL--------EGYEYRLLQ---SLSGGERQRAWIAMTLAQRTNVLLLDEPT 165
Cdd:COG1132 435 RY---------GRPDATDEEVEE-AAKAAQAhefiealpDGYDTVVGErgvNLSGGQRQRIAIARALLKDPPILILDEAT 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446549187 166 TFLDIVHQLEVMELVKRLNEefGMTIIMVLHDINQAAQySDRLLVLKRGKLQYDGIPEEVL 226
Cdd:COG1132 505 SALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTHEELL 562
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
17-220 |
1.57e-32 |
|
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: 119.36 E-value: 1.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 17 MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAMLPQMHDHQLDLTVKELI 96
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKTQLWWDLPVIDSF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 97 EFGRGPHKLWRGRLNKEDEEIVDwalsVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVHQLEV 176
Cdd:cd03267 117 YLLAAIYDLPPARFKKRLDELSE----LLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENI 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446549187 177 MELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDG 220
Cdd:cd03267 193 RNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
9-249 |
2.84e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 119.47 E-value: 2.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 9 YAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAMLPQMHDHQ- 87
Cdd:PRK13648 17 YQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQNPDNQf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 88 LDLTVKELIEFGRGPHKLwrgrLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTF 167
Cdd:PRK13648 97 VGSIVKYDVAFGLENHAV----PYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSM 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 168 LDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQySDRLLVLKRGKLQYDGIPEEVL-CHEMFQHVfgievdifqGSD 246
Cdd:PRK13648 173 LDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFdHAEELTRI---------GLD 242
|
...
gi 446549187 247 KPF 249
Cdd:PRK13648 243 LPF 245
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
24-226 |
3.83e-32 |
|
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: 120.99 E-value: 3.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 24 IKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGK-----------SIHTMKSADVAKQLAMLPQmhdhqldLTV 92
Cdd:TIGR02142 20 LPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfdsrkgiflPPEKRRIGYVFQEARLFPH-------LSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 93 KELIEFGRgphklWRGRlnkEDEEIVDWAlSVTNLEGYEY---RLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLD 169
Cdd:TIGR02142 93 RGNLRYGM-----KRAR---PSERRISFE-RVIELLGIGHllgRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446549187 170 IVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVL 226
Cdd:TIGR02142 164 DPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVW 220
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
17-225 |
4.04e-32 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 121.59 E-value: 4.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 17 MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIhTMKSAD------VAKQLAMLPQMhdhqldl 90
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI-THVPAEnrhvntVFQSYALFPHM------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 91 TVKELIEFGRGPHKlwrgRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDi 170
Cdd:PRK09452 102 TVFENVAFGLRMQK----TPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD- 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446549187 171 vHQLEV---MELvKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEV 225
Cdd:PRK09452 177 -YKLRKqmqNEL-KALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 232
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-232 |
9.56e-32 |
|
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: 117.33 E-value: 9.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 2 ISVNKVFYA-HSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAML 80
Cdd:cd03253 1 IEFENVTFAyDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 81 PQmhDHQL-DLTVKELIEFgrgphklwrGRLNKEDEEIVDWAL------SVTNL-EGYEYRLLQ---SLSGGERQRAWIA 149
Cdd:cd03253 81 PQ--DTVLfNDTIGYNIRY---------GRPDATDEEVIEAAKaaqihdKIMRFpDGYDTIVGErglKLSGGEKQRVAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 150 MTLAQRTNVLLLDEPTTFLDIVHQLEVMELVKRLNEefGMTIIMVLHDINQAAQySDRLLVLKRGKLQYDGIPEEVLC-- 227
Cdd:cd03253 150 RAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLAkg 226
|
....*...
gi 446549187 228 ---HEMFQ 232
Cdd:cd03253 227 glyAEMWK 234
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-230 |
9.97e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 117.71 E-value: 9.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 17 MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLK-----QSEGDIVLDGKSIHTMKSADVAKQLAMLPQMHDHQLDLT 91
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPIPNLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 92 VKELIEFGRGPHKLWRGRlnKEDEEIVDWALSVTNL-EGYEYRL---LQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTF 167
Cdd:PRK14247 99 IFENVALGLKLNRLVKSK--KELQERVRWALEKAQLwDEVKDRLdapAGKLSGGQQQRLCIARALAFQPEVLLADEPTAN 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446549187 168 LDIVHQLEVMELVKRLNEEfgMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVLC---HEM 230
Cdd:PRK14247 177 LDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTnprHEL 240
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
2-216 |
1.31e-31 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 116.30 E-value: 1.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 2 ISVNKVFYAHSERFQ-MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAK----Q 76
Cdd:TIGR02211 5 ENLGKRYQEGKLDTRvLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKlrnkK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 77 LAMLPQMHDHQLDLTVKELIEFgrgPhKLWRGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRT 156
Cdd:TIGR02211 85 LGFIYQFHHLLPDFTALENVAM---P-LLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 157 NVLLLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYsDRLLVLKRGKL 216
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQL 219
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
18-220 |
2.40e-31 |
|
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: 115.39 E-value: 2.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 18 QNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSihTMKSADVAKQLAML---PQMHDHqldLTVKE 94
Cdd:cd03268 17 DDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKS--YQKNIEALRRIGALieaPGFYPN---LTARE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 95 -LIEFGRGPhklwrGRLNKEDEEIVDwalsVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVHQ 173
Cdd:cd03268 92 nLRLLARLL-----GIRKKRIDEVLD----VVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGI 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446549187 174 LEVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDG 220
Cdd:cd03268 163 KELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
16-249 |
2.49e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 117.12 E-value: 2.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 16 QMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAMLPQMHDHQ-LDLTVKE 94
Cdd:PRK13642 22 QLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPDNQfVGATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 95 LIEFGRGPHKLWRGRLNKEdeeiVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVHQL 174
Cdd:PRK13642 102 DVAFGMENQGIPREEMIKR----VDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQ 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446549187 175 EVMELVKRLNEEFGMTIIMVLHDINQAAQySDRLLVLKRGKLQYDGIPEEvlchemfqhVFGIEVDIFQ-GSDKPF 249
Cdd:PRK13642 178 EIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSE---------LFATSEDMVEiGLDVPF 243
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-226 |
6.26e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 116.24 E-value: 6.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 1 MISVNKVFYAHSERF-QMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDG-KSIHTMKSADVAKQLA 78
Cdd:PRK13644 1 MIRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGiDTGDFSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 79 MLPQMHDHQ-LDLTVKELIEFGrgPHKLWRGRLnkEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTN 157
Cdd:PRK13644 81 IVFQNPETQfVGRTVEEDLAFG--PENLCLPPI--EIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446549187 158 VLLLDEPTTFLDIVHQLEVMELVKRLNEEfGMTIIMVLHDINQaAQYSDRLLVLKRGKLQYDGIPEEVL 226
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-244 |
9.42e-31 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 117.49 E-value: 9.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 2 ISVNKV--FYAHSErfQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSAD-----VA 74
Cdd:PRK10851 3 IEIANIkkSFGRTQ--VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDrkvgfVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 75 KQLAMLPQMhdhqldlTVKELIEFGRG--PHklwRGRLNKED-EEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMT 151
Cdd:PRK10851 81 QHYALFRHM-------TVFDNIAFGLTvlPR---RERPNAAAiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 152 LAQRTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVLCHEMF 231
Cdd:PRK10851 151 LAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPAT 230
|
250
....*....|....*
gi 446549187 232 QHV--FGIEVDIFQG 244
Cdd:PRK10851 231 RFVleFMGEVNRLQG 245
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-220 |
1.18e-30 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 114.00 E-value: 1.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 1 MISVN---KVFYAHSERFQ-MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKsADVAKQ 76
Cdd:cd03266 1 MITADaltKRFRDVKKTVQaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEP-AEARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 77 LAMLPQMHDHQLDLTVKELIEFGRGPHKLWRGRLNKEdeeiVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRT 156
Cdd:cd03266 80 LGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTAR----LEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446549187 157 NVLLLDEPTTFLDIVHQLEVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDG 220
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
17-226 |
1.28e-30 |
|
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: 113.86 E-value: 1.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 17 MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAMLPQmHDHQLDLTVKELI 96
Cdd:cd03254 19 LKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQ-DTFLFSGTIMENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 97 EFgrgphklwrGRLNKEDEEIVDwALSVTNL--------EGYEYRLL---QSLSGGERQRAWIAMTLAQRTNVLLLDEPT 165
Cdd:cd03254 98 RL---------GRPNATDEEVIE-AAKEAGAhdfimklpNGYDTVLGengGNLSQGERQLLAIARAMLRDPKILILDEAT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446549187 166 TFLDIVHQLEVMELVKRLNEefGMTIIMVLHDINqAAQYSDRLLVLKRGKLQYDGIPEEVL 226
Cdd:cd03254 168 SNIDTETEKLIQEALEKLMK--GRTSIIIAHRLS-TIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-214 |
2.18e-30 |
|
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: 113.33 E-value: 2.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 17 MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIhTMKSAD---VAKQLAMLPQMHDHQ-LDLTV 92
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI-TEPGPDrmvVFQNYSLLPWLTVREnIALAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 93 KELIefgrgphklwRGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVH 172
Cdd:TIGR01184 80 DRVL----------PDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446549187 173 QLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRG 214
Cdd:TIGR01184 150 RGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-216 |
3.26e-30 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 115.56 E-value: 3.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 1 MIS---VNKVFYAHSERFQ-MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVA-- 74
Cdd:COG1135 1 MIElenLSKTFPTKGGPVTaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRaa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 75 -KQLAMLPQmHDHQLD-LTVKELIEFgrgPHKLWrgRLNKED-EEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMT 151
Cdd:COG1135 81 rRKIGMIFQ-HFNLLSsRTVAENVAL---PLEIA--GVPKAEiRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446549187 152 LAQRTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKL 216
Cdd:COG1135 155 LANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
32-220 |
7.49e-30 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 111.52 E-value: 7.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 32 LIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSAdVAKQLAMLPQMHDHQLDLTVKELIEfgrgpHKLWRGRLN 111
Cdd:cd03264 30 LLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-LRRRIGYLPQEFGVYPNFTVREFLD-----YIAWLKGIP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 112 -KEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEfgMT 190
Cdd:cd03264 104 sKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGED--RI 181
|
170 180 190
....*....|....*....|....*....|
gi 446549187 191 IIMVLHDINQAAQYSDRLLVLKRGKLQYDG 220
Cdd:cd03264 182 VILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
9-250 |
1.86e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 112.20 E-value: 1.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 9 YAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLL---KQSEGDIVLDGKSIHTMKSADVAKQLAMLPQMHD 85
Cdd:PRK13640 15 YPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIREKVGIVFQNPD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 86 HQ-LDLTVKELIEFGRGPHKLWRGRLNKedeeIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEP 164
Cdd:PRK13640 95 NQfVGATVGDDVAFGLENRAVPRPEMIK----IVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDES 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 165 TTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQySDRLLVLKRGKLQYDGIPEEVLCH-EMFQHVfgievdifq 243
Cdd:PRK13640 171 TSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIFSKvEMLKEI--------- 240
|
....*..
gi 446549187 244 GSDKPFF 250
Cdd:PRK13640 241 GLDIPFV 247
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
19-226 |
1.91e-29 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 114.04 E-value: 1.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 19 NMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSI-HTMKSADVA---KQLAMLPQmhDHQLD--LTV 92
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqDSARGIFLPphrRRIGYVFQ--EARLFphLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 93 KELIEFG--RGPHKLWRGRLnkedEEIVDWaLSVTNLEGyeyRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDI 170
Cdd:COG4148 95 RGNLLYGrkRAPRAERRISF----DEVVEL-LGIGHLLD---RRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446549187 171 VHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVL 226
Cdd:COG4148 167 ARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVL 222
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-220 |
2.22e-29 |
|
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: 110.82 E-value: 2.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 18 QNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLL---KQSEGDIVLDGK--SIHTMKsadvaKQLAMLPQmHDHQLD-LT 91
Cdd:cd03234 24 NDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQprKPDQFQ-----KCVAYVRQ-DDILLPgLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 92 VKELIEFG---RGPHKLWRGRLNKEDEEIVDWALSVTNLEGYeyrLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFL 168
Cdd:cd03234 98 VRETLTYTailRLPRKSSDAIRKKRVEDVLLRDLALTRIGGN---LVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446549187 169 DIVHQLEVMELVKRLNEEfGMTIIMVLH----DInqaAQYSDRLLVLKRGKLQYDG 220
Cdd:cd03234 175 DSFTALNLVSTLSQLARR-NRIVILTIHqprsDL---FRLFDRILLLSSGEIVYSG 226
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
19-216 |
2.38e-29 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 111.28 E-value: 2.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 19 NMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLK-----QSEGDIVLDGKSIHTmKSADVA---KQLAMLPQ------Mh 84
Cdd:COG1117 29 DINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDlipgaRVEGEILLDGEDIYD-PDVDVVelrRRVGMVFQkpnpfpK- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 85 dhqldlTVKELIEFGrgpHKLwRGRLNKED-EEIVDWALSVTNL--EGYEyRLLQS---LSGGERQRAWIAMTLAQRTNV 158
Cdd:COG1117 107 ------SIYDNVAYG---LRL-HGIKSKSElDEIVEESLRKAALwdEVKD-RLKKSalgLSGGQQQRLCIARALAVEPEV 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446549187 159 LLLDEPTTFLDIVHQLEVMELVKRLNEEFgmTIIMVLHDINQAAQYSDRLLVLKRGKL 216
Cdd:COG1117 176 LLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLGEL 231
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-226 |
5.08e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 110.70 E-value: 5.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 6 KVFYAHSErfQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLK-----QSEGDIVLDGKSIHT--MKSADVAKQLA 78
Cdd:PRK14267 11 RVYYGSNH--VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSpdVDPIEVRREVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 79 MLPQMHDHQLDLTVKELIEFGRGPHKLWRGRlnKEDEEIVDWALSVTNL-EGYEYRL---LQSLSGGERQRAWIAMTLAQ 154
Cdd:PRK14267 89 MVFQYPNPFPHLTIYDNVAIGVKLNGLVKSK--KELDERVEWALKKAALwDEVKDRLndyPSNLSGGQRQRLVIARALAM 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446549187 155 RTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEFgmTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVL 226
Cdd:PRK14267 167 KPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVF 236
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
18-220 |
5.54e-29 |
|
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: 108.79 E-value: 5.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 18 QNMNVHIKAGEVVSLIGPNGSGKSTLLRLIA--RLLKQSEGDIVLDGKSIHtmkSADVAKQLAMLPQmHDHQL-DLTVKE 94
Cdd:cd03213 26 KNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLD---KRSFRKIIGYVPQ-DDILHpTLTVRE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 95 LIEFgrgphklwrgrlnkedeeivdwalSVtnlegyeyrLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVHQL 174
Cdd:cd03213 102 TLMF------------------------AA---------KLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSAL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446549187 175 EVMELVKRLNEEfGMTIIMVLHdinqAAQYS-----DRLLVLKRGKLQYDG 220
Cdd:cd03213 149 QVMSLLRRLADT-GRTIICSIH----QPSSEifelfDKLLLLSQGRVIYFG 194
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
24-222 |
5.79e-29 |
|
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: 110.19 E-value: 5.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 24 IKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIhtmksadvakqlAMLPQMHDHQLDLTVKEL---IEFGR 100
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV------------SYKPQYIKADYEGTVRDLlssITKDF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 101 GPHKLWRGRLNK--EDEEIVDwalsvtnlegyeyRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVHQLEVME 178
Cdd:cd03237 90 YTHPYFKTEIAKplQIEQILD-------------REVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446549187 179 LVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVlkrgklqYDGIP 222
Cdd:cd03237 157 VIRRFAENNEKTAFVVEHDIIMIDYLADRLIV-------FEGEP 193
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-235 |
8.27e-29 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 110.10 E-value: 8.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 1 MISVNKVFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLL---KQSEGDIVLDGKSIHTMK--SADVAK 75
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQREGrlARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 76 ---QLAMLPQMHDHQLDLTVKELIEFGR-GPHKLWRGRL---NKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWI 148
Cdd:PRK09984 84 sraNTGYIFQQFNLVNRLSVLENVLIGAlGSTPFWRTCFswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 149 AMTLAQRTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEvLCH 228
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ-FDN 242
|
....*..
gi 446549187 229 EMFQHVF 235
Cdd:PRK09984 243 ERFDHLY 249
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-216 |
1.19e-28 |
|
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: 107.30 E-value: 1.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 2 ISVNKVF--YAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAM 79
Cdd:cd03246 1 LEVENVSfrYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 80 LPQmhDHQL-DLTVKELIefgrgphklwrgrlnkedeeivdwalsvtnlegyeyrllqsLSGGERQRAWIAMTLAQRTNV 158
Cdd:cd03246 81 LPQ--DDELfSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446549187 159 LLLDEPTTFLDIVHQLEVMELVKRLNEEfGMTIIMVLHDINQAAQySDRLLVLKRGKL 216
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALKAA-GATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
24-215 |
2.96e-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: 107.37 E-value: 2.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 24 IKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIhtmkSADVAKQLAMLPQMHDHQLDLTVKE-LIEFGRgp 102
Cdd:cd03269 23 VEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL----DIAARNRIGYLPEERGLYPKMKVIDqLVYLAQ-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 103 hklWRGrLNKED--EEIVDWaLSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVHQLEVMELV 180
Cdd:cd03269 97 ---LKG-LKKEEarRRIDEW-LERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVI 171
|
170 180 190
....*....|....*....|....*....|....*
gi 446549187 181 KRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGK 215
Cdd:cd03269 172 RELARA-GKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-196 |
4.69e-28 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 106.50 E-value: 4.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 1 MISVNKVFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAML 80
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGHR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 81 PQMHDHqldLTVKELIEFgrgphklWRGRLNKEDEEIVDwALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLL 160
Cdd:PRK13539 82 NAMKPA---LTVAENLEF-------WAAFLGGEELDIAA-ALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWI 150
|
170 180 190
....*....|....*....|....*....|....*.
gi 446549187 161 LDEPTTFLDIVHQLEVMELVKRLNEEFGMtIIMVLH 196
Cdd:PRK13539 151 LDEPTAALDAAAVALFAELIRAHLAQGGI-VIAATH 185
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-225 |
7.07e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 108.33 E-value: 7.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 2 ISVNKVFYAHS-----ERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTmKSAD---- 72
Cdd:PRK13646 3 IRFDNVSYTYQkgtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITH-KTKDkyir 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 73 -VAKQLAMLPQMHDHQL-DLTVKELIEFGrgPHKLwrgrlNKEDEEIVDWALSVTNLEGYEYRLLQS----LSGGERQRA 146
Cdd:PRK13646 82 pVRKRIGMVFQFPESQLfEDTVEREIIFG--PKNF-----KMNLDEVKNYAHRLLMDLGFSRDVMSQspfqMSGGQMRKI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446549187 147 WIAMTLAQRTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEV 225
Cdd:PRK13646 155 AIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-220 |
1.87e-27 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 104.32 E-value: 1.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 2 ISVNKV-F-YAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSAdVAKQLAM 79
Cdd:cd03247 1 LSINNVsFsYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 80 LPQmHDHQLDLTVKELIefGRgphklwrgrlnkedeeivdwalsvtnlegyeyrllqSLSGGERQRAWIAMTLAQRTNVL 159
Cdd:cd03247 80 LNQ-RPYLFDTTLRNNL--GR------------------------------------RFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446549187 160 LLDEPTTFLDIVHQLEVMELVKRLNEEfgMTIIMVLHDInQAAQYSDRLLVLKRGKLQYDG 220
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKD--KTLIWITHHL-TGIEHMDKILFLENGKIIMQG 178
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-226 |
1.98e-27 |
|
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: 110.61 E-value: 1.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 2 ISVNKVFYAH--SERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAM 79
Cdd:COG4618 331 LSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 80 LPQmhDHQL-DLTVKELIefgrgphklwrGRLNKEDEEIV----------DWALSvtnL-EGYEYRL---LQSLSGGERQ 144
Cdd:COG4618 411 LPQ--DVELfDGTIAENI-----------ARFGDADPEKVvaaaklagvhEMILR---LpDGYDTRIgegGARLSGGQRQ 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 145 RAWIAMTLAQRTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEfGMTIIMVLHDINqAAQYSDRLLVLKRGKLQYDGIPEE 224
Cdd:COG4618 475 RIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDE 552
|
..
gi 446549187 225 VL 226
Cdd:COG4618 553 VL 554
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-234 |
1.98e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 106.75 E-value: 1.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 19 NMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSI-HTMKSAD---VAKQLAMLPQMHDHQL-DLTVK 93
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItSTSKNKDikqIRKKVGLVFQFPESQLfEETVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 94 ELIEFGrgPHKLwrGRLNKEDEEIvdwALSVTNLEGYEYRLLQ----SLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLD 169
Cdd:PRK13649 105 KDVAFG--PQNF--GVSQEEAEAL---AREKLALVGISESLFEknpfELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446549187 170 IVHQLEVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVlchemFQHV 234
Cdd:PRK13649 178 PKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI-----FQDV 236
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
19-230 |
2.22e-27 |
|
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: 105.70 E-value: 2.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 19 NMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTM---KSAdvAKQLAMLPQMHDHQLDLTVKEL 95
Cdd:cd03218 18 GVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLpmhKRA--RLGIGYLPQEASIFRKLTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 96 I----EFgrgphklwRGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIV 171
Cdd:cd03218 96 IlavlEI--------RGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446549187 172 HQLEVMELVKRLNeEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVLCHEM 230
Cdd:cd03218 168 AVQDIQKIIKILK-DRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
18-211 |
3.01e-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: 110.07 E-value: 3.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 18 QNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAMLPQmHDHQLDLTVKELIE 97
Cdd:TIGR02857 339 RPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQ-HPFLFAGTIAENIR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 98 FGRgphklwrgrlNKEDEEIVDWALSVTNL--------EGYEYRLLQS---LSGGERQRAWIAMTLAQRTNVLLLDEPTT 166
Cdd:TIGR02857 418 LAR----------PDASDAEIREALERAGLdefvaalpQGLDTPIGEGgagLSGGQAQRLALARAFLRDAPLLLLDEPTA 487
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446549187 167 FLDIVHQLEVMELVKRLNEefGMTIIMVLHDINQAAQYsDRLLVL 211
Cdd:TIGR02857 488 HLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALA-DRIVVL 529
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
18-211 |
3.85e-27 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 105.71 E-value: 3.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 18 QNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIhTMKSAD---VAKQLAMLPQmhdhqldLTVKE 94
Cdd:COG4525 24 QDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV-TGPGADrgvVFQKDALLPW-------LNVLD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 95 LIEFGRgphKLwRGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVHQL 174
Cdd:COG4525 96 NVAFGL---RL-RGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTRE 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 446549187 175 EVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVL 211
Cdd:COG4525 172 QMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
9-226 |
5.11e-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: 104.62 E-value: 5.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 9 YAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAMLPQmHDHQL 88
Cdd:cd03251 10 YPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVSQ-DVFLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 89 DLTVKELIEFgrgphklwrGRLNKEDEEIVDWALS------VTNL-EGYEYRLLQ---SLSGGERQRAWIAMTLAQRTNV 158
Cdd:cd03251 89 NDTVAENIAY---------GRPGATREEVEEAARAanahefIMELpEGYDTVIGErgvKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446549187 159 LLLDEPTTFLDIVHQLEVMELVKRLNEefGMTIIMVLH---DINQAaqysDRLLVLKRGKLQYDGIPEEVL 226
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMK--NRTTFVIAHrlsTIENA----DRIVVLEDGKIVERGTHEELL 224
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
24-223 |
7.52e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 105.20 E-value: 7.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 24 IKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAMLPQMHDHQL-DLTVKELIEFGrgP 102
Cdd:PRK13647 28 IPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDPDDQVfSSTVWDDVAFG--P 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 103 HKLWRGRlnKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVHQLEVMELVKR 182
Cdd:PRK13647 106 VNMGLDK--DEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDR 183
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446549187 183 LNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPE 223
Cdd:PRK13647 184 LHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS 223
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-220 |
9.84e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 105.94 E-value: 9.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 18 QNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTmKSADVAKQLAMLpqM-HDHQL--DLTVKE 94
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFK-RRKEFARRIGVV--FgQRSQLwwDLPAID 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 95 LIEFGRG----PHKLWRGRLnkedEEIVDwalsVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDI 170
Cdd:COG4586 116 SFRLLKAiyriPDAEYKKRL----DELVE----LLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDV 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446549187 171 VHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDG 220
Cdd:COG4586 188 VSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDG 237
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
12-229 |
1.14e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 104.88 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 12 SERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAMLPQMHDHQL-DL 90
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPDDQIfSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 91 TVKELIEFGrgPHKLwrGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDI 170
Cdd:PRK13652 95 TVEQDIAFG--PINL--GLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446549187 171 VHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVLCHE 229
Cdd:PRK13652 171 QGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
19-231 |
1.35e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 105.17 E-value: 1.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 19 NMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSA------------------------DVA 74
Cdd:PRK13651 25 NVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTkekekvleklviqktrfkkikkikEIR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 75 KQLAMLPQMHDHQL-DLTVKELIEFGrgPHKLwrGRLNKEDEEIVDWALSVTNL-EGYEYRLLQSLSGGERQRAWIAMTL 152
Cdd:PRK13651 105 RRVGVVFQFAEYQLfEQTIEKDIIFG--PVSM--GVSKEEAKKRAAKYIELVGLdESYLQRSPFELSGGQKRRVALAGIL 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446549187 153 AQRTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVLCHEMF 231
Cdd:PRK13651 181 AMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDILSDNKF 258
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
19-197 |
1.63e-26 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 107.83 E-value: 1.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 19 NMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAMLPQmHDHQLDLTVKELIEF 98
Cdd:TIGR02868 353 GVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQ-DAHLFDTTVRENLRL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 99 GRGphklwrgrlNKEDEEIVdWALSVTNLE--------GYEYRLL---QSLSGGERQRAWIAMTLAQRTNVLLLDEPTTF 167
Cdd:TIGR02868 432 ARP---------DATDEELW-AALERVGLAdwlralpdGLDTVLGeggARLSGGERQRLALARALLADAPILLLDEPTEH 501
|
170 180 190
....*....|....*....|....*....|
gi 446549187 168 LDIVHQLEVMELVkrLNEEFGMTIIMVLHD 197
Cdd:TIGR02868 502 LDAETADELLEDL--LAALSGRTVVLITHH 529
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
23-216 |
1.76e-26 |
|
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: 107.85 E-value: 1.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 23 HIKAGEVVSLIGPNGSGKS----TLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAK----QLAMLPQ--M------Hdh 86
Cdd:COG4172 32 DIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgnRIAMIFQepMtslnplH-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 87 qldlTV-KELIEfgrgPHKLWRGrLNKED--EEIVDWaLSVTNLEGYEYRLLQ---SLSGGERQRAWIAMTLAQRTNVLL 160
Cdd:COG4172 110 ----TIgKQIAE----VLRLHRG-LSGAAarARALEL-LERVGIPDPERRLDAyphQLSGGQRQRVMIAMALANEPDLLI 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446549187 161 LDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKL 216
Cdd:COG4172 180 ADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEI 235
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
18-226 |
2.59e-26 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 103.24 E-value: 2.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 18 QNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSihtmkSADVAKQLAMLPqmhdhqlDLTVKELIE 97
Cdd:COG1134 43 KDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRV-----SALLELGAGFHP-------ELTGRENIY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 98 FgrgphklwRGRL---NKED-----EEIVDWAlsvtNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLD 169
Cdd:COG1134 111 L--------NGRLlglSRKEidekfDEIVEFA----ELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446549187 170 IVHQLEVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVL 226
Cdd:COG1134 179 AAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVI 234
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
18-216 |
2.65e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 107.03 E-value: 2.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 18 QNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHtMKSADVAKQL--AMLPQmhdH-QL--DLTV 92
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVR-IRSPRDAIALgiGMVHQ---HfMLvpNLTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 93 KELIEFGRGPHKLWRGRLNKEDEEIVdwALSvtnlEGYE-----YRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTF 167
Cdd:COG3845 98 AENIVLGLEPTKGGRLDRKAARARIR--ELS----ERYGldvdpDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446549187 168 LDIVHQLEVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKL 216
Cdd:COG3845 172 LTPQEADELFEILRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-216 |
2.90e-26 |
|
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: 100.58 E-value: 2.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 19 NMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTmKSADVAKQL--AMLPQmhdhqldltvkeli 96
Cdd:cd03216 18 GVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSF-ASPRDARRAgiAMVYQ-------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 97 efgrgphklwrgrlnkedeeivdwalsvtnlegyeyrllqsLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDiVHQLE- 175
Cdd:cd03216 83 -----------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALT-PAEVEr 120
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446549187 176 VMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKL 216
Cdd:cd03216 121 LFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
18-220 |
2.97e-26 |
|
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: 102.23 E-value: 2.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 18 QNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSihtmkSADVAKQLAMLPqmhdhqlDLTVKELIE 97
Cdd:cd03220 39 KDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV-----SSLLGLGGGFNP-------ELTGRENIY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 98 FgRGphkLWRGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVHQLEVM 177
Cdd:cd03220 107 L-NG---RLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQ 182
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446549187 178 ELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDG 220
Cdd:cd03220 183 RRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
9-228 |
4.21e-26 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 106.72 E-value: 4.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 9 YAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAMLPQmHDHQL 88
Cdd:TIGR02203 340 YPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQ-DVVLF 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 89 DLTVKELIEFGRGphklwrgrlNKEDEEIVDWALSVTNLEGYEYRL---LQS--------LSGGERQRAWIAMTLAQRTN 157
Cdd:TIGR02203 419 NDTIANNIAYGRT---------EQADRAEIERALAAAYAQDFVDKLplgLDTpigengvlLSGGQRQRLAIARALLKDAP 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446549187 158 VLLLDEPTTFLDIVHQLEVMELVKRLNEefGMTIIMVLHDINqAAQYSDRLLVLKRGKLQYDGIPEEVLCH 228
Cdd:TIGR02203 490 ILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLS-TIEKADRIVVMDDGRIVERGTHNELLAR 557
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
17-253 |
5.78e-26 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 103.04 E-value: 5.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 17 MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVakqLAMLPQMH--DHQLDLTVKE 94
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQSEevDWSFPVLVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 95 LIEFGRGPHKLWRGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVHQL 174
Cdd:PRK15056 100 VVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 175 EVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKrGKLQYDGIPEEVLCHEMFQHVF----------GIEVDIFQG 244
Cdd:PRK15056 180 RIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYTVMVK-GTVLASGPTETTFTAENLELAFsgvlrhvalnGSEESIITD 257
|
....*....
gi 446549187 245 SDKPFFTPK 253
Cdd:PRK15056 258 DERPFISHR 266
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-219 |
2.12e-25 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 100.91 E-value: 2.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 2 ISVNKVFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIvLDGksihTMKSADVAKQLAMLP 81
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAG----TAPLAEAREDTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 82 QmhDHQLdLTVKELIE-FGRGPHKLWRGRLNKedeeivdwALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLL 160
Cdd:PRK11247 88 Q--DARL-LPWKKVIDnVGLGLKGQWRDAALQ--------ALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446549187 161 LDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYD 219
Cdd:PRK11247 157 LDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLD 215
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
18-216 |
2.28e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 104.33 E-value: 2.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 18 QNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHtMKSADVAKQL--AMLPQmhDHQL--DLTVK 93
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVR-FRSPRDAQAAgiAIIHQ--ELNLvpNLSVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 94 ELIEFGRGPHKLW---RGRLNKEDEEI---VDWALSVTnlegyeyRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTF 167
Cdd:COG1129 98 ENIFLGREPRRGGlidWRAMRRRARELlarLGLDIDPD-------TPVGDLSVAQQQLVEIARALSRDARVLILDEPTAS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446549187 168 LDI--VHQLevMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKL 216
Cdd:COG1129 171 LTEreVERL--FRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
18-215 |
2.34e-25 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 104.38 E-value: 2.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 18 QNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKqSEGDIVLDGKSIHTMKSAdvakqlAMLPQMHDHQ---------L 88
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRR------ALRPLRRRMQvvfqdpfgsL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 89 D--LTVKELIEFGRGPHKLWRGRlnKEDEEIVDWALSVTNL-EGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPT 165
Cdd:COG4172 376 SprMTVGQIIAEGLRVHGPGLSA--AERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPT 453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446549187 166 TFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGK 215
Cdd:COG4172 454 SALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGK 503
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-226 |
2.51e-25 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 100.31 E-value: 2.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 18 QNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAMLPQmhDHQL-DLTVKELI 96
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQ--EPVLfDGTIAENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 97 EFGRGPhklwrgrlnKEDEEIVDWALS------VTNL-EGYEYRLLQ---SLSGGERQRAWIAMTLAQRTNVLLLDEPTT 166
Cdd:cd03249 98 RYGKPD---------ATDEEVEEAAKKanihdfIMSLpDGYDTLVGErgsQLSGGQKQRIAIARALLRNPKILLLDEATS 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 167 FLDIVHQLEVMELVKRLNEefGMTIIMVLHDINqAAQYSDRLLVLKRGKLQYDGIPEEVL 226
Cdd:cd03249 169 ALDAESEKLVQEALDRAMK--GRTTIVIAHRLS-TIRNADLIAVLQNGQVVEQGTHDELM 225
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-225 |
3.14e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 101.06 E-value: 3.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 2 ISVNKVFYAHSERFQMQ-----NMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSA----D 72
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEkkgldNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNknlkK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 73 VAKQLAMLPQMHDHQL-DLTVKELIEFgrGPHKLwrGRLNKEDEE-IVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAM 150
Cdd:PRK13641 83 LRKKVSLVFQFPEAQLfENTVLKDVEF--GPKNF--GFSEDEAKEkALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446549187 151 TLAQRTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEV 225
Cdd:PRK13641 159 VMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-228 |
3.90e-25 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 101.80 E-value: 3.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 1 MI---SVNKVFYAHSERFQ-MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAK- 75
Cdd:PRK11153 1 MIelkNISKVFPQGGRTIHaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 76 --QLAMLPQmHdhqLDL----TVKELIEFgrgPHKLwrgrLNKEDEEI---VDWALSVTNLEGYEYRLLQSLSGGERQRA 146
Cdd:PRK11153 81 rrQIGMIFQ-H---FNLlssrTVFDNVAL---PLEL----AGTPKAEIkarVTELLELVGLSDKADRYPAQLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 147 WIAMTLAQRTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVL 226
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVF 229
|
..
gi 446549187 227 CH 228
Cdd:PRK11153 230 SH 231
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-211 |
4.16e-25 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 99.09 E-value: 4.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 1 MISVNKVFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLK---QSEGDIVLDGKSIHTMKSAdvAKQL 77
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGRRLTALPAE--QRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 78 AMLPQMH---DHqldLTVKELIEFGRgPHKLwrGRLNKEDEeiVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQ 154
Cdd:COG4136 79 GILFQDDllfPH---LSVGENLAFAL-PPTI--GRAQRRAR--VEQALEEAGLAGFADRDPATLSGGQRARVALLRALLA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446549187 155 RTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSdRLLVL 211
Cdd:COG4136 151 EPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAG-RVLDL 206
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-226 |
4.27e-25 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 100.04 E-value: 4.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 2 ISVNKVFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSAD--------- 72
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDgqlkvadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 73 ----VAKQLAMLPQMHDHQLDLTVKELIEfgRGPHKLWRGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWI 148
Cdd:PRK10619 86 qlrlLRTRLTMVFQHFNLWSHMTVLENVM--EAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446549187 149 AMTLAQRTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVL 226
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLF 240
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-233 |
4.44e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 100.47 E-value: 4.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 1 MISVNKVFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVA--KQLA 78
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLAlrQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 79 MLPQMHDHQLDLT-VKELIEFGRGphklwrgRLNKEDEEI---VDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQ 154
Cdd:PRK13638 81 TVFQDPEQQIFYTdIDSDIAFSLR-------NLGVPEAEItrrVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 155 RTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVL-CHEMFQH 233
Cdd:PRK13638 154 QARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFaCTEAMEQ 232
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
24-222 |
5.05e-25 |
|
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: 103.71 E-value: 5.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 24 IKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKsihtmksadvakqLAMLPQMHDHQLDLTVKELIEFGRGPh 103
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK-------------ISYKPQYISPDYDGTVEEFLRSANTD- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 104 klwRGRLNKEDEEIVDwALSVTNLegYEyRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVHQLEVMELVKRL 183
Cdd:COG1245 429 ---DFGSSYYKTEIIK-PLGLEKL--LD-KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRF 501
|
170 180 190
....*....|....*....|....*....|....*....
gi 446549187 184 NEEFGMTIIMVLHDINQAAQYSDRLLVlkrgklqYDGIP 222
Cdd:COG1245 502 AENRGKTAMVVDHDIYLIDYISDRLMV-------FEGEP 533
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-229 |
5.86e-25 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 99.18 E-value: 5.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 1 MISVNKVfYAHSERFQ-MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQ-LA 78
Cdd:PRK11614 5 MLSFDKV-SAHYGKIQaLHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREaVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 79 MLPQMHDHQLDLTVKEliefgrgphKLWRGRLNKEDEEIVDWALSVTNL--EGYEYRLLQS--LSGGERQRAWIAMTLAQ 154
Cdd:PRK11614 84 IVPEGRRVFSRMTVEE---------NLAMGGFFAERDQFQERIKWVYELfpRLHERRIQRAgtMSGGEQQMLAIGRALMS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446549187 155 RTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVLCHE 229
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANE 228
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-220 |
6.79e-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: 6.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 4 VNKVFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKsihtmksadvaKQLAMLPQM 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG-----------LRIGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 84 HDHQLDLTVKELIEFGRGPHKLWRGRLNK-------EDEEIVDWALSVTNLE---GYEY-------------------RL 134
Cdd:COG0488 70 PPLDDDLTVLDTVLDGDAELRALEAELEEleaklaePDEDLERLAELQEEFEalgGWEAearaeeilsglgfpeedldRP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 135 LQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDI--VHQLEvmELVKRlneeFGMTIIMVLHD---INQAAqysDRLL 209
Cdd:COG0488 150 VSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLesIEWLE--EFLKN----YPGTVLVVSHDryfLDRVA---TRIL 220
|
250
....*....|..
gi 446549187 210 VLKRGKLQ-YDG 220
Cdd:COG0488 221 ELDRGKLTlYPG 232
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-226 |
8.76e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 100.08 E-value: 8.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 2 ISVNKVFYAHSER--FQ---MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDG-------KSIHTMK 69
Cdd:PRK13645 7 IILDNVSYTYAKKtpFEfkaLNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 70 saDVAKQLAMLPQMHDHQL-DLTVKELIEFGrgPHKLwrGRLNKEDEEIVDWALSVTNL-EGYEYRLLQSLSGGERQRAW 147
Cdd:PRK13645 87 --RLRKEIGLVFQFPEYQLfQETIEKDIAFG--PVNL--GENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446549187 148 IAMTLAQRTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVL 226
Cdd:PRK13645 161 LAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-225 |
2.06e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 99.03 E-value: 2.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 19 NMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIhtmkSADVAKQLAMLP-------QMhdhqldlT 91
Cdd:COG4152 19 DVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL----DPEDRRRIGYLPeerglypKM-------K 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 92 VKE-LIEFGRgphkLwRGrLNKED--EEIVDWaLSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFL 168
Cdd:COG4152 88 VGEqLVYLAR----L-KG-LSKAEakRRADEW-LERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446549187 169 DIVHQLEVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEV 225
Cdd:COG4152 161 DPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
18-220 |
2.56e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 101.68 E-value: 2.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 18 QNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLdGKSIhtmksadvakQLAMLPQMHDhQLDLTvKELIE 97
Cdd:COG0488 332 DDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------KIGYFDQHQE-ELDPD-KTVLD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 98 FgrgphkLWRGRLNKEDEEIVDWaLSVTNLEGYE-YRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIvhqlEV 176
Cdd:COG0488 399 E------LRDGAPGGTEQEVRGY-LGRFLFSGDDaFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDI----ET 467
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446549187 177 MELVKRLNEEFGMTIIMVLHD---INQAAqysDRLLVLKRGKLQ-YDG 220
Cdd:COG0488 468 LEALEEALDDFPGTVLLVSHDryfLDRVA---TRILEFEDGGVReYPG 512
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
24-222 |
2.57e-24 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 101.81 E-value: 2.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 24 IKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKsihtmksadvakqLAMLPQMHDHQLDLTVKELIE-----F 98
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK-------------ISYKPQYIKPDYDGTVEDLLRsitddL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 99 GRGPHKlwrgrlnkedEEIVDwALSVTNLegYEyRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVHQLEVME 178
Cdd:PRK13409 429 GSSYYK----------SEIIK-PLQLERL--LD-KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAK 494
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446549187 179 LVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVlkrgklqYDGIP 222
Cdd:PRK13409 495 AIRRIAEEREATALVVDHDIYMIDYISDRLMV-------FEGEP 531
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
18-216 |
3.32e-24 |
|
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: 97.12 E-value: 3.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 18 QNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMkSADvakQLAMLPQMH------DHQL--D 89
Cdd:COG4181 29 KGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAL-DED---ARARLRARHvgfvfqSFQLlpT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 90 LTVKE-----LIEFGRgphklwrgrlnKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEP 164
Cdd:COG4181 105 LTALEnvmlpLELAGR-----------RDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446549187 165 TTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDiNQAAQYSDRLLVLKRGKL 216
Cdd:COG4181 174 TGNLDAATGEQIIDLLFELNRERGTTLVLVTHD-PALAARCDRVLRLRAGRL 224
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-214 |
3.90e-24 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 97.46 E-value: 3.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 1 MISVNKVFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIhTMKSAD---VAKQL 77
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV-EGPGAErgvVFQNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 78 AMLPQmhdhqldLTVKELIEFG---RGPHKLWRgrlnkedEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQ 154
Cdd:PRK11248 80 GLLPW-------RNVQDNVAFGlqlAGVEKMQR-------LEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 155 RTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRG 214
Cdd:PRK11248 146 NPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
17-258 |
4.55e-24 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 100.11 E-value: 4.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 17 MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVA----KQLAMLPQMHDHQLDLTV 92
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 93 KELIEFGRGphklWRGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVH 172
Cdd:PRK10070 124 LDNTAFGME----LAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 173 QLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVLCHEMFQHV--FGIEVDIFQgsdkpFF 250
Cdd:PRK10070 200 RTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVrtFFRGVDISQ-----VF 274
|
....*...
gi 446549187 251 TPKRISKK 258
Cdd:PRK10070 275 SAKDIARR 282
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-226 |
5.12e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 97.43 E-value: 5.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 1 MISVNKVFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLK------QSEGDIVLDGKSIHTMKSADVA 74
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 75 KQLAMLPQMHDHQLDLTVKELIEFGRGPHKLwrgRLNKEDEEIVDWALSVTNLEGYEYRLLQS----LSGGERQRAWIAM 150
Cdd:PRK14246 90 KEVGMVFQQPNPFPHLSIYDNIAYPLKSHGI---KEKREIKKIVEECLRKVGLWKEVYDRLNSpasqLSGGQQQRLTIAR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446549187 151 TLAQRTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEfgMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVL 226
Cdd:PRK14246 167 ALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIF 240
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
9-226 |
6.06e-24 |
|
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: 96.79 E-value: 6.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 9 YAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAMLPQmHDHQL 88
Cdd:cd03252 10 YKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQ-ENVLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 89 DLTVKELIEFGRGPHKLWR----GRLNKEDEEIVDWAlsvtnlEGYEYRLLQ---SLSGGERQRAWIAMTLAQRTNVLLL 161
Cdd:cd03252 89 NRSIRDNIALADPGMSMERvieaAKLAGAHDFISELP------EGYDTIVGEqgaGLSGGQRQRIAIARALIHNPRILIF 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446549187 162 DEPTTFLDIVHQLEVMELVKRLNEefGMTIIMVLHDINqAAQYSDRLLVLKRGKLQYDGIPEEVL 226
Cdd:cd03252 163 DEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDELL 224
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
2-228 |
6.08e-24 |
|
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: 100.50 E-value: 6.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 2 ISVNKVFYAH--SERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAM 79
Cdd:TIGR01842 317 LSVENVTIVPpgGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGY 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 80 LPQmhDHQL-DLTVKELI-EFGRgphklwrgrlNKEDEEIVDWA-LS-----VTNLE-GYEYRLLQ---SLSGGERQRAW 147
Cdd:TIGR01842 397 LPQ--DVELfPGTVAENIaRFGE----------NADPEKIIEAAkLAgvhelILRLPdGYDTVIGPggaTLSGGQRQRIA 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 148 IAMTLAQRTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEfGMTIIMVLHDINqAAQYSDRLLVLKRGKLQYDGIPEEVLC 227
Cdd:TIGR01842 465 LARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITHRPS-LLGCVDKILVLQDGRIARFGERDEVLA 542
|
.
gi 446549187 228 H 228
Cdd:TIGR01842 543 K 543
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
18-256 |
6.59e-24 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 98.95 E-value: 6.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 18 QNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADvaKQLAMLPQMHDHQLDLTVKELIE 97
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE--RGVGMVFQSYALYPHLSVAENMS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 98 FGRgphKLwrGRLNKED-EEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVHQLEV 176
Cdd:PRK11000 98 FGL---KL--AGAKKEEiNQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQM 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 177 MELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVLCHEMFQHVFGievdiFQGSDKPFFTPKRIS 256
Cdd:PRK11000 173 RIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAG-----FIGSPKMNFLPVKVT 247
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
23-216 |
8.00e-24 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 98.27 E-value: 8.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 23 HIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVA---KQLAMLPQmhDHQ--LD--LTVKEL 95
Cdd:COG4608 40 DIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRplrRRMQMVFQ--DPYasLNprMTVGDI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 96 IEFGRGPHKLWRGrlnKEDEEIVDWALSVTNL-EGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVHQL 174
Cdd:COG4608 118 IAEPLRIHGLASK---AERRERVAELLELVGLrPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQA 194
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446549187 175 EVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKL 216
Cdd:COG4608 195 QVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKI 236
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-216 |
1.09e-23 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 95.71 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 1 MISVNKVFYAH-SERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVA---KQ 76
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPflrRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 77 LAMLPQMHDHQLDLTVKE-----LIEFGRGPHKLWRGrlnkedeeiVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMT 151
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDnvaipLIIAGASGDDIRRR---------VSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446549187 152 LAQRTNVLLLDEPTTFLDIvhqlEVMELVKRLNEEF---GMTIIMVLHDINQAAQYSDRLLVLKRGKL 216
Cdd:PRK10908 152 VVNKPAVLLADEPTGNLDD----ALSEGILRLFEEFnrvGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-236 |
3.13e-23 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 95.18 E-value: 3.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 1 MISVNKVFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKsihtMKSADVAKQLAMl 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK----LRIGYVPQKLYL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 81 pqmhDHQLDLTVKELIefgrgphklwRGRLNKEDEEIVDwALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLL 160
Cdd:PRK09544 79 ----DTTLPLTVNRFL----------RLRPGTKKEDILP-ALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLV 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446549187 161 LDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRgKLQYDGIPEEVLCHEMFQHVFG 236
Cdd:PRK09544 144 LDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEVVSLHPEFISMFG 218
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-256 |
3.36e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 96.03 E-value: 3.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 2 ISVNKVFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTmkSADVAKQ-LAML 80
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS--RARHARQrVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 81 PQMHDHQLDLTVKE-LIEFGRgphklWRGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVL 159
Cdd:PRK13537 86 PQFDNLDPDFTVREnLLVFGR-----YFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 160 LLDEPTTFLDIVHQLEVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVLCHEM---FQHVFG 236
Cdd:PRK13537 161 VLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEIgcdVIEIYG 239
|
250 260
....*....|....*....|
gi 446549187 237 IEVDIFQGSDKPFFTPKRIS 256
Cdd:PRK13537 240 PDPVALRDELAPLAERTEIS 259
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
7-206 |
3.86e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 95.23 E-value: 3.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 7 VFYAHSerFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARL--LKQS---EGDIVLDGKSIHT--MKSADVAKQLAM 79
Cdd:PRK14243 18 VYYGSF--LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGfrvEGKVTFHGKNLYApdVDPVEVRRRIGM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 80 LPQmHDHQLDLTVKELIEFGrgphklwrGRLN--KED-EEIVDWALSVTNL-EGYEYRLLQS---LSGGERQRAWIAMTL 152
Cdd:PRK14243 96 VFQ-KPNPFPKSIYDNIAYG--------ARINgyKGDmDELVERSLRQAALwDEVKDKLKQSglsLSGGQQQRLCIARAI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446549187 153 AQRTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEFgmTIIMVLHDINQAAQYSD 206
Cdd:PRK14243 167 AVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSD 218
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
7-216 |
4.52e-23 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 95.14 E-value: 4.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 7 VFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAK-----QL---- 77
Cdd:PRK10419 18 LSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAfrrdiQMvfqd 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 78 ---AMLPQMhdhqldlTVKELIefgRGP--HKLW---RGRLNKEDE--EIVDWALSVTNlegyeyRLLQSLSGGERQRAW 147
Cdd:PRK10419 98 sisAVNPRK-------TVREII---REPlrHLLSldkAERLARASEmlRAVDLDDSVLD------KRPPQLSGGQLQRVC 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446549187 148 IAMTLAQRTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKL 216
Cdd:PRK10419 162 LARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
8-216 |
7.86e-23 |
|
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: 94.49 E-value: 7.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 8 FYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSAD---VAKQLAML---- 80
Cdd:TIGR02769 18 FGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrraFRRDVQLVfqds 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 81 -----PQMhdhqldlTVKELIefgRGPHKLWRGRLNKEDEEIVDWALSVTNLEGYEY-RLLQSLSGGERQRAWIAMTLAQ 154
Cdd:TIGR02769 98 psavnPRM-------TVRQII---GEPLRHLTSLDESEQKARIAELLDMVGLRSEDAdKLPRQLSGGQLQRINIARALAV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446549187 155 RTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKL 216
Cdd:TIGR02769 168 KPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
19-235 |
1.18e-22 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 93.11 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 19 NMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQ-LAMLPQMHDHQLDLTVKELI- 96
Cdd:TIGR04406 19 DVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLgIGYLPQEASIFRKLTVEENIm 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 97 ---EFgrgPHKLWRGRLNKEDEEIVDwALSVTNLEGyeyRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVHQ 173
Cdd:TIGR04406 99 avlEI---RKDLDRAEREERLEALLE-EFQISHLRD---NKAMSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAV 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446549187 174 LEVMELVKRLnEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVLCHEMFQHVF 235
Cdd:TIGR04406 172 GDIKKIIKHL-KERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVRRVY 232
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
10-235 |
1.19e-22 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 93.42 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 10 AHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQ-LAMLPQMHDHQL 88
Cdd:PRK10895 12 AYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgIGYLPQEASIFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 89 DLTVKE----LIEFgrgphklwRGRLNKED-EEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDE 163
Cdd:PRK10895 92 RLSVYDnlmaVLQI--------RDDLSAEQrEDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446549187 164 PTTFLDIVHQLEVMELVKRLnEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVLCHEMFQHVF 235
Cdd:PRK10895 164 PFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVY 234
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-241 |
3.14e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 92.85 E-value: 3.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 17 MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEG-----DIVLDGKSIHTMKSA-DVAKQLAMLPQmHDHQLDL 90
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVlEFRRRVGMLFQ-RPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 91 TVKELIEFGRGPHKL-----WRGRLNKEDEEIVDWALSVTNLEGYEYRLlqslSGGERQRAWIAMTLAQRTNVLLLDEPT 165
Cdd:PRK14271 116 SIMDNVLAGVRAHKLvprkeFRGVAQARLTEVGLWDAVKDRLSDSPFRL----SGGQQQLLCLARTLAVNPEVLLLDEPT 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 166 TFLDIVHQLEVMELVKRLNEEfgMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVLCH----EMFQHVFGIEVDI 241
Cdd:PRK14271 192 SALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSpkhaETARYVAGLSGDV 269
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
19-225 |
3.78e-22 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 92.36 E-value: 3.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 19 NMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQlAMLPQMHDHQL--DLTVKELI 96
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM-GVVRTFQHVRLfrEMTVIENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 97 EFGRGPH---KLWRGRLN-----KEDEEIVDWA---LSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPT 165
Cdd:PRK11300 102 LVAQHQQlktGLFSGLLKtpafrRAESEALDRAatwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 166 TFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEV 225
Cdd:PRK11300 182 AGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 241
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
26-201 |
4.29e-22 |
|
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: 90.63 E-value: 4.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 26 AGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSAdVAKQLAMLPQMHDHQLDLTVKELIEFGRGPHkl 105
Cdd:cd03231 25 AGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDS-IARGLLYLGHAPGIKTTLSVLENLRFWHADH-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 106 wrgrlnkeDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVHQLEVMELVKRLNE 185
Cdd:cd03231 102 --------SDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCA 173
|
170
....*....|....*.
gi 446549187 186 EFGMTIIMVLHDINQA 201
Cdd:cd03231 174 RGGMVVLTTHQDLGLS 189
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
2-201 |
4.50e-22 |
|
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: 90.50 E-value: 4.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 2 ISVNKVFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSaDVAKQLAMLP 81
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD-EPHENILYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 82 QMHDHQLDLTVKELIEFgrgphklWRGRLNKEDEEIVDwALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLL 161
Cdd:TIGR01189 80 HLPGLKPELSALENLHF-------WAAIHGGAQRTIED-ALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWIL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446549187 162 DEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQA 201
Cdd:TIGR01189 152 DEPTTALDKAGVALLAGLLRAHLARGGIVLLTTHQDLGLV 191
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
17-220 |
6.05e-22 |
|
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: 90.00 E-value: 6.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 17 MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQS--EGDIVLDGKSihtmKSADVAKQLAMLPQMHDHQLDLTVKE 94
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRP----LDKNFQRSTGYVEQQDVHSPNLTVRE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 95 LIEFgrgpHKLWRGrlnkedeeivdwalsvtnlegyeyrllqsLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVHQL 174
Cdd:cd03232 99 ALRF----SALLRG-----------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAY 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446549187 175 EVMELVKRLNEEfGMTIIMVLHDINQAA-QYSDRLLVLKR-GKLQYDG 220
Cdd:cd03232 146 NIVRFLKKLADS-GQAILCTIHQPSASIfEKFDRLLLLKRgGKTVYFG 192
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
17-217 |
1.15e-21 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 90.65 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 17 MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAK----QLAMLPQMHDHQLDLTV 92
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAElrnqKLGFIYQFHHLLPDFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 93 KELIEFGRGPHKLWRGRLNKEDEEIvdwaLSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVH 172
Cdd:PRK11629 105 LENVAMPLLIGKKKPAEINSRALEM----LAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446549187 173 QLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSdRLLVLKRGKLQ 217
Cdd:PRK11629 181 ADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGRLT 224
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
6-220 |
1.17e-21 |
|
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: 89.63 E-value: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 6 KVFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLK---QSEGDIVLDGKSIHTMKSADVAkQLAMLPQ 82
Cdd:cd03233 12 TTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEgnvSVEGDIHYNGIPYKEFAEKYPG-EIIYVSE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 83 MHDHQLDLTVKELIEFgrgphklwrgrlnkedeeivdwalsVTNLEGYEYrlLQSLSGGERQRAWIAMTLAQRTNVLLLD 162
Cdd:cd03233 91 EDVHFPTLTVRETLDF-------------------------ALRCKGNEF--VRGISGGERKRVSIAEALVSRASVLCWD 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446549187 163 EPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHdinQAAQ--YS--DRLLVLKRGKLQYDG 220
Cdd:cd03233 144 NSTRGLDSSTALEILKCIRTMADVLKTTTFVSLY---QASDeiYDlfDKVLVLYEGRQIYYG 202
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
24-217 |
1.20e-21 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 90.22 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 24 IKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTM----KSADVAKQLAMLPQMHDHQLDLTVKELIEFG 99
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeeaRAKLRAKHVGFVFQSFMLIPTLNALENVELP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 100 rgphKLWRGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVHQLEVMEL 179
Cdd:PRK10584 113 ----ALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADL 188
|
170 180 190
....*....|....*....|....*....|....*...
gi 446549187 180 VKRLNEEFGMTIIMVLHDiNQAAQYSDRLLVLKRGKLQ 217
Cdd:PRK10584 189 LFSLNREHGTTLILVTHD-LQLAARCDRRLRLVNGQLQ 225
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
4-225 |
1.44e-21 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 93.77 E-value: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 4 VNKVFYAHSERFQ-MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDG--------KSIHTMKSADVA 74
Cdd:PRK10261 18 LNIAFMQEQQKIAaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrQVIELSEQSAAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 75 KQ------LAMLPQMHDHQLD--LTVKELI-EFGRGPHKLWRGRLNKEDEEIVDwALSVTNLEGYEYRLLQSLSGGERQR 145
Cdd:PRK10261 98 MRhvrgadMAMIFQEPMTSLNpvFTVGEQIaESIRLHQGASREEAMVEAKRMLD-QVRIPEAQTILSRYPHQLSGGMRQR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 146 AWIAMTLAQRTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEV 225
Cdd:PRK10261 177 VMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-226 |
1.44e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 91.33 E-value: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 1 MISVNKVFYAHSERF-----QMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEG-----DIVLDGKSiHTMKS 70
Cdd:PRK13643 1 MIKFEKVNYTYQPNSpfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGkvtvgDIVVSSTS-KQKEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 71 ADVAKQLAMLPQMHDHQL-DLTVKELIEFGrgPHKLwrGRLNKEDEEIVDWALSVTNL--EGYEYRLLQsLSGGERQRAW 147
Cdd:PRK13643 80 KPVRKKVGVVFQFPESQLfEETVLKDVAFG--PQNF--GIPKEKAEKIAAEKLEMVGLadEFWEKSPFE-LSGGQMRRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446549187 148 IAMTLAQRTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVL 226
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
20-244 |
1.55e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 92.20 E-value: 1.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 20 MNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKqLAMLPQMHDHQLDLTVKE-LIEF 98
Cdd:PRK13536 60 LSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARAR-IGVVPQFDNLDLEFTVREnLLVF 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 99 GRgphklWRGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVHQLEVME 178
Cdd:PRK13536 139 GR-----YFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWE 213
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446549187 179 LVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPeevlcHEMFQHVFGIEV-DIFQG 244
Cdd:PRK13536 214 RLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRP-----HALIDEHIGCQViEIYGG 274
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-215 |
1.94e-21 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 87.50 E-value: 1.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 2 ISVNKVFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIvldgKSIHTMKsadvakqLAMLP 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV----TWGSTVK-------IGYFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 82 QmhdhqldltvkeliefgrgphklwrgrlnkedeeivdwalsvtnlegyeyrllqsLSGGERQRAWIAMTLAQRTNVLLL 161
Cdd:cd03221 70 Q-------------------------------------------------------LSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446549187 162 DEPTTFLDIVHQLEVMELVKrlneEFGMTIIMVLHD---INQAAqysDRLLVLKRGK 215
Cdd:cd03221 95 DEPTNHLDLESIEALEEALK----EYPGTVILVSHDryfLDQVA---TKIIELEDGK 144
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
19-228 |
2.87e-21 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 91.32 E-value: 2.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 19 NMNVHIKAGEVVSLIGPNGSGKS-TLLRLIARLLKQS--EGDIVLDGKSIHTMKSADV----AKQLAMLPQ--MHDHQLD 89
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANGriGGSATFNGREILNLPEKELnklrAEQISMIFQdpMTSLNPY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 90 LTVKE-LIEFGRgPHKlwrgRLNKEDEeivdWALSVTNLEGY---EYRLLQSL-----SGGERQRAWIAMTLAQRTNVLL 160
Cdd:PRK09473 114 MRVGEqLMEVLM-LHK----GMSKAEA----FEESVRMLDAVkmpEARKRMKMyphefSGGMRQRVMIAMALLCRPKLLI 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446549187 161 LDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVLCH 228
Cdd:PRK09473 185 ADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQ 252
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
17-220 |
4.87e-21 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 92.48 E-value: 4.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 17 MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAMLPQmhdhqldltvkELI 96
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQ-----------EPV 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 97 EFGRG-PHKLWRGRLNKEDEEIVDWALS------VTNLE-GYEYRL---LQSLSGGERQRAWIAMTLAQRTNVLLLDEPT 165
Cdd:TIGR00958 566 LFSGSvRENIAYGLTDTPDEEIMAAAKAanahdfIMEFPnGYDTEVgekGSQLSGGQKQRIAIARALVRKPRVLILDEAT 645
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446549187 166 TFLDIvhqlEVMELVKRLNEEFGMTIIMVLHDInQAAQYSDRLLVLKRGKLQYDG 220
Cdd:TIGR00958 646 SALDA----ECEQLLQESRSRASRTVLLIAHRL-STVERADQILVLKKGSVVEMG 695
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
17-219 |
5.12e-21 |
|
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: 88.24 E-value: 5.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 17 MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAMLPQmhDHQL-DLTVKEL 95
Cdd:cd03369 24 LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQ--DPTLfSGTIRSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 96 IEfgrgphklwrgRLNKEDEEIVDWALSVTnlEGYEyrllqSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVHQLE 175
Cdd:cd03369 102 LD-----------PFDEYSDEEIYGALRVS--EGGL-----NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446549187 176 VMELVKrlnEEF-GMTIIMVLHDINQAAQYsDRLLVLKRGKL-QYD 219
Cdd:cd03369 164 IQKTIR---EEFtNSTILTIAHRLRTIIDY-DKILVMDAGEVkEYD 205
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
7-207 |
5.75e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 89.06 E-value: 5.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 7 VFYAHSERFQMQNMNVHIKagEVVSLIGPNGSGKSTLLRLIARLLK-----QSEGDIVLDGKSIHTMK--SADVAKQLAM 79
Cdd:PRK14239 13 VYYNKKKALNSVSLDFYPN--EITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYSPRtdTVDLRKEIGM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 80 LPQmHDHQLDLTVKELIEFGRgphklwrgRLNKE-DEEIVDWALSvTNLEGYEY------RLLQS---LSGGERQRAWIA 149
Cdd:PRK14239 91 VFQ-QPNPFPMSIYENVVYGL--------RLKGIkDKQVLDEAVE-KSLKGASIwdevkdRLHDSalgLSGGQQQRVCIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446549187 150 MTLAQRTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEFgmTIIMVLHDINQAAQYSDR 207
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDR 216
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-198 |
6.77e-21 |
|
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: 88.96 E-value: 6.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 25 KAGEVVSLIGPNGSGKSTLLRLIARLLKQSEG--------DIVLD---GKSIHT----MKSADVakQLAMLPQMHDH--- 86
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGkfddppdwDEILDefrGSELQNyftkLLEGDV--KVIVKPQYVDLipk 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 87 QLDLTVKELIEfgrgpHKLWRGRLnkedEEIVDwalsVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTT 166
Cdd:cd03236 102 AVKGKVGELLK-----KKDERGKL----DELVD----QLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSS 168
|
170 180 190
....*....|....*....|....*....|..
gi 446549187 167 FLDIVHQLEVMELVKRLNEEfGMTIIMVLHDI 198
Cdd:cd03236 169 YLDIKQRLNAARLIRELAED-DNYVLVVEHDL 199
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
18-216 |
1.05e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 90.85 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 18 QNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSAD-VAKQLAMLPQMHDHQ---LDLTVK 93
Cdd:COG1129 269 RDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRAGIAYVPEDRKGEglvLDLSIR 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 94 ELIEFGRGPHKLWRGRLN--KEDEEIVDW--ALSV--TNLEgyeyRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTF 167
Cdd:COG1129 349 ENITLASLDRLSRGGLLDrrRERALAEEYikRLRIktPSPE----QPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRG 424
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446549187 168 LDIVHQLEVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKL 216
Cdd:COG1129 425 IDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-228 |
1.16e-20 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 88.27 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 1 MISVNKVFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIaRLLKQSE------GDIVLDGksihtmkSADVA 74
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCI-NLLEQPEagtirvGDITIDT-------ARSLS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 75 KQLAMLPQMHDH------QLDL----TVKE-LIEfgrGPhKLWRGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGER 143
Cdd:PRK11264 75 QQKGLIRQLRQHvgfvfqNFNLfphrTVLEnIIE---GP-VIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 144 QRAWIAMTLAQRTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPE 223
Cdd:PRK11264 151 QRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAK 229
|
....*
gi 446549187 224 EVLCH 228
Cdd:PRK11264 230 ALFAD 234
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
14-222 |
3.15e-20 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 90.46 E-value: 3.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 14 RFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTmkSADVAKQ-LAMLPQMHDHQLDLTV 92
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET--NLDAVRQsLGMCPQHNILFHHLTV 1020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 93 KELIEFgrgpHKLWRGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVH 172
Cdd:TIGR01257 1021 AEHILF----YAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYS 1096
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446549187 173 QLEVMELVkrLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIP 222
Cdd:TIGR01257 1097 RRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
19-219 |
3.77e-20 |
|
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: 86.01 E-value: 3.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 19 NMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAMLPQmhDHQL-DLTVKELIE 97
Cdd:cd03244 22 NISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQ--DPVLfSGTIRSNLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 98 fgrgPHKLWrgrlnkEDEEIVD-------WALSVTNLEGYEYRLLQS---LSGGERQRAWIAMTLAQRTNVLLLDEPTTF 167
Cdd:cd03244 100 ----PFGEY------SDEELWQalervglKEFVESLPGGLDTVVEEGgenLSVGQRQLLCLARALLRKSKILVLDEATAS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446549187 168 LDIvhqlEVMELVKR-LNEEF-GMTIIMVLHDINQAAQYsDRLLVLKRGKL-QYD 219
Cdd:cd03244 170 VDP----ETDALIQKtIREAFkDCTVLTIAHRLDTIIDS-DRILVLDKGRVvEFD 219
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-198 |
3.88e-20 |
|
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: 89.46 E-value: 3.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 25 KAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDI--------VLD---GKSIHTMKSADVAKQL--AMLPQMHD---HQL 88
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYdeepswdeVLKrfrGTELQDYFKKLANGEIkvAHKPQYVDlipKVF 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 89 DLTVKELiefgrgphklwrgrLNKEDE-----EIVDwALSVTNLEGyeyRLLQSLSGGERQRAWIAMTLAQRTNVLLLDE 163
Cdd:COG1245 177 KGTVREL--------------LEKVDErgkldELAE-KLGLENILD---RDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190
....*....|....*....|....*....|....*
gi 446549187 164 PTTFLDIVHQLEVMELVKRLNEEfGMTIIMVLHDI 198
Cdd:COG1245 239 PSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDL 272
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
21-214 |
4.22e-20 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 87.84 E-value: 4.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 21 NVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSA---DVAKQLAMLPQMHDHQLD--LTVKEL 95
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDewrAVRSDIQMIFQDPLASLNprMTIGEI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 96 IEfgrGPHKLWRGRLNKED--EEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVHQ 173
Cdd:PRK15079 121 IA---EPLRTYHPKLSRQEvkDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQ 197
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446549187 174 LEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRG 214
Cdd:PRK15079 198 AQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLG 238
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
12-215 |
4.66e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 89.38 E-value: 4.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 12 SERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQS-----EGDIVLDGKSihtMKSADVAK-------QLAM 79
Cdd:PRK15134 20 TVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGES---LLHASEQTlrgvrgnKIAM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 80 L---PQMHDHQLDLTVKELIEFgrgpHKLWRG-RLNKEDEEIVDwALSVTNLEGYEYRLL---QSLSGGERQRAWIAMTL 152
Cdd:PRK15134 97 IfqePMVSLNPLHTLEKQLYEV----LSLHRGmRREAARGEILN-CLDRVGIRQAAKRLTdypHQLSGGERQRVMIAMAL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446549187 153 AQRTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGK 215
Cdd:PRK15134 172 LTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
21-225 |
5.61e-20 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 87.98 E-value: 5.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 21 NVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSAD-----VAKQLAMLPQMhdhqldlTVKEL 95
Cdd:PRK11650 24 DLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADrdiamVFQNYALYPHM-------SVREN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 96 IEFG---RGPHKlwrgrlnkedEEI---VDWALSVTNLEGYEYRLLQSLSGGERQRawIAMTLA--QRTNVLLLDEPTTF 167
Cdd:PRK11650 97 MAYGlkiRGMPK----------AEIeerVAEAARILELEPLLDRKPRELSGGQRQR--VAMGRAivREPAVFLFDEPLSN 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 168 LDIvhQLEV-MEL-VKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEV 225
Cdd:PRK11650 165 LDA--KLRVqMRLeIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEV 222
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
18-216 |
5.80e-20 |
|
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: 84.41 E-value: 5.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 18 QNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQ-LAMLPQmhDHQ-----LDLT 91
Cdd:cd03215 17 RDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPE--DRKreglvLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 92 VKEliefgrgphklwrgrlnkedeeivdwalsvtNLegyeyRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIV 171
Cdd:cd03215 95 VAE-------------------------------NI-----ALSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446549187 172 HQLEVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKL 216
Cdd:cd03215 139 AKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-216 |
2.13e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 87.57 E-value: 2.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 2 ISVNKVFYAHSERFQ--MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAM 79
Cdd:PRK11160 339 LTLNNVSFTYPDQPQpvLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 80 LPQmHDHQLDLTVKEliefgrgphKLWRGRLNKEDEEIVDwALSVTNLEgyeyRLLQS--------------LSGGERQR 145
Cdd:PRK11160 419 VSQ-RVHLFSATLRD---------NLLLAAPNASDEALIE-VLQQVGLE----KLLEDdkglnawlgeggrqLSGGEQRR 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446549187 146 AWIAMTLAQRTNVLLLDEPTTFLDIVHQLEVMELvkrLNEEF-GMTIIMVLHDINQAAQYsDRLLVLKRGKL 216
Cdd:PRK11160 484 LGIARALLHDAPLLLLDEPTEGLDAETERQILEL---LAEHAqNKTVLMITHRLTGLEQF-DRICVMDNGQI 551
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-225 |
2.26e-19 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 84.82 E-value: 2.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 1 MISVNKVFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSA---DVAKQL 77
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSrlyTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 78 AMLPQMHDHQLDLTVKE-----LIEFGRGPHKLWRgrlnkedeEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTL 152
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDnvaypLREHTQLPAPLLH--------STVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446549187 153 AQRTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEV 225
Cdd:PRK11831 159 ALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-201 |
2.53e-19 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 84.00 E-value: 2.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 1 MISVNKVFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAML 80
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 81 PQMHDHQLDlTVKELIEFgrgPhklWRGRLNKEDEE-----IVDWALSVTNLEgyeyRLLQSLSGGERQRAWIAMTLAQR 155
Cdd:PRK10247 87 AQTPTLFGD-TVYDNLIF---P---WQIRNQQPDPAiflddLERFALPDTILT----KNIAELSGGEKQRISLIRNLQFM 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446549187 156 TNVLLLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHD---INQA 201
Cdd:PRK10247 156 PKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDkdeINHA 204
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
17-216 |
2.90e-19 |
|
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: 83.67 E-value: 2.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 17 MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAMLPQmhDHQL-DLTVKEL 95
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQ--EPVLfARSLQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 96 IEFGRGphklwrgrlNKEDEEIVDWALS------VTNLE-GYEYRLLQS---LSGGERQRAWIAMTLAQRTNVLLLDEPT 165
Cdd:cd03248 108 IAYGLQ---------SCSFECVKEAAQKahahsfISELAsGYDTEVGEKgsqLSGGQKQRVAIARALIRNPQVLILDEAT 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446549187 166 TFLDIVHQLEVMELVKRLNEEfgMTIIMVLHDINqAAQYSDRLLVLKRGKL 216
Cdd:cd03248 179 SALDAESEQQVQQALYDWPER--RTVLVIAHRLS-TVERADQILVLDGGRI 226
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-226 |
3.55e-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: 86.72 E-value: 3.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 2 ISVNKVFYAHS-ERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAML 80
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 81 PQmHDHQLDLTVKELIEFGRGPhklwrgrlNKEDEEI---VDWALSVTNLE----GYEYRLLQ---SLSGGERQRAWIAM 150
Cdd:TIGR01193 554 PQ-EPYIFSGSILENLLLGAKE--------NVSQDEIwaaCEIAEIKDDIEnmplGYQTELSEegsSISGGQKQRIALAR 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446549187 151 TLAQRTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEfgmTIIMVLHDINQAAQySDRLLVLKRGKLQYDGIPEEVL 226
Cdd:TIGR01193 625 ALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDELL 696
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
17-233 |
4.17e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 86.30 E-value: 4.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 17 MQNMNVHIKAGEVVSLIGPNGSGKST----LLRLIArllkqSEGDIVLDGKSIHTMKSadvaKQlaMLPQMHDHQL---- 88
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNR----RQ--LLPVRHRIQVvfqd 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 89 -------DLTVKELIEFGRGPHklwRGRLN-KEDEEIVDWALSVTNLE-GYEYRLLQSLSGGERQRAWIAMTLAQRTNVL 159
Cdd:PRK15134 371 pnsslnpRLNVLQIIEEGLRVH---QPTLSaAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLI 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446549187 160 LLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKlqydgIPEEVLCHEMFQH 233
Cdd:PRK15134 448 ILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGE-----VVEQGDCERVFAA 516
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-206 |
4.73e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 83.93 E-value: 4.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 2 ISVNKVFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLlKQSEGDIVLDGK------SIHTMKSA--DV 73
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM-NELESEVRVEGRveffnqNIYERRVNlnRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 74 AKQLAML---PQMhdhqLDLTVKELIEFGRgphKL--WRGRLnkEDEEIVDWALSVTNL-EGYEYRLLQS---LSGGERQ 144
Cdd:PRK14258 87 RRQVSMVhpkPNL----FPMSVYDNVAYGV---KIvgWRPKL--EIDDIVESALKDADLwDEIKHKIHKSaldLSGGQQQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446549187 145 RAWIAMTLAQRTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSD 206
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
18-230 |
7.37e-19 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 82.77 E-value: 7.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 18 QNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTM---KSAdvakQLAM--LPQmhDHQL--DL 90
Cdd:COG1137 20 KDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLpmhKRA----RLGIgyLPQ--EASIfrKL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 91 TVKELI----EFgRGPHKlwrgrlnKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTT 166
Cdd:COG1137 94 TVEDNIlavlEL-RKLSK-------KEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446549187 167 FLDIVHQLEVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVLCHEM 230
Cdd:COG1137 166 GVDPIAVADIQKIIRHLKER-GIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPL 228
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
17-224 |
7.43e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 85.93 E-value: 7.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 17 MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSadvaKQLAMLPQMH-------DHQLD 89
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDA----DALAQLRREHfgfifqrYHLLS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 90 -LTVKELIEF-----GRGPHKlwrgRLNKEDEEIVDWALSvtnlEGYEYRLLQsLSGGERQRAWIAMTLAQRTNVLLLDE 163
Cdd:PRK10535 100 hLTAAQNVEVpavyaGLERKQ----RLLRAQELLQRLGLE----DRVEYQPSQ-LSGGQQQRVSIARALMNGGQVILADE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446549187 164 PTTFLDIVHQLEVMELVKRLNEEfGMTIIMVLHDINQAAQySDRLLVLKRGKLQYDGIPEE 224
Cdd:PRK10535 171 PTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPPAQE 229
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-216 |
9.23e-19 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 82.75 E-value: 9.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 2 ISVNKV--FY-AHSERFqmqNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADvAKQLA 78
Cdd:PRK11124 3 IQLNGIncFYgAHQALF---DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPS-DKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 79 MLPQ---MHDHQLDL----TVKE-LIEfgrGPHKLwRGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAM 150
Cdd:PRK11124 79 ELRRnvgMVFQQYNLwphlTVQQnLIE---APCRV-LGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446549187 151 TLAQRTNVLLLDEPTTFLD--IVHQleVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKL 216
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAALDpeITAQ--IVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
15-226 |
1.13e-18 |
|
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: 85.77 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 15 FQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAMLPQmhdhqldltvkE 94
Cdd:TIGR00957 1300 LVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQ-----------D 1368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 95 LIEFGrGPHKLWRGRLNKEDEEIVDWALSVTNLEGYEYRLL-----------QSLSGGERQRAWIAMTLAQRTNVLLLDE 163
Cdd:TIGR00957 1369 PVLFS-GSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPdkldhecaeggENLSVGQRQLVCLARALLRKTKILVLDE 1447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446549187 164 PTTFLDivhqLEVMELVKR-LNEEF-GMTIIMVLHDINQAAQYSdRLLVLKRGKLQYDGIPEEVL 226
Cdd:TIGR00957 1448 ATAAVD----LETDNLIQStIRTQFeDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLL 1507
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
24-216 |
1.17e-18 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 82.83 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 24 IKAGEVVSLIGPNGSGKS----TLLRLIARLLKQSEGDIVLDGKSIH--TMKSADVAKQL-----AMLP--QMHDHQldl 90
Cdd:PRK10418 26 LQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVApcALRGRKIATIMqnprsAFNPlhTMHTHA--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 91 tvkelIEFGRGphklwRGRLNKEDEEIVdwALSVTNLEGYEyRLLQS----LSGGERQRAWIAMTLAQRTNVLLLDEPTT 166
Cdd:PRK10418 103 -----RETCLA-----LGKPADDATLTA--ALEAVGLENAA-RVLKLypfeMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446549187 167 FLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKL 216
Cdd:PRK10418 170 DLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
24-198 |
3.70e-18 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 83.70 E-value: 3.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 24 IKAGEVVSLIGPNGSGKSTLLRLIARLLK------QSEGDI--VLD---GKSIHTMKSADVAKQL--AMLPQMHD---HQ 87
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIpnlgdyEEEPSWdeVLKrfrGTELQNYFKKLYNGEIkvVHKPQYVDlipKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 88 LDLTVKELiefgrgphklwrgrLNKEDEE-IVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTT 166
Cdd:PRK13409 176 FKGKVREL--------------LKKVDERgKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTS 241
|
170 180 190
....*....|....*....|....*....|..
gi 446549187 167 FLDIVHQLEVMELVKRLNEefGMTIIMVLHDI 198
Cdd:PRK13409 242 YLDIRQRLNVARLIRELAE--GKYVLVVEHDL 271
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
27-226 |
7.64e-18 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 80.36 E-value: 7.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 27 GEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKS-----IHTMKSAdvakQLAMLPQ-----MHDHQLD---LTV- 92
Cdd:PRK11701 32 GEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrdLYALSEA----ERRRLLRtewgfVHQHPRDglrMQVs 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 93 ------KELIEFGrgphklWR--GRLNkedEEIVDWalsvtnLEGYEYRLLQ------SLSGGERQRAWIAMTLAQRTNV 158
Cdd:PRK11701 108 aggnigERLMAVG------ARhyGDIR---ATAGDW------LERVEIDAARiddlptTFSGGMQQRLQIARNLVTHPRL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446549187 159 LLLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVL 226
Cdd:PRK11701 173 VFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVL 240
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
20-183 |
1.01e-17 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 79.51 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 20 MNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGksiHTMKSADVAKQLAMLPQMHDHQLDLTVKELIEFG 99
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDG---KTATRGDRSRFMAYLGHLPGLKADLSTLENLHFL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 100 RGPHklwrGRLNKedeEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDivhqLEVMEL 179
Cdd:PRK13543 107 CGLH----GRRAK---QMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD----LEGITL 175
|
....
gi 446549187 180 VKRL 183
Cdd:PRK13543 176 VNRM 179
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
18-197 |
1.07e-17 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 82.25 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 18 QNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIvldgksihtmKSADVAkQLAMLPQMHDHQL--DLTVKEL 95
Cdd:PRK15064 336 KNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV----------KWSENA-NIGYYAQDHAYDFenDLTLFDW 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 96 IEFGRGPhklwrgrlnKEDEEIVDWALSvtnlegyeyRLLQS----------LSGGERQRAWIAMTLAQRTNVLLLDEPT 165
Cdd:PRK15064 405 MSQWRQE---------GDDEQAVRGTLG---------RLLFSqddikksvkvLSGGEKGRMLFGKLMMQKPNVLVMDEPT 466
|
170 180 190
....*....|....*....|....*....|....*
gi 446549187 166 TFLDivhqlevMELVKRLN---EEFGMTIIMVLHD 197
Cdd:PRK15064 467 NHMD-------MESIESLNmalEKYEGTLIFVSHD 494
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
18-229 |
1.47e-17 |
|
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: 78.72 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 18 QNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARL--LKQSEGDIVLDGKSIhtmksadvakqlamlpqmhdhqLDLTVKEl 95
Cdd:cd03217 17 KGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDI----------------------TDLPPEE- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 96 iefgrgphklwRGRLN-----KEDEEIVdwalSVTNLEgyeyrLLQSL----SGGERQRAWIAMTLAQRTNVLLLDEPTT 166
Cdd:cd03217 74 -----------RARLGiflafQYPPEIP----GVKNAD-----FLRYVnegfSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446549187 167 FLDIVHQLEVMELVKRLNEEfGMTIIMVLHdINQAAQY--SDRLLVLKRGKLQYDGIPEEVLCHE 229
Cdd:cd03217 134 GLDIDALRLVAEVINKLREE-GKSVLIITH-YQRLLDYikPDRVHVLYDGRIVKSGDKELALEIE 196
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
17-214 |
1.95e-17 |
|
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: 79.02 E-value: 1.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 17 MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDgksiHTMKSADVAK------------------Q-L 77
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVR----HDGGWVDLAQaspreilalrrrtigyvsQfL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 78 AMLPQMHdhQLDLTVKELIEFGRGPH------KLWRGRLNKeDEEIvdWALSVTNLegyeyrllqslSGGERQRAWIAMT 151
Cdd:COG4778 103 RVIPRVS--ALDVVAEPLLERGVDREeararaRELLARLNL-PERL--WDLPPATF-----------SGGEQQRVNIARG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446549187 152 LAQRTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRG 214
Cdd:COG4778 167 FIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-216 |
2.48e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 81.20 E-value: 2.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 19 NMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSAD-VAKQLAMLPQMHDHQ---LDLTVKE 94
Cdd:PRK10762 270 DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDgLANGIVYISEDRKRDglvLGMSVKE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 95 ------LIEFGRGPhklwrGRLNKEDEEI-VDWALSVTNLEGYEY-RLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTT 166
Cdd:PRK10762 350 nmsltaLRYFSRAG-----GSLKHADEQQaVSDFIRLFNIKTPSMeQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTR 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446549187 167 FLDIVHQLEVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKL 216
Cdd:PRK10762 425 GVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
23-224 |
3.83e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 80.86 E-value: 3.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 23 HIKAGEVVSLIGPNGSGKSTLLRLIA-RLLKQSE--GDIVLDGKSIhtmkSADVAKQLAMLPQMHDHQL-DLTVKELIEF 98
Cdd:TIGR00955 47 VAKPGELLAVMGSSGAGKTTLMNALAfRSPKGVKgsGSVLLNGMPI----DAKEMRAISAYVQQDDLFIpTLTVREHLMF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 99 gRGPHKLWRGRLNKEDEEIVDWALSVTNLE-------GYEYRLlQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIV 171
Cdd:TIGR00955 123 -QAHLRMPRRVTKKEKRERVDEVLQALGLRkcantriGVPGRV-KGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSF 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 172 HQLEVMELVKRLNEEfGMTIIMVLHdinqaaQYS-------DRLLVLKRGKLQYDGIPEE 224
Cdd:TIGR00955 201 MAYSVVQVLKGLAQK-GKTIICTIH------QPSselfelfDKIILMAEGRVAYLGSPDQ 253
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-216 |
3.88e-17 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 78.13 E-value: 3.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 2 ISVNKV--FYAHSErfQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKS------IHTMKSADV 73
Cdd:COG4161 3 IQLKNIncFYGSHQ--ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdfsqkPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 74 AKQLAMLPQMHDHQLDLTVKE-LIEfgrGPHKLWRgrLNKED-EEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMT 151
Cdd:COG4161 81 RQKVGMVFQQYNLWPHLTVMEnLIE---APCKVLG--LSKEQaREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446549187 152 LAQRTNVLLLDEPTTFLD--IVHQleVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKL 216
Cdd:COG4161 156 LMMEPQVLLFDEPTAALDpeITAQ--VVEIIRELSQT-GITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
32-239 |
4.00e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 79.51 E-value: 4.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 32 LIGPNGSGKSTLLRLIARLLKQSEGDI------------VLDGKSIHTMKSADVAKQL----AMLPQMHDHQL-DLTVKE 94
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyigdkknNHELITNPYSKKIKNFKELrrrvSMVFQFPEYQLfKDTIEK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 95 LIEFGrgPHKLwrGRLNKEDEEIVDWALsvtNLEGYEYRLLQ----SLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDI 170
Cdd:PRK13631 137 DIMFG--PVAL--GVKKSEAKKLAKFYL---NKMGLDDSYLErspfGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDP 209
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446549187 171 VHQLEVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVLCHEMFQHVFGIEV 239
Cdd:PRK13631 210 KGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQHIINSTSIQV 277
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
24-211 |
5.32e-17 |
|
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: 76.46 E-value: 5.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 24 IKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIhtmksadvakqlAMLPQMHDhqldltvkeliefgrgph 103
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITP------------VYKPQYID------------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 104 klwrgrlnkedeeivdwalsvtnlegyeyrllqsLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVHQLEVMELVKRL 183
Cdd:cd03222 72 ----------------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117
|
170 180
....*....|....*....|....*...
gi 446549187 184 NEEFGMTIIMVLHDINQAAQYSDRLLVL 211
Cdd:cd03222 118 SEEGKKTALVVEHDLAVLDYLSDRIHVF 145
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
8-229 |
8.75e-17 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 79.68 E-value: 8.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 8 FYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAMLPQmHDHQ 87
Cdd:PRK11176 350 TYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQ-NVHL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 88 LDLTVKELIEFGRGphklwrGRLNKED-EEIVDWALSVTNLEGYEYRLLQ-------SLSGGERQRAWIAMTLAQRTNVL 159
Cdd:PRK11176 429 FNDTIANNIAYART------EQYSREQiEEAARMAYAMDFINKMDNGLDTvigengvLLSGGQRQRIAIARALLRDSPIL 502
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 160 LLDEPTTFLDIVHQLEVMELVKRLNEEfgMTIIMVLHDINQAAQySDRLLVLKRGKLQYDGIPEEVLCHE 229
Cdd:PRK11176 503 ILDEATSALDTESERAIQAALDELQKN--RTSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAELLAQN 569
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
19-216 |
1.35e-16 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 79.16 E-value: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 19 NMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAMLPQmhDHQL-DLTVKELIE 97
Cdd:TIGR01192 353 DVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQ--DAGLfNRSIRENIR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 98 FGRGphklwrgrlNKEDEEIVDWALSVT-------NLEGYEYRLLQ---SLSGGERQRAWIAMTLAQRTNVLLLDEPTTF 167
Cdd:TIGR01192 431 LGRE---------GATDEEVYEAAKAAAahdfilkRSNGYDTLVGErgnRLSGGERQRLAIARAILKNAPILVLDEATSA 501
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446549187 168 LDIVHQLEVMELVKRLNEEfgMTIIMVLHDINqAAQYSDRLLVLKRGKL 216
Cdd:TIGR01192 502 LDVETEARVKNAIDALRKN--RTTFIIAHRLS-TVRNADLVLFLDQGRL 547
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-197 |
2.70e-16 |
|
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: 78.05 E-value: 2.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 2 ISVNKVFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLdGKSIHtmksadvakqLAMLP 81
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK----------LAYVD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 82 QMHDHqLDltvkeliefgrGPHKLWrgrlnkedEEIVDwALSVTNLEGYE-----Y------------RLLQSLSGGERQ 144
Cdd:TIGR03719 392 QSRDA-LD-----------PNKTVW--------EEISG-GLDIIKLGKREipsraYvgrfnfkgsdqqKKVGQLSGGERN 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446549187 145 RAWIAMTLAQRTNVLLLDEPTTFLDIvhqlEVMELVKRLNEEFGMTIIMVLHD 197
Cdd:TIGR03719 451 RVHLAKTLKSGGNVLLLDEPTNDLDV----ETLRALEEALLNFAGCAVVISHD 499
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
19-225 |
3.56e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 77.22 E-value: 3.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 19 NMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHtmksaDVAKQLAMLPQ-------MHDHQLdlt 91
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLF-----DAEKGICLPPEkrrigyvFQDARL--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 92 vkelieFgrgPHKLWRGRLN----KEDEEIVDwalSVTNLEGYEY---RLLQSLSGGERQRAWIAMTLAQRTNVLLLDEP 164
Cdd:PRK11144 88 ------F---PHYKVRGNLRygmaKSMVAQFD---KIVALLGIEPlldRYPGSLSGGEKQRVAIGRALLTAPELLLMDEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446549187 165 TTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEV 225
Cdd:PRK11144 156 LASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
19-169 |
4.29e-16 |
|
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: 77.55 E-value: 4.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 19 NMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAMLPQmhDHQL--DlTVKELI 96
Cdd:COG5265 376 GVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQ--DTVLfnD-TIAYNI 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 97 EFgrgphklwrGRLNKEDEEIVDWALS------VTNL-EGYEY----RLLQsLSGGERQRAWIAMTLAQRTNVLLLDEPT 165
Cdd:COG5265 453 AY---------GRPDASEEEVEAAARAaqihdfIESLpDGYDTrvgeRGLK-LSGGEKQRVAIARTLLKNPPILIFDEAT 522
|
....
gi 446549187 166 TFLD 169
Cdd:COG5265 523 SALD 526
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
14-221 |
4.65e-16 |
|
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: 77.56 E-value: 4.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 14 RFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLR-LIARLLKQSEGDIVLDGKSIHTMKSAD-VAKQLAMLPQMHDHQ---L 88
Cdd:TIGR02633 273 RKRVDDVSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPVDIRNPAQaIRAGIAMVPEDRKRHgivP 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 89 DLTVKELIEFGRGPHKLWRGRLNKEDEE-IVDWALSVTNLEGYEYRL-LQSLSGGERQRAWIAMTLAQRTNVLLLDEPTT 166
Cdd:TIGR02633 353 ILGVGKNITLSVLKSFCFKMRIDAAAELqIIGSAIQRLKVKTASPFLpIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446549187 167 FLDIVHQLEVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGI 221
Cdd:TIGR02633 433 GVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLKGDFV 486
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
19-226 |
5.14e-16 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 77.54 E-value: 5.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 19 NMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIV-------LDGKSIHTMKSADVAKQLAMLpqmhdHQldlt 91
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewVDMTKPGPDGRGRAKRYIGIL-----HQ---- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 92 vkeliEFGRGPHKLWRGRLNKE------DEEIVDWALSVTNLEGYEY--------RLLQSLSGGERQRAWIAMTLAQRTN 157
Cdd:TIGR03269 373 -----EYDLYPHRTVLDNLTEAiglelpDELARMKAVITLKMVGFDEekaeeildKYPDELSEGERHRVALAQVLIKEPR 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446549187 158 VLLLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVL 226
Cdd:TIGR03269 448 IVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
18-216 |
5.26e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 77.58 E-value: 5.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 18 QNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQsEGDIVLDGKSIHTMKSADVAKQLAMLPQmHDHQLDLTVKELIE 97
Cdd:PRK11174 367 GPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIELRELDPESWRKHLSWVGQ-NPQLPHGTLRDNVL 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 98 FGRGphklwrgrlNKEDEEIvDWALSVTNLEGYEYRLLQ-----------SLSGGERQRAWIAMTLAQRTNVLLLDEPTT 166
Cdd:PRK11174 445 LGNP---------DASDEQL-QQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTA 514
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446549187 167 FLDIVHQLEVMELVKRLNEefGMTIIMVLHDINQAAQYsDRLLVLKRGKL 216
Cdd:PRK11174 515 SLDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQW-DQIWVMQDGQI 561
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-216 |
5.97e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 77.20 E-value: 5.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 17 MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTM---KSADVAKQLAMLPQMHDHQLD--LT 91
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLspgKLQALRRDIQFIFQDPYASLDprQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 92 VKELIEFGRGPHKLWRGrlnKEDEEIVDWALSVTNLE-GYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDI 170
Cdd:PRK10261 420 VGDSIMEPLRVHGLLPG---KAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446549187 171 VHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKL 216
Cdd:PRK10261 497 SIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
19-216 |
6.08e-16 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 77.31 E-value: 6.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 19 NMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAMLPQmhdhqldltvkELIEF 98
Cdd:PRK13657 353 DVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQ-----------DAGLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 99 GRGPHKLWR-GRLNKEDEEIVDWA-------LSVTNLEGYEYRLLQ---SLSGGERQRAWIAMTLAQRTNVLLLDEPTTF 167
Cdd:PRK13657 422 NRSIEDNIRvGRPDATDEEMRAAAeraqahdFIERKPDGYDTVVGErgrQLSGGERQRLAIARALLKDPPILILDEATSA 501
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446549187 168 LDIVHQLEVMELVKRLNEefGMTIIMVLHDINQAAQySDRLLVLKRGKL 216
Cdd:PRK13657 502 LDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRN-ADRILVFDNGRV 547
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
9-217 |
6.43e-16 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 77.75 E-value: 6.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 9 YAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSaDVAKQLAMLPQMHDHQL 88
Cdd:TIGR01257 1947 YSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNIS-DVHQNMGYCPQFDAIDD 2025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 89 DLTVKE-LIEFGRgphklWRGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTF 167
Cdd:TIGR01257 2026 LLTGREhLYLYAR-----LRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTG 2100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446549187 168 LDIVHQLEVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKLQ 217
Cdd:TIGR01257 2101 MDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQ 2149
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
5-217 |
9.91e-16 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 76.55 E-value: 9.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 5 NKVFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQL-AMLPQM 83
Cdd:PRK10522 327 NVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFsAVFTDF 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 84 H--DHQLD----LTVKELIEfgrgphkLWRGRLNKEDE-EIVDWALSVTNlegyeyrllqsLSGGERQRAWIAMTLAQRT 156
Cdd:PRK10522 407 HlfDQLLGpegkPANPALVE-------KWLERLKMAHKlELEDGRISNLK-----------LSKGQKKRLALLLALAEER 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446549187 157 NVLLLDE------PtTFLDIVHQlevmELVKRLNEEfGMTIIMVLHDiNQAAQYSDRLLVLKRGKLQ 217
Cdd:PRK10522 469 DILLLDEwaadqdP-HFRREFYQ----VLLPLLQEM-GKTIFAISHD-DHYFIHADRLLEMRNGQLS 528
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
13-175 |
1.58e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 72.91 E-value: 1.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 13 ERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKsADVAKQLAMLpqmhDHQL---- 88
Cdd:PRK13538 13 ERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQR-DEYHQDLLYL----GHQPgikt 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 89 DLTVKEliefgrgpHKLWRGRLNKE-DEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTF 167
Cdd:PRK13538 88 ELTALE--------NLRFYQRLHGPgDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTA 159
|
170
....*....|
gi 446549187 168 LDI--VHQLE 175
Cdd:PRK13538 160 IDKqgVARLE 169
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
32-224 |
2.73e-15 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 75.36 E-value: 2.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 32 LIGPNGSGKSTLLRLIARLLKQSEGDIVLdgksihtMKSADVAkqlaMLPQmhDHQLD--LTVKELIEFGRGPHKLWRGR 109
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVDKDFNGEARP-------QPGIKVG----YLPQ--EPQLDptKTVRENVEEGVAEIKDALDR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 110 LNK--------------------EDEEIVD----WALSvTNLE--GYEYRL------LQSLSGGERQRAWIAMTLAQRTN 157
Cdd:TIGR03719 103 FNEisakyaepdadfdklaaeqaELQEIIDaadaWDLD-SQLEiaMDALRCppwdadVTKLSGGERRRVALCRLLLSKPD 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 158 VLLLDEPTTFLDIvhqlEVMELVKRLNEEFGMTIIMVLHD---INQAAQYsdrLLVLKRGKlqydGIPEE 224
Cdd:TIGR03719 182 MLLLDEPTNHLDA----ESVAWLERHLQEYPGTVVAVTHDryfLDNVAGW---ILELDRGR----GIPWE 240
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
24-225 |
3.67e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 74.01 E-value: 3.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 24 IKAGEVVSLIGPNGSGKS----TLLRLIARLLKQSEGDIVLDGKSIHTMKSAD----VAKQLAMLPQ--MHDHQLDLTV- 92
Cdd:PRK11022 30 VKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKErrnlVGAEVAMIFQdpMTSLNPCYTVg 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 93 ---KELIEFGRGPHKLWRGRLNKEDEEIVDWALSVTNLEGYEYRllqsLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLD 169
Cdd:PRK11022 110 fqiMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQ----LSGGMSQRVMIAMAIACRPKLLIADEPTTALD 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446549187 170 IVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEV 225
Cdd:PRK11022 186 VTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
17-216 |
4.51e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 74.56 E-value: 4.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 17 MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSAD-----VA---KQLAMLPQMhdhql 88
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAalaagVAiiyQELHLVPEM----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 89 dlTVKELIEFGRGPHKLwrGRLNKedEEIVDWALSvtNLEGYEYRL-----LQSLSGGERQRAWIAMTLAQRTNVLLLDE 163
Cdd:PRK11288 95 --TVAENLYLGQLPHKG--GIVNR--RLLNYEARE--QLEHLGVDIdpdtpLKYLSIGQRQMVEIAKALARNARVIAFDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446549187 164 PTTFLDIVHQLEVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKL 216
Cdd:PRK11288 167 PTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
19-226 |
8.50e-15 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 73.02 E-value: 8.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 19 NMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQS---EGD-IVLDGKSIHTMKSAD----VAKQLAMLPQMHDHQLDL 90
Cdd:COG4170 25 RVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvTADrFRWNGIDLLKLSPRErrkiIGREIAMIFQEPSSCLDP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 91 TVK------ELIEFGRGPHKLWRgRLNKEDEEIVDWALSV------TNLEGYEYRLlqslSGGERQRAWIAMTLAQRTNV 158
Cdd:COG4170 105 SAKigdqliEAIPSWTFKGKWWQ-RFKWRKKRAIELLHRVgikdhkDIMNSYPHEL----TEGECQKVMIAMAIANQPRL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446549187 159 LLLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVL 226
Cdd:COG4170 180 LIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQIL 247
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
32-224 |
9.31e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 73.61 E-value: 9.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 32 LIGPNGSGKSTLLRLIARLLKQSEGDIVL-DGKSIhtmksadvakqlAMLPQmhDHQLD--LTVKELIEFGRGPHKLWRG 108
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGEARPaPGIKV------------GYLPQ--EPQLDpeKTVRENVEEGVAEVKAALD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 109 RLNK--------------------EDEEIVDwALSVTNLegyEYRLLQ---------------SLSGGERQRAWIAMTLA 153
Cdd:PRK11819 104 RFNEiyaayaepdadfdalaaeqgELQEIID-AADAWDL---DSQLEIamdalrcppwdakvtKLSGGERRRVALCRLLL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446549187 154 QRTNVLLLDEPTTFLDI--VHQLEvmelvkRLNEEFGMTIIMVLHD---INQAAQYsdrLLVLKRGKlqydGIPEE 224
Cdd:PRK11819 180 EKPDMLLLDEPTNHLDAesVAWLE------QFLHDYPGTVVAVTHDryfLDNVAGW---ILELDRGR----GIPWE 242
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-170 |
9.76e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 73.61 E-value: 9.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 2 ISVNKVFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLdGKSIhtmksadvakQLAMLP 81
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV----------KLAYVD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 82 QMHDHqLDltvkeliefgrgPHK-LWrgrlnkedEEIVDwALSVTNLEGYE-----Y------------RLLQSLSGGER 143
Cdd:PRK11819 394 QSRDA-LD------------PNKtVW--------EEISG-GLDIIKVGNREipsraYvgrfnfkggdqqKKVGVLSGGER 451
|
170 180
....*....|....*....|....*..
gi 446549187 144 QRAWIAMTLAQRTNVLLLDEPTTFLDI 170
Cdd:PRK11819 452 NRLHLAKTLKQGGNVLLLDEPTNDLDV 478
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
24-216 |
1.07e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 73.41 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 24 IKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAML-PQmhDHQLD-----LTVKELIE 97
Cdd:PRK11288 276 VRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMLcPE--DRKAEgiipvHSVADNIN 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 98 FGRGPHKLWRGRL---NKE----DEEIVDWALSVTNLEgyeyRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDI 170
Cdd:PRK11288 354 ISARRHHLRAGCLinnRWEaenaDRFIRSLNIKTPSRE----QLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDV 429
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446549187 171 VHQLEVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKL 216
Cdd:PRK11288 430 GAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
17-225 |
1.23e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 73.28 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 17 MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQ-LAMLPQMHDHQLDLTVKEL 95
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGIIYQELSVIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 96 IEFGRGPHKLWRGrlnkedEEIVDWA---------LSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTT 166
Cdd:PRK09700 101 LYIGRHLTKKVCG------VNIIDWRemrvraammLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTS 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446549187 167 FLDivhQLEVMEL---VKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEV 225
Cdd:PRK09700 175 SLT---NKEVDYLfliMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-229 |
2.85e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 72.70 E-value: 2.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 17 MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAMLPQMhdhqlDLTVKELI 96
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQS-----PVLFSGTV 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 97 EFGRGPHK------LWRGRLNKEDEEIVD---WALSVTNLEGYEyrllqSLSGGERQRAWIAMTLAQRTNVLLLDEPTTF 167
Cdd:PLN03232 1327 RFNIDPFSehndadLWEALERAHIKDVIDrnpFGLDAEVSEGGE-----NFSVGQRQLLSLARALLRRSKILVLDEATAS 1401
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446549187 168 LDIvhqlEVMELVKR-LNEEF-GMTIIMVLHDINQAAQySDRLLVLKRGK-LQYDGiPEEVLCHE 229
Cdd:PLN03232 1402 VDV----RTDSLIQRtIREEFkSCTMLVIAHRLNTIID-CDKILVLSSGQvLEYDS-PQELLSRD 1460
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
11-226 |
3.21e-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: 3.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 11 HSERFQ-MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQS----EGDIVLDGKSIHTMK---SADVakqlAMLPQ 82
Cdd:TIGR00956 70 DTKTFDiLKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFhigvEGVITYDGITPEEIKkhyRGDV----VYNAE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 83 MHDHQLDLTVKELIEFG---RGPHKLWRGrLNKED--EEIVDWALSVTNLE-------GYEyrLLQSLSGGERQRAWIAM 150
Cdd:TIGR00956 146 TDVHFPHLTVGETLDFAarcKTPQNRPDG-VSREEyaKHIADVYMATYGLShtrntkvGND--FVRGVSGGERKRVSIAE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 151 TLAQRTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHdinQAAQ--YS--DRLLVLKRGKLQYDGIPEEVL 226
Cdd:TIGR00956 223 ASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIY---QCSQdaYElfDKVIVLYEGYQIYFGPADKAK 299
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
21-214 |
4.38e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 71.76 E-value: 4.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 21 NVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVL-DGKSIhtmksadvakqlAMLPQ---MhdhqLDLTVKELI 96
Cdd:COG4178 383 SLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARV------------LFLPQrpyL----PLGTLREAL 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 97 EFGRGPHKLwrgrlnkEDEEIVDwALSVTNLEGYEYRL------LQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDI 170
Cdd:COG4178 447 LYPATAEAF-------SDAELRE-ALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDE 518
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446549187 171 VHQLEVMELVKRlnEEFGMTIIMVLHDiNQAAQYSDRLLVLKRG 214
Cdd:COG4178 519 ENEAALYQLLRE--ELPGTTVISVGHR-STLAAFHDRVLELTGD 559
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
19-236 |
1.50e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 70.08 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 19 NMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSAD-VAKQLAMLP---QMH----DHQLDL 90
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPedrQSSglylDAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 91 TVKELIeFGRGPHKLWRGRLNKEdeeivdwalsvtnLEGYeYRLL-----------QSLSGGERQRAWIAMTLAQRTNVL 159
Cdd:PRK15439 361 NVCALT-HNRRGFWIKPARENAV-------------LERY-RRALnikfnhaeqaaRTLSGGNQQKVLIAKCLEASPQLL 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446549187 160 LLDEPTTFLDIVHQLEVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVLCHEMFQHVFG 236
Cdd:PRK15439 426 IVDEPTRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAINVDTIMRLAFG 501
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-216 |
1.89e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 69.98 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 1 MISVNKVFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGK----------------S 64
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDlivarlqqdpprnvegT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 65 IHTMKSADVAKQLAMLPQMHD--HQL--DLTVKELIEFGRGPHKLWRGRLNKEDEEIVDwALSVTNLEGYEyrLLQSLSG 140
Cdd:PRK11147 83 VYDFVAEGIEEQAEYLKRYHDisHLVetDPSEKNLNELAKLQEQLDHHNLWQLENRINE-VLAQLGLDPDA--ALSSLSG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446549187 141 GERQRAWIAMTLAQRTNVLLLDEPTTFLDIvhqlEVMELVKRLNEEFGMTIIMVLHD---INQAAQysdRLLVLKRGKL 216
Cdd:PRK11147 160 GWLRKAALGRALVSNPDVLLLDEPTNHLDI----ETIEWLEGFLKTFQGSIIFISHDrsfIRNMAT---RIVDLDRGKL 231
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
9-236 |
2.16e-13 |
|
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: 69.94 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 9 YAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLkQSEGDIVLDGKSIHTMKSADVAKQLAMLPQmhdhql 88
Cdd:TIGR01271 1227 YTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWNSVTLQTWRKAFGVIPQ------ 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 89 dltvKELIEFGR-----GPHKLWrgrlnkEDEEIVDWALSV---TNLEGY----EYRLLQS---LSGGERQRAWIAMTLA 153
Cdd:TIGR01271 1300 ----KVFIFSGTfrknlDPYEQW------SDEEIWKVAEEVglkSVIEQFpdklDFVLVDGgyvLSNGHKQLMCLARSIL 1369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 154 QRTNVLLLDEPTTFLD-IVHQLevmeLVKRLNEEFG-MTIIMVLHDInQAAQYSDRLLVLKRGKL-QYDGIPEEVLCHEM 230
Cdd:TIGR01271 1370 SKAKILLLDEPSAHLDpVTLQI----IRKTLKQSFSnCTVILSEHRV-EALLECQQFLVIEGSSVkQYDSIQKLLNETSL 1444
|
....*.
gi 446549187 231 FQHVFG 236
Cdd:TIGR01271 1445 FKQAMS 1450
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
2-214 |
2.30e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 69.74 E-value: 2.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 2 ISVNKVFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAMLP 81
Cdd:PRK10789 316 VNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVS 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 82 QMHDHQLDlTVKELIEFGRgPhklwrgrlNKEDEEIvDWALSVTNL--------EGYEYRLLQS---LSGGERQRAWIAM 150
Cdd:PRK10789 396 QTPFLFSD-TVANNIALGR-P--------DATQQEI-EHVARLASVhddilrlpQGYDTEVGERgvmLSGGQKQRISIAR 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446549187 151 TLAQRTNVLLLDEPTTFLDIVHQLEVMELVKRLNEefGMTIIMVLHDINqAAQYSDRLLVLKRG 214
Cdd:PRK10789 465 ALLLNAEILILDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLS-ALTEASEILVMQHG 525
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
19-215 |
2.69e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.19 E-value: 2.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 19 NMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQS--EGDIVLDG-----KSIHTMKSADVA---KQLAMLPQMhdhql 88
Cdd:PRK13549 23 NVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGeelqaSNIRDTERAGIAiihQELALVKEL----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 89 dlTVKELIEFGRGPHKlwRGRLN-----KEDEEI-------VDWALSVTNlegyeyrllqsLSGGERQRAWIAMTLAQRT 156
Cdd:PRK13549 98 --SVLENIFLGNEITP--GGIMDydamyLRAQKLlaqlkldINPATPVGN-----------LGLGQQQLVEIAKALNKQA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446549187 157 NVLLLDEPT---------TFLDIVHQLevmelvkrlnEEFGMTIIMVLHDINQAAQYSDRLLVLKRGK 215
Cdd:PRK13549 163 RLLILDEPTasltesetaVLLDIIRDL----------KAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
18-196 |
4.59e-13 |
|
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: 65.64 E-value: 4.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 18 QNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSihtmksadvakQLAMLPQmHDHQLDLTVKELIe 97
Cdd:cd03223 18 KDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE-----------DLLFLPQ-RPYLPLGTLREQL- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 98 fgrgphklwrgrlnkedeeIVDWAlsvtnlegyeyrllQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVHQLEVM 177
Cdd:cd03223 85 -------------------IYPWD--------------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLY 131
|
170
....*....|....*....
gi 446549187 178 ELVKrlneEFGMTIIMVLH 196
Cdd:cd03223 132 QLLK----ELGITVISVGH 146
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
19-223 |
8.53e-13 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 66.24 E-value: 8.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 19 NMNVHIKAGEVVSLIGPNGSGKSTLLRLIA--RLLKQSEGDIVLDGKSIHTMKSADVAKQ---LAM-----LPQMhdhql 88
Cdd:COG0396 18 GVNLTIKPGEVHAIMGPNGSGKSTLAKVLMghPKYEVTSGSILLDGEDILELSPDERARAgifLAFqypveIPGV----- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 89 dlTVKELIefgrgphklwRGRLNKEDEEIVDWALSVTNLEGYEYRL------LQ-----SLSGGERQRAWIAMTLAQRTN 157
Cdd:COG0396 93 --SVSNFL----------RTALNARRGEELSAREFLKLLKEKMKELgldedfLDryvneGFSGGEKKRNEILQMLLLEPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446549187 158 VLLLDEPTTFLDI----VhqleVMELVKRLNEEfGMTIIMVLH-----DINQAaqysDRLLVLKRGKLQYDGIPE 223
Cdd:COG0396 161 LAILDETDSGLDIdalrI----VAEGVNKLRSP-DRGILIITHyqrilDYIKP----DFVHVLVDGRIVKSGGKE 226
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-232 |
1.10e-12 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 67.44 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 2 ISVNKVFYA-HSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAML 80
Cdd:PRK10790 341 IDIDNVSFAyRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 81 PQ----MHDhqldlTVKELIEFGR--GPHKLWRGRlnkedeEIVDWALSVTNL-EGYEYRLLQ---SLSGGERQRAWIAM 150
Cdd:PRK10790 421 QQdpvvLAD-----TFLANVTLGRdiSEEQVWQAL------ETVQLAELARSLpDGLYTPLGEqgnNLSVGQKQLLALAR 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 151 TLAQRTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEfgMTIIMVLHDINQAAQySDRLLVLKRGKLQYDGIPEEVLC--- 227
Cdd:PRK10790 490 VLVQTPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLLAaqg 566
|
....*..
gi 446549187 228 --HEMFQ 232
Cdd:PRK10790 567 ryWQMYQ 573
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
19-226 |
1.29e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 67.46 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 19 NMNVHIKAGEVVSLIGPNGSGKSTLLRLIA--RLLKQseGDI-VLDGKsihtMKSA----DVAKQLAMLPQMHDHQL--D 89
Cdd:NF033858 19 DVSLDIPAGCMVGLIGPDGVGKSSLLSLIAgaRKIQQ--GRVeVLGGD----MADArhrrAVCPRIAYMPQGLGKNLypT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 90 LTVKELIEFgrgphklwRGRL----NKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPT 165
Cdd:NF033858 93 LSVFENLDF--------FGRLfgqdAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446549187 166 TFLDIVHQLEVMELVKRLNEEF-GMTIIMVLHDINQAAQYsDRLLVLKRGKLQYDGIPEEVL 226
Cdd:NF033858 165 TGVDPLSRRQFWELIDRIRAERpGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELL 225
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
13-220 |
1.30e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 67.60 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 13 ERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQS--EGDIVLDGKSI--HTMKSADVAKQLAMLpqmHDHql 88
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPtkQILKRTGFVTQDDIL---YPH-- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 89 dLTVKELIEFG---RGPHKLWRGRLNKEDEEIVDwALSVTNLEG--YEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDE 163
Cdd:PLN03211 155 -LTVRETLVFCsllRLPKSLTKQEKILVAESVIS-ELGLTKCENtiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDE 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446549187 164 PTTFLDIVHQLEVMELVKRLNEEfGMTIIMVLHD-INQAAQYSDRLLVLKRGKLQYDG 220
Cdd:PLN03211 233 PTSGLDATAAYRLVLTLGSLAQK-GKTIVTSMHQpSSRVYQMFDSVLVLSEGRCLFFG 289
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
19-224 |
1.45e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 67.26 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 19 NMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLK-QSEGDIVLDGKSIHTMKSAD-VAKQLAMLPQMHDHQ---LDLTVK 93
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQaIAQGIAMVPEDRKRDgivPVMGVG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 94 ELI------EFGRGphklwrGRLNKEDEE-IVDWALSVTNLEGYEYRL-LQSLSGGERQRAWIAMTLAQRTNVLLLDEPT 165
Cdd:PRK13549 360 KNItlaaldRFTGG------SRIDDAAELkTILESIQRLKVKTASPELaIARLSGGNQQKAVLAKCLLLNPKILILDEPT 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446549187 166 TFLDIVHQLEVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEE 224
Cdd:PRK13549 434 RGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKLKGDLINHN 491
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-223 |
1.56e-12 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 67.13 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 2 ISVNKVFYAH-----SERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIhTMKSADVAKQ 76
Cdd:COG4615 328 LELRGVTYRYpgedgDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV-TADNREAYRQ 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 77 L-----------AMLPQMHDHQLDLTVKELIEfgrgphklwrgRLNKEDE-EIVDWALSVTNlegyeyrllqsLSGGERQ 144
Cdd:COG4615 407 LfsavfsdfhlfDRLLGLDGEADPARARELLE-----------RLELDHKvSVEDGRFSTTD-----------LSQGQRK 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 145 R-AWIAMTLAQRtNVLLLDE------PtTFLDIVHQLEVMELvKRLneefGMTIIMVLHDinqaAQY---SDRLLVLKRG 214
Cdd:COG4615 465 RlALLVALLEDR-PILVFDEwaadqdP-EFRRVFYTELLPEL-KAR----GKTVIAISHD----DRYfdlADRVLKMDYG 533
|
....*....
gi 446549187 215 KLQYDGIPE 223
Cdd:COG4615 534 KLVELTGPA 542
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
18-225 |
3.84e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 65.82 E-value: 3.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 18 QNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQ-LAMLPQmhDHQ-----LDLT 91
Cdd:COG3845 275 KDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYIPE--DRLgrglvPDMS 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 92 VKE--LIEFGRGPHKLWRGRLNKedEEIVDWALSVtnLEGYEYR------LLQSLSGGERQRAWIAMTLAQRTNVLLLDE 163
Cdd:COG3845 353 VAEnlILGRYRRPPFSRGGFLDR--KAIRAFAEEL--IEEFDVRtpgpdtPARSLSGGNQQKVILARELSRDPKLLIAAQ 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446549187 164 PTTFLDI-----VHQlevmELVKRLNEefGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEV 225
Cdd:COG3845 429 PTRGLDVgaiefIHQ----RLLELRDA--GAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
17-236 |
6.33e-12 |
|
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: 63.82 E-value: 6.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 17 MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIA--RLLKQSEGDIVLDGKSIHTMKSADVAKQ-LAMLPQMHDHQLDLTVK 93
Cdd:TIGR01978 16 LKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAghPSYEVTSGTILFKGQDLLELEPDERARAgLFLAFQYPEEIPGVSNL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 94 ELIefgRGPHKLWRGRLNKEDEEIVDWA-LSVTNLEGYEY------RLL-QSLSGGERQRAWIAMTLAQRTNVLLLDEPT 165
Cdd:TIGR01978 96 EFL---RSALNARRSARGEEPLDLLDFEkLLKEKLALLDMdeeflnRSVnEGFSGGEKKRNEILQMALLEPKLAILDEID 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446549187 166 TFLDIVHQLEVMELVKRLNEEfGMTIIMVLHDiNQAAQY--SDRLLVLKRGKLQYDGIPEevLCHEMFQHVFG 236
Cdd:TIGR01978 173 SGLDIDALKIVAEGINRLREP-DRSFLIITHY-QRLLNYikPDYVHVLLDGRIVKSGDVE--LAKELEAKGYD 241
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
15-215 |
6.81e-12 |
|
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: 62.87 E-value: 6.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 15 FQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLdGKSIhtmksADVAkQLAMLPQMhdhqldlTVKE 94
Cdd:cd03250 19 FTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV-PGSI-----AYVS-QEPWIQNG-------TIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 95 LIEFGRgphklwrgrlnKEDEEIVDWALSVTNLEgyeyRLLQ---------------SLSGGERQRAWIAMTLAQRTNVL 159
Cdd:cd03250 85 NILFGK-----------PFDEERYEKVIKACALE----PDLEilpdgdlteigekgiNLSGGQKQRISLARAVYSDADIY 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446549187 160 LLDEPTTFLD------IVHQLevmeLVKRLNEefGMTIIMVLHDInQAAQYSDRLLVLKRGK 215
Cdd:cd03250 150 LLDDPLSAVDahvgrhIFENC----ILGLLLN--NKTRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
18-216 |
8.49e-12 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 64.88 E-value: 8.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 18 QNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIvldgksihtMKSADVakQLAMLPQMHDHQLDLTVKELIE 97
Cdd:PLN03073 526 KNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV---------FRSAKV--RMAVFSQHHVDGLDLSSNPLLY 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 98 FGR----GPHKLWRGRLNkedeeivdwALSVT-NLegyEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDivh 172
Cdd:PLN03073 595 MMRcfpgVPEQKLRAHLG---------SFGVTgNL---ALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD--- 659
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446549187 173 qLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKL 216
Cdd:PLN03073 660 -LDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
17-225 |
8.67e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 64.82 E-value: 8.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 17 MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIaRLLKQSEGDivlDGKSIH--------------------------TMKS 70
Cdd:TIGR03269 16 LKNISFTIEEGEVLGILGRSGAGKSVLMHVL-RGMDQYEPT---SGRIIYhvalcekcgyverpskvgepcpvcggTLEP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 71 -------------ADVAKQLAMLPQM------HDHQLDLTVKELIEFGRgphklwrgrlnkEDEEIVDWALSVTNLEGYE 131
Cdd:TIGR03269 92 eevdfwnlsdklrRRIRKRIAIMLQRtfalygDDTVLDNVLEALEEIGY------------EGKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 132 YRLL---QSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLD-----IVHQLeVMELVKrlneEFGMTIIMVLHDINQAAQ 203
Cdd:TIGR03269 160 HRIThiaRDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDpqtakLVHNA-LEEAVK----ASGISMVLTSHWPEVIED 234
|
250 260
....*....|....*....|..
gi 446549187 204 YSDRLLVLKRGKLQYDGIPEEV 225
Cdd:TIGR03269 235 LSDKAIWLENGEIKEEGTPDEV 256
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
17-215 |
1.06e-11 |
|
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: 64.46 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 17 MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQS--EGDIVLDGKSIHTMKSADV-AKQLAMLPQMHDHQLDLTVK 93
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVPELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 94 ELIEFG-----RGPHKLWRGRLNKEDEEIVDWALSVTNLEgyeyRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFL 168
Cdd:TIGR02633 97 ENIFLGneitlPGGRMAYNAMYLRAKNLLRELQLDADNVT----RPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446549187 169 DIVHQLEVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGK 215
Cdd:TIGR02633 173 TEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
26-220 |
1.11e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 64.30 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 26 AGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADvAKQLA--MLPQMHDHQLDLTVKELIEFGrgph 103
Cdd:PRK15439 36 AGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAK-AHQLGiyLVPQEPLLFPNLSVKENILFG---- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 104 kLWRGRLNKEDEEIVDWALSVT-NLEGyeyrLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVhqlEVMELVKR 182
Cdd:PRK15439 111 -LPKRQASMQKMKQLLAALGCQlDLDS----SAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPA---ETERLFSR 182
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446549187 183 LNE--EFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDG 220
Cdd:PRK15439 183 IREllAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSG 222
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-215 |
1.52e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.87 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 20 MNVHikAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIH--TMKSADVA------KQLAMLPQmhdhqldLT 91
Cdd:PRK10762 25 LNVY--PGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfnGPKSSQEAgigiihQELNLIPQ-------LT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 92 VKELIEFGRGPHKLWrGRLN-KEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTtflDI 170
Cdd:PRK10762 96 IAENIFLGREFVNRF-GRIDwKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPT---DA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446549187 171 VHQLEVMELVKRLNE--EFGMTIIMVLHDINQAAQYSDRLLVLKRGK 215
Cdd:PRK10762 172 LTDTETESLFRVIRElkSQGRGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
17-230 |
1.81e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 62.88 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 17 MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAMLPQMHDHQLD--LTVKE 94
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPSTSLNprQRISQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 95 LIEFgrgPHKLWRGRLNKEDEEIVDWAL-SVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVHQ 173
Cdd:PRK15112 109 ILDF---PLRLNTDLEPEQREKQIIETLrQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMR 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 174 LEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVLC---HEM 230
Cdd:PRK15112 186 SQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLAsplHEL 245
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
138-226 |
1.87e-11 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 63.28 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 138 LSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQ 217
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
....*....
gi 446549187 218 YDGIPEEVL 226
Cdd:PRK15093 239 ETAPSKELV 247
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
17-221 |
2.14e-11 |
|
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: 62.56 E-value: 2.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 17 MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLkQSEGDIVLDGKSIHTMKSADVAKQLAMLPQmhdhqldltvKELI 96
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGDIQIDGVSWNSVPLQKWRKAFGVIPQ----------KVFI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 97 EFGR-----GPHKLWRgrlnkeDEEIVDWALSV---TNLEGY----EYRLLQS---LSGGERQRAWIAMTLAQRTNVLLL 161
Cdd:cd03289 89 FSGTfrknlDPYGKWS------DEEIWKVAEEVglkSVIEQFpgqlDFVLVDGgcvLSHGHKQLMCLARSVLSKAKILLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446549187 162 DEPTTFLD-IVHQLevmeLVKRLNEEF-GMTIIMVLHDInQAAQYSDRLLVLKRGKL-QYDGI 221
Cdd:cd03289 163 DEPSAHLDpITYQV----IRKTLKQAFaDCTVILSEHRI-EAMLECQRFLVIEENKVrQYDSI 220
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
17-214 |
2.14e-11 |
|
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: 61.96 E-value: 2.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 17 MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADvAKQLAMLPQMHDHQ----LDLTV 92
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEA-TRSRNRYSVAYAAQkpwlLNATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 93 KELIEFGrgphklwrGRLNKEDEEIVDWALSVT-NLE----GYEYRLLQ---SLSGGERQRAWIAMTLAQRTNVLLLDEP 164
Cdd:cd03290 96 EENITFG--------SPFNKQRYKAVTDACSLQpDIDllpfGDQTEIGErgiNLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446549187 165 TTFLDIVHQLEVME--LVKRLNEEfGMTIIMVLHDInQAAQYSDRLLVLKRG 214
Cdd:cd03290 168 FSALDIHLSDHLMQegILKFLQDD-KRTLVLVTHKL-QYLPHADWIIAMKDG 217
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
20-229 |
2.82e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 63.60 E-value: 2.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 20 MNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAMLPQMhdhqlDLTVKELIEFG 99
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQA-----PVLFSGTVRFN 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 100 RGP---HK---LW----RGRLnKEDEEIVDWALSVTNLEGYEyrllqSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLD 169
Cdd:PLN03130 1333 LDPfneHNdadLWesleRAHL-KDVIRRNSLGLDAEVSEAGE-----NFSVGQRQLLSLARALLRRSKILVLDEATAAVD 1406
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446549187 170 IVHQLEVMelvKRLNEEF-GMTIIMVLHDINQAAQySDRLLVLKRGKLQYDGIPEEVLCHE 229
Cdd:PLN03130 1407 VRTDALIQ---KTIREEFkSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLSNE 1463
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
24-214 |
3.38e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.20 E-value: 3.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 24 IKAGEVVSLIGPNGSGKSTLLRLIARLLKQ---SEGDIVLDGKSIhtmkSADVAKQLAMLPQMHDHQLDLTVKELIEFG- 99
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPL----DSSFQRSIGYVQQQDLHLPTSTVRESLRFSa 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 100 --RGPHKLWRgrlnKEDEEIVDWALSVTNLEGYEYRLL----QSLSGGERQRAWIAMTLAQRTNVLL-LDEPTTFLDIVH 172
Cdd:TIGR00956 862 ylRQPKSVSK----SEKMEYVEEVIKLLEMESYADAVVgvpgEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQT 937
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446549187 173 QLEVMELVKRLNEEfGMTIIMVLH----DINQAAqysDRLLVLKRG 214
Cdd:TIGR00956 938 AWSICKLMRKLADH-GQAILCTIHqpsaILFEEF---DRLLLLQKG 979
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-197 |
1.72e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.12 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 4 VNKVFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGdivldgkSIHTMKSADVA--KQlamlp 81
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSG-------RIHCGTKLEVAyfDQ----- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 82 qmHDHQLDL--TV--------KELIEFGRGPHKLwrgrlnkedeeivdwalsvtnleGYeyrlLQ--------------S 137
Cdd:PRK11147 390 --HRAELDPekTVmdnlaegkQEVMVNGRPRHVL-----------------------GY----LQdflfhpkramtpvkA 440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 138 LSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIvhqlEVMELVKRLNEEFGMTIIMVLHD 197
Cdd:PRK11147 441 LSGGERNRLLLARLFLKPSNLLILDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHD 496
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
15-269 |
1.98e-10 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 60.67 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 15 FQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAMLpqmhdhqldltvkE 94
Cdd:PRK13545 38 YALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTGI-------------E 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 95 LIEFgRGphkLWRGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPttfLDIVHQL 174
Cdd:PRK13545 105 NIEL-KG---LMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEA---LSVGDQT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 175 EVMELVKRLNE--EFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVLCH----------------EMFQ--HV 234
Cdd:PRK13545 178 FTKKCLDKMNEfkEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHydeflkkynqmsveerKDFReeQI 257
|
250 260 270
....*....|....*....|....*....|....*
gi 446549187 235 FGIEVDIFQGSDKPFFTPKRISKKGGAKCEQKNVL 269
Cdd:PRK13545 258 SQFQHGLLQEDQTGRERKRKKGKKTSRKFKKKRVL 292
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-169 |
3.33e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.42 E-value: 3.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 1 MISVNKVFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSAdVAKQLAML 80
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCT-YQKQLCFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 81 PQMHDHQLDLTVKELIEFgrgphKLWRGRLNKEDEEIVdwalSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLL 160
Cdd:PRK13540 80 GHRSGINPYLTLRENCLY-----DIHFSPGAVGITELC----RLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWL 150
|
....*....
gi 446549187 161 LDEPTTFLD 169
Cdd:PRK13540 151 LDEPLVALD 159
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
5-235 |
4.85e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 58.67 E-value: 4.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 5 NKVFYAhserfqMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQlamlpqmh 84
Cdd:PRK13546 34 NKTFFA------LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGLSGQ-------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 85 dhqldLTVKELIEFgrgpHKLWRGRLNKEDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEP 164
Cdd:PRK13546 100 -----LTGIENIEF----KMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446549187 165 TTFLDIVHQLEVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKLQYDGIPEEVLCH-EMFQHVF 235
Cdd:PRK13546 171 LSVGDQTFAQKCLDKIYEFKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKyEAFLNDF 241
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-215 |
8.56e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.59 E-value: 8.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 17 MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSI--HTMKSAdVAKQLAMLPQMHDHQLDLTVKE 94
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfKSSKEA-LENGISMVHQELNLVLQRSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 95 LIEFGRGPHKLW---RGRLNKEDEEIVDwALSVtNLEGYEYrlLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDiv 171
Cdd:PRK10982 93 NMWLGRYPTKGMfvdQDKMYRDTKAIFD-ELDI-DIDPRAK--VATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLT-- 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446549187 172 hQLEVMELVKRLNE--EFGMTIIMVLHDINQAAQYSDRLLVLKRGK 215
Cdd:PRK10982 167 -EKEVNHLFTIIRKlkERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-220 |
8.57e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 59.03 E-value: 8.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 1 MISVNKVFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLdGKSIhtmksadvakQLAML 80
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGI----------KLGYF 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 81 PQmhdHQLdltvkELIEFGRGP-HKLWRGRLNKEDEEIVDWalsvtnLEGYEYR------LLQSLSGGERQRAWIAMTLA 153
Cdd:PRK10636 381 AQ---HQL-----EFLRADESPlQHLARLAPQELEQKLRDY------LGGFGFQgdkvteETRRFSGGEKARLVLALIVW 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446549187 154 QRTNVLLLDEPTTFLDivhqlevMELVKRLNE---EFGMTIIMVLHDINQAAQYSDRLLVLKRGKLQ-YDG 220
Cdd:PRK10636 447 QRPNLLLLDEPTNHLD-------LDMRQALTEaliDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEpFDG 510
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
24-225 |
1.39e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 58.64 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 24 IKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAMLPQ---MHDHQLDLTVKELIEfgR 100
Cdd:PTZ00243 1333 IAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQdpvLFDGTVRQNVDPFLE--A 1410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 101 GPHKLW--------RGRLNKEDeeivdwalsvtnlEGYEYRLLQ---SLSGGERQRAWIAMTLAQR-TNVLLLDEPTT-- 166
Cdd:PTZ00243 1411 SSAEVWaalelvglRERVASES-------------EGIDSRVLEggsNYSVGQRQLMCMARALLKKgSGFILMDEATAni 1477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446549187 167 --FLDIVHQLEVMELVKrlneefGMTIIMVLHDINQAAQYsDRLLVLKRGKLQYDGIPEEV 225
Cdd:PTZ00243 1478 dpALDRQIQATVMSAFS------AYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPREL 1531
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
24-215 |
1.42e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 57.67 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 24 IKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKsihtmksaDVAKqlamlpqmHDHQldlTVKEL-----IEF 98
Cdd:PRK11308 38 LERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQ--------DLLK--------ADPE---AQKLLrqkiqIVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 99 gRGPHklwrGRLN--KEDEEIVDWALSV-TNLEGYEYR--LLQSL-----------------SGGERQRAWIAMTLAQRT 156
Cdd:PRK11308 99 -QNPY----GSLNprKKVGQILEEPLLInTSLSAAERRekALAMMakvglrpehydryphmfSGGQRQRIAIARALMLDP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446549187 157 NVLLLDEPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRGK 215
Cdd:PRK11308 174 DVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGR 232
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-214 |
1.77e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 55.07 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 27 GEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDgksihtmksadvakqlamlpqmhdhqldltvkeliefgrgphklw 106
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYI--------------------------------------------- 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 107 rgrlnkeDEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVHQLEVMELV-----K 181
Cdd:smart00382 37 -------DGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrllL 109
|
170 180 190
....*....|....*....|....*....|....*...
gi 446549187 182 RLNEEFGMTIIMVLHDINQ-----AAQYSDRLLVLKRG 214
Cdd:smart00382 110 LLKSEKNLTVILTTNDEKDlgpalLRRRFDRRIVLLLI 147
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
17-209 |
1.92e-09 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 55.41 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 17 MQNMNVHIKAGEVVSLIGPNGSGKSTLlrliarllkqsegdiVLDGKSihtmksADVAKQLAMLPQMHDHQLDLTVKELi 96
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL---------------VNEGLY------ASGKARLISFLPKFSRNKLIFIDQL- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 97 efgrgphklwrgrlnkedEEIVDWALSVTNLEgyeyRLLQSLSGGERQRAWIAMTLAQRT--NVLLLDEPTTFLDIVHQL 174
Cdd:cd03238 69 ------------------QFLIDVGLGYLTLG----QKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDIN 126
|
170 180 190
....*....|....*....|....*....|....*
gi 446549187 175 EVMELVKRLNEEfGMTIIMVLHDInQAAQYSDRLL 209
Cdd:cd03238 127 QLLEVIKGLIDL-GNTVILIEHNL-DVLSSADWII 159
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
7-229 |
3.46e-09 |
|
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: 56.07 E-value: 3.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 7 VFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSI-----HTMKSadvakQLAMLP 81
Cdd:cd03288 27 VRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDIsklplHTLRS-----RLSIIL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 82 QmhDHQLdltVKELIEFGRGPHK------LWrgrlnkEDEEIVDWALSVTNLEGYEYRLL----QSLSGGERQRAWIAMT 151
Cdd:cd03288 102 Q--DPIL---FSGSIRFNLDPECkctddrLW------EALEIAQLKNMVKSLPGGLDAVVteggENFSVGQRQLFCLARA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446549187 152 LAQRTNVLLLDEPTTFLDIVHQLEVMELVkrLNEEFGMTIIMVLHDINQAAQySDRLLVLKRGKLQYDGIPEEVLCHE 229
Cdd:cd03288 171 FVRKSSILIMDEATASIDMATENILQKVV--MTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQE 245
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
18-224 |
3.62e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 55.73 E-value: 3.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 18 QNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAMLPQMHDhqldltVKELI- 96
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGREASLIDAIGRKGDFKD------AVELLn 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 97 EFGRGPHKLWRgRLNKEdeeivdwalsvtnlegyeyrllqsLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVHQLEV 176
Cdd:COG2401 121 AVGLSDAVLWL-RRFKE------------------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRV 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446549187 177 MELVKRLNEEFGMTIIMVLHDINQAAQYSDRLLVLKRgklqYDGIPEE 224
Cdd:COG2401 176 ARNLQKLARRAGITLVVATHHYDVIDDLQPDLLIFVG----YGGVPEE 219
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
18-215 |
3.77e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 56.72 E-value: 3.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 18 QNMNVHIKAGEVVSLIGPNGSGKSTLLRLIarllkqS--------EGDIVLDG-----KSIHTMKSADVA---KQLAMLP 81
Cdd:NF040905 18 DDVNLSVREGEIHALCGENGAGKSTLMKVL------SgvyphgsyEGEILFDGevcrfKDIRDSEALGIViihQELALIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 82 QmhdhqldLTVKELIEFGRGPHKlwRGrlnkedeeIVDWalSVTNLEGYEY-----------RLLQSLSGGERQRAWIAM 150
Cdd:NF040905 92 Y-------LSIAENIFLGNERAK--RG--------VIDW--NETNRRARELlakvgldespdTLVTDIGVGKQQLVEIAK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446549187 151 TLAQRTNVLLLDEPTTFL---DIVHQLevmELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGK 215
Cdd:NF040905 153 ALSKDVKLLILDEPTAALneeDSAALL---DLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
13-216 |
5.02e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 56.33 E-value: 5.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 13 ERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSAD-VAKQLAMLPQMHDHQ---L 88
Cdd:PRK09700 275 DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDaVKKGMAYITESRRDNgffP 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 89 DLTVKELIEFGR----GPHKLWRGRLNKEDEEIV------DWALSVTNLEgyeyRLLQSLSGGERQRAWIAMTLAQRTNV 158
Cdd:PRK09700 355 NFSIAQNMAISRslkdGGYKGAMGLFHEVDEQRTaenqreLLALKCHSVN----QNITELSGGNQQKVLISKWLCCCPEV 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446549187 159 LLLDEPTTFLDIVHQLEVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKL 216
Cdd:PRK09700 431 IIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
17-65 |
2.38e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 53.49 E-value: 2.38e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 446549187 17 MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIA--RLLKQSEGDIVLDGKSI 65
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAghPAYKILEGDILFKGESI 73
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-216 |
3.04e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.97 E-value: 3.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 17 MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQ-LAMLPQMHDH-----QLDL 90
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHgFALVTEERRStgiyaYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 91 TVKELIEFGRGPHKLWRGRLNKEDEEIVDWALSVTNLEGYEYR-LLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLD 169
Cdd:PRK10982 344 GFNSLISNIRNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRtQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGID 423
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446549187 170 IVHQLEVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLKRGKL 216
Cdd:PRK10982 424 VGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
25-214 |
7.52e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 53.31 E-value: 7.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 25 KAGEVVSLIGPNGSGKSTLLRLIA--RLLKQSEGDIVLDGksiHTMKSADVAKQLAMLPQMHDHQLDLTVKE-LI--EFG 99
Cdd:PLN03140 904 RPGVLTALMGVSGAGKTTLMDVLAgrKTGGYIEGDIRISG---FPKKQETFARISGYCEQNDIHSPQVTVREsLIysAFL 980
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 100 RGPHKLwrgrlNKEDEEI-VDWALSVTNLEGYEYRL-----LQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVHQ 173
Cdd:PLN03140 981 RLPKEV-----SKEEKMMfVDEVMELVELDNLKDAIvglpgVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAA 1055
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446549187 174 LEVMELVkRLNEEFGMTIIMVLH----DINQAAqysDRLLVLKRG 214
Cdd:PLN03140 1056 AIVMRTV-RNTVDTGRTVVCTIHqpsiDIFEAF---DELLLMKRG 1096
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
12-226 |
8.08e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.11 E-value: 8.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 12 SERFQMQ----NMNVHIKAGEVVSLIGPNGSGKSTLLRliarllkQSEGDIVLDGKSIHTMKSADVAKQLAMLPQmHDHQ 87
Cdd:PTZ00265 1236 MTNEQDYqgdeEQNVGMKNVNEFSLTKEGGSGEDSTVF-------KNSGKILLDGVDICDYNLKDLRNLFSIVSQ-EPML 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 88 LDLTVKELIEFGRGPHKLWRGRLNKEDEEIVDWALSV-----TNLEGYEyrllQSLSGGERQRAWIAMTLAQRTNVLLLD 162
Cdd:PTZ00265 1308 FNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLpnkydTNVGPYG----KSLSGGQKQRIAIARALLREPKILLLD 1383
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446549187 163 EPTTFLDIVHQLEVMELVKRLNEEFGMTIIMVLHDInQAAQYSDRLLVL----KRGK-LQYDGIPEEVL 226
Cdd:PTZ00265 1384 EATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI-ASIKRSDKIVVFnnpdRTGSfVQAHGTHEELL 1451
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
133-225 |
9.89e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 52.43 E-value: 9.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 133 RLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEfGMTIIMVLHDINQAAQYSDRLLVLK 212
Cdd:NF000106 140 RAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVID 218
|
90
....*....|...
gi 446549187 213 RGKLQYDGIPEEV 225
Cdd:NF000106 219 RGRVIADGKVDEL 231
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
17-214 |
1.55e-07 |
|
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: 52.22 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 17 MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKsihtmksadvakqLAMLPQMhDHQLDLTVKELI 96
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQT-SWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 97 EFGRGPHKL-WRGRLN----KEDEEIVDWALSVTNLEGYeyrllQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIV 171
Cdd:TIGR01271 508 IFGLSYDEYrYTSVIKacqlEEDIALFPEKDKTVLGEGG-----ITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVV 582
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446549187 172 HQLEVME--LVKRLNEEFGMTIIMVLHDINQAaqysDRLLVLKRG 214
Cdd:TIGR01271 583 TEKEIFEscLCKLMSNKTRILVTSKLEHLKKA----DKILLLHEG 623
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
17-225 |
3.21e-07 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 50.24 E-value: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 17 MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKsihtmksADVAKQLA-MLPQmhdhqldlTVKEL 95
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------ISFSSQFSwIMPG--------TIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 96 IEFG------RGPHKLWRGRLNKEDEEIVDWALSVTNLEGYeyrllqSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLD 169
Cdd:cd03291 118 IIFGvsydeyRYKSVVKACQLEEDITKFPEKDNTVLGEGGI------TLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446549187 170 IVHQLEVME--LVKRLNEEfgmTIIMVLHDINQAAQySDRLLVLKRGKLQYDGIPEEV 225
Cdd:cd03291 192 VFTEKEIFEscVCKLMANK---TRILVTSKMEHLKK-ADKILILHEGSSYFYGTFSEL 245
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
10-232 |
3.99e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.89 E-value: 3.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 10 AHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLR-LIARLLKQSEGDIVLDGKsihtmksadvakqLAMLPQMhDHQL 88
Cdd:PLN03130 626 SKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGT-------------VAYVPQV-SWIF 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 89 DLTVKELIEFGR--GPHKLWRgrlnkedeeivdwALSVTNLEgYEYRLLQ------------SLSGGERQRAWIAMTLAQ 154
Cdd:PLN03130 692 NATVRDNILFGSpfDPERYER-------------AIDVTALQ-HDLDLLPggdlteigergvNISGGQKQRVSMARAVYS 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 155 RTNVLLLDEPTTFLDIVHQLEVMElvKRLNEEF-GMTIIMV---LHDINQAaqysDRLLVLKRGKLQYDGIPEEvLCH-- 228
Cdd:PLN03130 758 NSDVYIFDDPLSALDAHVGRQVFD--KCIKDELrGKTRVLVtnqLHFLSQV----DRIILVHEGMIKEEGTYEE-LSNng 830
|
....
gi 446549187 229 EMFQ 232
Cdd:PLN03130 831 PLFQ 834
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
32-197 |
6.87e-07 |
|
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: 48.76 E-value: 6.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 32 LIGPNGSGKSTLLRLI--------ARLLKQSEGD-----------------IVLDGKSIHTMKSADVAKQLAMLPQmhdh 86
Cdd:cd03240 27 IVGQNGAGKTTIIEALkyaltgelPPNSKGGAHDpkliregevraqvklafENANGKKYTITRSLAILENVIFCHQ---- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 87 qldltvkeliefgrgphklwrgrlnkedEEIvDWALsvtnlegyeYRLLQSLSGGERQ------RAWIAMTLAQRTNVLL 160
Cdd:cd03240 103 ----------------------------GES-NWPL---------LDMRGRCSGGEKVlasliiRLALAETFGSNCGILA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446549187 161 LDEPTTFLD---IVHQLEvmELVKRLNEEFGMTIIMVLHD 197
Cdd:cd03240 145 LDEPTTNLDeenIEESLA--EIIEERKSQKNFQLIVITHD 182
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
18-211 |
7.87e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.03 E-value: 7.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 18 QNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVL------------------------------------- 60
Cdd:PTZ00265 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIndshnlkdinlkwwrskigvvsqdpllfsnsiknnik 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 61 ------------------DGKSIHTMKSADVAKQLAMLPQMHDHQLDLTVKELIEFGRGPHKLwrgrlnkEDEEIVDWAL 122
Cdd:PTZ00265 482 yslyslkdlealsnyyneDGNDSQENKNKRNSCRAKCAGDLNDMSNTTDSNELIEMRKNYQTI-------KDSEVVDVSK 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 123 S------VTNLEGYEYRLLQS----LSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEFGMTII 192
Cdd:PTZ00265 555 KvlihdfVSALPDKYETLVGSnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITI 634
|
250
....*....|....*....
gi 446549187 193 MVLHDINqAAQYSDRLLVL 211
Cdd:PTZ00265 635 IIAHRLS-TIRYANTIFVL 652
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
129-225 |
1.34e-06 |
|
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: 49.24 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 129 GYEY-RLLQS---LSGGERQRAWIAMTLAQRTN---VLLLDEPTT---FLDIVHQLEVmelVKRLNEEfGMTIIMVLHD- 197
Cdd:TIGR00630 817 GLGYiRLGQPattLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTglhFDDIKKLLEV---LQRLVDK-GNTVVVIEHNl 892
|
90 100 110
....*....|....*....|....*....|....*.
gi 446549187 198 --INQAaqysDRLLVL------KRGKLQYDGIPEEV 225
Cdd:TIGR00630 893 dvIKTA----DYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
24-232 |
1.82e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.07 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 24 IKAGEVVSLIGPNGSGKSTLLRLIARLLKQS---EGDIVLDGksiHTMKSADVAKQLAMLPQMHDHQLDLTVKELIEF-- 98
Cdd:PLN03140 188 IKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNG---YRLNEFVPRKTSAYISQNDVHVGVMTVKETLDFsa 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 99 ---GRGP-HKLWRGRLNKED------EEIVDWALSVTNLEGYEYRL-----------------------LQSLSGGERQR 145
Cdd:PLN03140 265 rcqGVGTrYDLLSELARREKdagifpEAEVDLFMKATAMEGVKSSLitdytlkilgldickdtivgdemIRGISGGQKKR 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 146 AWIAMTLAQRTNVLLLDEPTTFLDivhQLEVMELVKRLNEEFGMTIIMVLHDINQAAQYS----DRLLVLKRGKLQYDGI 221
Cdd:PLN03140 345 VTTGEMIVGPTKTLFMDEISTGLD---SSTTYQIVKCLQQIVHLTEATVLMSLLQPAPETfdlfDDIILLSEGQIVYQGP 421
|
250
....*....|.
gi 446549187 222 PEEVLchEMFQ 232
Cdd:PLN03140 422 RDHIL--EFFE 430
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-225 |
2.07e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.82 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 17 MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEgdivldgksihtMKSADVAKQLAMLPQMhDHQLDLTVKELI 96
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAE------------TSSVVIRGSVAYVPQV-SWIFNATVRENI 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 97 EFGRG--PHKLWRgrlnkedeeivdwALSVTNLEgYEYRLLQ------------SLSGGERQRAWIAMTLAQRTNVLLLD 162
Cdd:PLN03232 700 LFGSDfeSERYWR-------------AIDVTALQ-HDLDLLPgrdlteigergvNISGGQKQRVSMARAVYSNSDIYIFD 765
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446549187 163 EPTTFLD--IVHQLeVMELVKrlNEEFGMTIIMVLHDINQAAQYsDRLLVLKRGKLQYDGIPEEV 225
Cdd:PLN03232 766 DPLSALDahVAHQV-FDSCMK--DELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAEL 826
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
14-197 |
2.45e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.24 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 14 RFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIarllkqsEGDIVLDGKSIhtmkSADVAKQLAMLPQmHDHQLDLTVK 93
Cdd:PRK10636 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALL-------KNEISADGGSY----TFPGNWQLAWVNQ-ETPALPQPAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 94 ELIEFGRGPHKLWRGRLNKEDEE---------------IVDW-----ALSVTNLEGYEYRLLQ----SLSGGERQRAWIA 149
Cdd:PRK10636 82 EYVIDGDREYRQLEAQLHDANERndghaiatihgkldaIDAWtirsrAASLLHGLGFSNEQLErpvsDFSGGWRMRLNLA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446549187 150 MTLAQRTNVLLLDEPTTFLDIVhqlEVMELVKRLNEEFGmTIIMVLHD 197
Cdd:PRK10636 162 QALICRSDLLLLDEPTNHLDLD---AVIWLEKWLKSYQG-TLILISHD 205
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
22-192 |
3.22e-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: 46.20 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 22 VHIKAGEVVSLIGPNGSGKSTLLRLIArllkqsegdIVLDGKSIHTMKSADVAKqlamlpqmhdhqldltvkeliefgrg 101
Cdd:cd03227 16 VTFGEGSLTIITGPNGSGKSTILDAIG---------LALGGAQSATRRRSGVKA-------------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 102 phklwrgRLNKEDEEIVdwalsvtnlegYEYRLLQsLSGGERQRAWIAMTLA----QRTNVLLLDEPTTFLDIVHQLEVM 177
Cdd:cd03227 61 -------GCIVAAVSAE-----------LIFTRLQ-LSGGEKELSALALILAlaslKPRPLYILDEIDRGLDPRDGQALA 121
|
170
....*....|....*
gi 446549187 178 ELVKRLNEEFGMTII 192
Cdd:cd03227 122 EAILEHLVKGAQVIV 136
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-220 |
5.74e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.47 E-value: 5.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 17 MQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDiVLDGKSIhtmksadvakqlAMLPQmhdhQ---LDLTVK 93
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGR-VWAERSI------------AYVPQ----QawiMNATVR 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 94 ELIEFgrgphklwrgrLNKEDEEIVDWALSVTNLE--------GYEYRLLQ---SLSGGERQRAWIAMTLAQRTNVLLLD 162
Cdd:PTZ00243 739 GNILF-----------FDEEDAARLADAVRVSQLEadlaqlggGLETEIGEkgvNLSGGQKARVSLARAVYANRDVYLLD 807
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446549187 163 EPTTFLDI-VHQLEVMELVkrLNEEFGMTIIMVLHDINQAAQySDRLLVLKRGKLQYDG 220
Cdd:PTZ00243 808 DPLSALDAhVGERVVEECF--LGALAGKTRVLATHQVHVVPR-ADYVVALGDGRVEFSG 863
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
17-204 |
7.55e-06 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 46.07 E-value: 7.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 17 MQNMNVHIKAGEVVSLIGPNGSGKSTLL-----RLIARLLKQSEGD----------------IVLD-------------- 61
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlyPALARRLHLKKEQpgnhdrieglehidkvIVIDqspigrtprsnpat 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 62 -------------------------------GKSIhtmksADVakqlamlpqmhdhqLDLTVKELIEFGRGPHKLWRgrl 110
Cdd:cd03271 91 ytgvfdeirelfcevckgkrynretlevrykGKSI-----ADV--------------LDMTVEEALEFFENIPKIAR--- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 111 nkedeeivdwALSVTNLEGYEY-RLLQS---LSGGERQRAWIAMTLAQRTN---VLLLDEPTT---FLDIVHQLEVM-EL 179
Cdd:cd03271 149 ----------KLQTLCDVGLGYiKLGQPattLSGGEAQRIKLAKELSKRSTgktLYILDEPTTglhFHDVKKLLEVLqRL 218
|
250 260
....*....|....*....|....*..
gi 446549187 180 VKRlneefGMTIIMVLH--DINQAAQY 204
Cdd:cd03271 219 VDK-----GNTVVVIEHnlDVIKCADW 240
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
62-196 |
1.20e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 46.17 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 62 GKSIhtmksADVakqlamlpqmhdhqLDLTVKELIEFGRGPHKLwRGRLnkedEEIVDwalsVtnleGYEY-RLLQS--- 137
Cdd:COG0178 779 GKNI-----ADV--------------LDMTVEEALEFFENIPKI-ARKL----QTLQD----V----GLGYiKLGQPatt 826
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446549187 138 LSGGERQRAWIAMTLAQRTN---VLLLDEPTT---FLDIVHQLEVME-LVkrlneEFGMTIIMVLH 196
Cdd:COG0178 827 LSGGEAQRVKLASELSKRSTgktLYILDEPTTglhFHDIRKLLEVLHrLV-----DKGNTVVVIEH 887
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
133-226 |
1.93e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.98 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 133 RLLQSLSGGERQRAWIAMTL-AQRTNVL-LLDEPTTFLDIVHQLEVMELVKRLNEEfGMTIIMVLHDiNQAAQYSDRLLV 210
Cdd:PRK00635 472 RALATLSGGEQERTALAKHLgAELIGITyILDEPSIGLHPQDTHKLINVIKKLRDQ-GNTVLLVEHD-EQMISLADRIID 549
|
90 100
....*....|....*....|..
gi 446549187 211 LKR------GKLQYDGIPEEVL 226
Cdd:PRK00635 550 IGPgagifgGEVLFNGSPREFL 571
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
60-226 |
6.25e-05 |
|
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: 44.23 E-value: 6.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 60 LDGKSIHTMKSADVAKQLAMLpqmhdHQLDLT-VKELIefGRGPHKLWRGRLnkedEEIVDWALSVTNLEgyeyRLLQSL 138
Cdd:TIGR00630 425 VGGKSIADVSELSIREAHEFF-----NQLTLTpEEKKI--AEEVLKEIRERL----GFLIDVGLDYLSLS----RAAGTL 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 139 SGGERQRAWIAMTL-AQRTNVL-LLDEPTTFLdivHQ---LEVMELVKRLnEEFGMTIIMVLHDiNQAAQYSDRLLVL-- 211
Cdd:TIGR00630 490 SGGEAQRIRLATQIgSGLTGVLyVLDEPSIGL---HQrdnRRLINTLKRL-RDLGNTLIVVEHD-EDTIRAADYVIDIgp 564
|
170
....*....|....*....
gi 446549187 212 ----KRGKLQYDGIPEEVL 226
Cdd:TIGR00630 565 gageHGGEVVASGTPEEIL 583
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-74 |
1.70e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 42.09 E-value: 1.70e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446549187 1 MISVNKVFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIA--RLLKQSEGDIVLDGKSIHTMKSADVA 74
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPEDRA 76
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
34-178 |
2.52e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 41.01 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 34 GPNGSGKSTLLRLIARLLKQSEGDIVLdgKSIHTMKSAD-----VAKQLAMlpqmhdhQLDLTVKELIEFgrgphklWRG 108
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYY--KNCNINNIAKpyctyIGHNLGL-------KLEMTVFENLKF-------WSE 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446549187 109 RLNKedEEIVDWALSVTNLEGYEYRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFL-----DIVHQLEVME 178
Cdd:PRK13541 97 IYNS--AETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLskenrDLLNNLIVMK 169
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
32-58 |
3.55e-04 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 41.14 E-value: 3.55e-04
10 20
....*....|....*....|....*..
gi 446549187 32 LIGPNGSGKSTLLRLIARLLKQSEGDI 58
Cdd:COG3950 30 LVGENGSGKTTLLEAIALALSGLLSRL 56
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
22-51 |
3.86e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 37.96 E-value: 3.86e-04
10 20 30
....*....|....*....|....*....|
gi 446549187 22 VHIKAGEVVSLIGPNGSGKSTLLRLIARLL 51
Cdd:pfam13555 17 IPIDPRGNTLLTGPSGSGKSTLLDAIQTLL 46
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
132-197 |
4.90e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 40.32 E-value: 4.90e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 132 YRLLQSLSGGERQRAWIAMTL-AQRTNVL-LLDEPTTFLdivHQLEVMELVKRLNE--EFGMTIIMVLHD 197
Cdd:cd03270 132 SRSAPTLSGGEAQRIRLATQIgSGLTGVLyVLDEPSIGL---HPRDNDRLIETLKRlrDLGNTVLVVEHD 198
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
133-196 |
5.68e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.21 E-value: 5.68e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446549187 133 RLLQS---LSGGERQRAWIAMTLAQRTN---VLLLDEPTT---FLDIVHQLEVM-ELVKRlneefGMTIIMVLH 196
Cdd:PRK00349 823 KLGQPattLSGGEAQRVKLAKELSKRSTgktLYILDEPTTglhFEDIRKLLEVLhRLVDK-----GNTVVVIEH 891
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
21-204 |
5.87e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.77 E-value: 5.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 21 NVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLDGKSIHTMKSADVAKQLAMLPQMHDHQL--------DLTV 92
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDEWQRNNTDMlspgeddtGRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 93 KELIEFGrgphklwrgrlNKEDEEIVDWA--LSVTNLEGyeyRLLQSLSGGERQRAWIAMTLAQRTNVLLLDEPTTFLDI 170
Cdd:PRK10938 103 AEIIQDE-----------VKDPARCEQLAqqFGITALLD---RRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDV 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 446549187 171 VHQLEVMELVKRLNEEfGMTIIMVL---HDINQAAQY 204
Cdd:PRK10938 169 ASRQQLAELLASLHQS-GITLVLVLnrfDEIPDFVQF 204
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-182 |
8.62e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.38 E-value: 8.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 2 ISVNKVFYAHSERFQMQNMNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQS-EGDIVL------DGKSIHTMKS--AD 72
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGySNDLTLfgrrrgSGETIWDIKKhiGY 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 73 VAKQLAMlpqmhDHQLDLTVKELIEFGR----GPHKLWRGRLNKEDEEivdWaLSVTNLEGyeyRL----LQSLSGGERQ 144
Cdd:PRK10938 341 VSSSLHL-----DYRVSTSVRNVILSGFfdsiGIYQAVSDRQQKLAQQ---W-LDILGIDK---RTadapFHSLSWGQQR 408
|
170 180 190
....*....|....*....|....*....|....*...
gi 446549187 145 RAWIAMTLAQRTNVLLLDEPTTFLDIVHQLevmeLVKR 182
Cdd:PRK10938 409 LALIVRALVKHPTLLILDEPLQGLDPLNRQ----LVRR 442
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
32-196 |
9.50e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 39.99 E-value: 9.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 32 LIGPNGSGKSTLLRLIARLLKQSEG---------------------DIVLD---GKSIHTMKSADVAKQLAMLPQMHDHQ 87
Cdd:COG3593 28 LVGENNSGKSSILEALRLLLGPSSSrkfdeedfylgddpdlpeieiELTFGsllSRLLRLLLKEEDKEELEEALEELNEE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 88 LDLTVKELIE----FGRGPHKLWRGRLNKEDEEIVDWA--LSVTNLEGYEYRLLQSlsgGERQRAWIAMTLAQ------- 154
Cdd:COG3593 108 LKEALKALNEllseYLKELLDGLDLELELSLDELEDLLksLSLRIEDGKELPLDRL---GSGFQRLILLALLSalaelkr 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446549187 155 --RTNVLLLDEPTTFLDIVHQLEVMELVKRLNEEfGMTIIMVLH 196
Cdd:COG3593 185 apANPILLIEEPEAHLHPQAQRRLLKLLKELSEK-PNQVIITTH 227
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
21-54 |
1.25e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 39.91 E-value: 1.25e-03
10 20 30
....*....|....*....|....*....|....*..
gi 446549187 21 NVHIKAGEVVSLIGPNGSGKSTL---LRLIARLLKQS 54
Cdd:COG4637 15 DLELPLGPLTVLIGANGSGKSNLldaLRFLSDAARGG 51
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
29-51 |
2.35e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 38.91 E-value: 2.35e-03
|
| COG4928 |
COG4928 |
Predicted P-loop ATPase, KAP-like [General function prediction only]; |
20-61 |
2.79e-03 |
|
Predicted P-loop ATPase, KAP-like [General function prediction only];
Pssm-ID: 443956 Cd Length: 386 Bit Score: 38.74 E-value: 2.79e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 446549187 20 MNVHIKAGEVVSLIGPNGSGKSTLLRLIARLLKQSEGDIVLD 61
Cdd:COG4928 22 KSSDADEPLVIGLDGEWGSGKTSFLNLIEKELESNEKVIVVY 63
|
|
| PRK13341 |
PRK13341 |
AAA family ATPase; |
24-49 |
2.86e-03 |
|
AAA family ATPase;
Pssm-ID: 237354 [Multi-domain] Cd Length: 725 Bit Score: 38.88 E-value: 2.86e-03
10 20
....*....|....*....|....*...
gi 446549187 24 IKAGEVVSLI--GPNGSGKSTLLRLIAR 49
Cdd:PRK13341 47 IKADRVGSLIlyGPPGVGKTTLARIIAN 74
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
21-197 |
3.54e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 38.33 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 21 NVHIKAGE--VVSLIGPNGSGKSTLLRLIARLLKQSEGDIvldgksihtmkSADVAKQLAMLPQMHDHQLDLTVKELIEF 98
Cdd:PRK15064 19 NISVKFGGgnRYGLIGANGCGKSTFMKILGGDLEPSAGNV-----------SLDPNERLGKLRQDQFAFEEFTVLDTVIM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446549187 99 GRgpHKLWrgRLNKEDEEIvdWALS---------VTNLE-------GY--EYR-----------------LLQSLSGGER 143
Cdd:PRK15064 88 GH--TELW--EVKQERDRI--YALPemseedgmkVADLEvkfaemdGYtaEARagelllgvgipeeqhygLMSEVAPGWK 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446549187 144 QRAWIAMTLAQRTNVLLLDEPTTFLDIvHQLEVMELVkrLNEEfGMTIIMVLHD 197
Cdd:PRK15064 162 LRVLLAQALFSNPDILLLDEPTNNLDI-NTIRWLEDV--LNER-NSTMIIISHD 211
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
133-199 |
4.80e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 38.27 E-value: 4.80e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446549187 133 RLLQSLSGGERQRAWIAMTL---AQRTNVLLLDEPTTFLDI--VHQLevMELVKRLNEEfGMTIIMVLHDIN 199
Cdd:PRK00635 805 RPLSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHThdIKAL--IYVLQSLTHQ-GHTVVIIEHNMH 873
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
138-197 |
5.37e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 38.10 E-value: 5.37e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446549187 138 LSGGERQ------RAWIAMTLAQ------RTNVLLLDEPTTFLDIVHQLEVMELVKRLnEEFGM-TIIMVLHD 197
Cdd:PRK02224 782 LSGGERAlfnlslRCAIYRLLAEgiegdaPLPPLILDEPTVFLDSGHVSQLVDLVESM-RRLGVeQIVVVSHD 853
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
24-49 |
5.49e-03 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 37.76 E-value: 5.49e-03
10 20
....*....|....*....|....*...
gi 446549187 24 IKAGEVVSLI--GPNGSGKSTLLRLIAR 49
Cdd:PRK13342 31 IEAGRLSSMIlwGPPGTGKTTLARIIAG 58
|
|
| |
