|
Name |
Accession |
Description |
Interval |
E-value |
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-252 |
4.08e-170 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 469.18 E-value: 4.08e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSIL 80
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 81 RQENTLTARITVEDLVSFGRYPYSHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILLD 160
Cdd:COG4604 81 RQENHINSRLTVRELVAFGRFPYSKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 161 EPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMKDEILSAIYDIDIKVK 240
Cdd:COG4604 161 EPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEVLSDIYDTDIEVE 240
|
250
....*....|..
gi 1150389631 241 DIDGQKIAVYYR 252
Cdd:COG4604 241 EIDGKRICVYFR 252
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-239 |
6.75e-104 |
|
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: 301.58 E-value: 6.75e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSIL 80
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 81 RQENTLTARITVEDLVSFGRYPYSH--GVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYIL 158
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGRYPHLGlfGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 159 LDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMKDEILSAIYDIDIK 238
Cdd:COG1120 161 LDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVYGVEAR 240
|
.
gi 1150389631 239 V 239
Cdd:COG1120 241 V 241
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-239 |
2.02e-76 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 231.83 E-value: 2.02e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSIL 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 81 RQENTLTARITVEDLVSFGRYPY-SH-GVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYIL 158
Cdd:PRK11231 82 PQHHLTPEGITVRELVAYGRSPWlSLwGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 159 LDEPLNNLDMRHAVSMMKRLRNAADElGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMKDEILSAIYDIDIK 238
Cdd:PRK11231 162 LDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVFDVEAE 240
|
.
gi 1150389631 239 V 239
Cdd:PRK11231 241 I 241
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-218 |
4.67e-74 |
|
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: 223.08 E-value: 4.67e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 3 EISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSILRQ 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 83 entltaritvedlvsfgrypyshgvltkedktfvdnAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILLDEP 162
Cdd:cd03214 81 ------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1150389631 163 LNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSG 218
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-239 |
2.21e-71 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 219.26 E-value: 2.21e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSIL 80
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 81 RQENTLTARITVEDLVSFGRYPysHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTD----- 155
Cdd:PRK13548 82 PQHSSLSFPFTVEEVVAMGRAP--HGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQLWEpdgpp 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 156 -YILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMKDEILSAIYD 234
Cdd:PRK13548 160 rWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPETLRRVYG 239
|
....*
gi 1150389631 235 IDIKV 239
Cdd:PRK13548 240 ADVLV 244
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-239 |
4.04e-67 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 208.05 E-value: 4.04e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSIL 80
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 81 RQENTLTARITVEDLVSFGRYPysHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQ---NTD-- 155
Cdd:COG4559 81 PQHSSLAFPFTVEEVVALGRAP--HGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQlwePVDgg 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 156 --YILLDEPLNNLDMRHAVSMMKRLRNAADElGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMKDEILSAIY 233
Cdd:COG4559 159 prWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELLERVY 237
|
....*.
gi 1150389631 234 DIDIKV 239
Cdd:COG4559 238 GADLRV 243
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-239 |
7.47e-67 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 207.25 E-value: 7.47e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKgadfaKRLSIL 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRAR-----RRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 81 RQENTLTAR--ITVEDLVSFGRYPYS--HGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDY 156
Cdd:COG1121 81 PQRAEVDWDfpITVRDVVLMGRYGRRglFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 157 ILLDEPLNNLDMRHAVSMMKRLRNAADElGKTIIMVMHDLNFASCYSDLIIALKEGkLVFSGAPENVMKDEILSAIYDID 236
Cdd:COG1121 161 LLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVLTPENLSRAYGGP 238
|
...
gi 1150389631 237 IKV 239
Cdd:COG1121 239 VAL 241
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-234 |
3.01e-61 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 192.96 E-value: 3.01e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSY-DDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAK---R 76
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRlrrR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 77 LSILRQENTLTARITVEDLVSFGRYPYSH------GVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVI 150
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVLAGRLGRTStwrsllGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 151 SQNTDYILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVmKDEILS 230
Cdd:COG3638 162 VQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL-TDAVLR 240
|
....
gi 1150389631 231 AIYD 234
Cdd:COG3638 241 EIYG 244
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-218 |
7.59e-60 |
|
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: 188.13 E-value: 7.59e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 3 EISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKaKGADFA---KRLSI 79
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK-ERKRIGyvpQRRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 80 LRqentlTARITVEDLVSFGRYPYS--HGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYI 157
Cdd:cd03235 80 DR-----DFPISVRDVVLMGLYGHKglFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1150389631 158 LLDEPLNNLDMRHAVSMMKRLRNAADElGKTIIMVMHDLNFASCYSDLIIALKeGKLVFSG 218
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLN-RTVVASG 213
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-227 |
1.93e-59 |
|
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: 187.54 E-value: 1.93e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNS-IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSIL 80
Cdd:COG1122 1 IELENLSFSYPGGTpALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 81 RQ--ENTLTARiTVEDLVSFGryPYSHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYIL 158
Cdd:COG1122 81 FQnpDDQLFAP-TVEEDVAFG--PENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1150389631 159 LDEPLNNLDMRHAVSMMKRLRNAADElGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMKDE 227
Cdd:COG1122 158 LDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
13-235 |
3.22e-59 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 188.46 E-value: 3.22e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 13 DNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSILRQENTLTARITV 92
Cdd:PRK10575 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGMTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 93 EDLVSFGRYPYsHGVLTK---EDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILLDEPLNNLDMR 169
Cdd:PRK10575 103 RELVAIGRYPW-HGALGRfgaADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1150389631 170 HAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMKDEILSAIYDI 235
Cdd:PRK10575 182 HQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIYGI 247
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-233 |
2.66e-58 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 185.08 E-value: 2.66e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDN-SIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGAD---FAKRL 77
Cdd:cd03256 1 IEVENLSKTYPNGkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 78 SILRQENTLTARITVEDLVSFGRYPYSH------GVLTKEDKtfvDNAISYL---GLDPYRKRFLDELSGGQRQRAFVAM 148
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRLGRRStwrslfGLFPKEEK---QRALAALervGLLDKAYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 149 VISQNTDYILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVmKDEI 228
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL-TDEV 236
|
....*
gi 1150389631 229 LSAIY 233
Cdd:cd03256 237 LDEIY 241
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
11-233 |
1.46e-57 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 184.03 E-value: 1.46e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 11 YDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSILRQENTLTARI 90
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 91 TVEDLVSFGRYPYsHGVLT---KEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILLDEPLNNLD 167
Cdd:PRK10253 97 TVQELVARGRYPH-QPLFTrwrKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1150389631 168 MRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMKDEILSAIY 233
Cdd:PRK10253 176 ISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIY 241
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-238 |
1.44e-54 |
|
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: 175.82 E-value: 1.44e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKaKGADFAKRLSIL 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK-EPREARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 81 RQENTLTARITVEDLVSFgrYPYSHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILLD 160
Cdd:COG4555 80 PDERGLYDRLTVRENIRY--FAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1150389631 161 EPLNNLDMRHAVSMMKRLRNAADElGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMKDEILSAIYDIDIK 238
Cdd:COG4555 158 EPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEENLEDAFVA 234
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-233 |
9.94e-54 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 173.33 E-value: 9.94e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAkGADFAKRLSILR 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARD-PAEVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 82 QENTLTARITVEDLVSF-GRYpysHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILLD 160
Cdd:COG1131 80 QEPALYPDLTVRENLRFfARL---YGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1150389631 161 EPLNNLDMRHAVSMMKRLRNAADElGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENvMKDEILSAIY 233
Cdd:COG1131 157 EPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDE-LKARLLEDVF 227
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-234 |
5.99e-53 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 171.71 E-value: 5.99e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSY-DDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAK---R 76
Cdd:TIGR02315 1 MLEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKlrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 77 LSILRQENTLTARITVEDLVSFGRYPYSH------GVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVI 150
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHGRLGYKPtwrsllGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 151 SQNTDYILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVmKDEILS 230
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL-DDEVLR 239
|
....
gi 1150389631 231 AIYD 234
Cdd:TIGR02315 240 HIYG 243
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-215 |
8.81e-52 |
|
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: 167.70 E-value: 8.81e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADfaKRLSILR 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER--RNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 82 QENTLTARITVEDLVSFGryPYSHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILLDE 161
Cdd:cd03259 79 QDYALFPHLTVAENIAFG--LKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1150389631 162 PLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLV 215
Cdd:cd03259 157 PLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-213 |
1.48e-51 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 166.87 E-value: 1.48e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 3 EISHVFKSYDDNS--IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSIL 80
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 81 RQ--ENTLTARiTVEDLVSFGryPYSHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYIL 158
Cdd:cd03225 81 FQnpDDQFFGP-TVEEEVAFG--LENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1150389631 159 LDEPLNNLDMRHAVSMMKRLRNAADElGKTIIMVMHDLNFASCYSDLIIALKEGK 213
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-239 |
1.51e-51 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 172.72 E-value: 1.51e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSIL 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 81 RQENTLTARITVEDLVSFGRYPYSH--GVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYIL 158
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVEMGRTPHRSrfDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 159 LDEPLNNLDMRHAVSMMKRLRNAADElGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMKDEILSAIYDIDIK 238
Cdd:PRK09536 163 LDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFDARTA 241
|
.
gi 1150389631 239 V 239
Cdd:PRK09536 242 V 242
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-226 |
4.08e-50 |
|
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: 171.24 E-value: 4.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNS-----IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGAD--- 72
Cdd:COG1123 260 LLEVRNLSKRYPVRGkggvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlre 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 73 FAKRLSILRQ--ENTLTARITVEDLVSFGryPYSHGVLTKED-KTFVDNAISYLGLDP-YRKRFLDELSGGQRQRAFVAM 148
Cdd:COG1123 340 LRRRVQMVFQdpYSSLNPRMTVGDIIAEP--LRLHGLLSRAErRERVAELLERVGLPPdLADRYPHELSGGQRQRVAIAR 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1150389631 149 VISQNTDYILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMKD 226
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-214 |
2.03e-49 |
|
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: 161.50 E-value: 2.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNS----IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFA--- 74
Cdd:cd03255 1 IELKNLSKTYGGGGekvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 75 -KRLSILRQENTLTARITVEDLVSFGryPYSHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQN 153
Cdd:cd03255 81 rRHIGFVFQSFNLLPDLTALENVELP--LLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1150389631 154 TDYILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFAScYSDLIIALKEGKL 214
Cdd:cd03255 159 PKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-215 |
5.07e-47 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 155.59 E-value: 5.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNS----IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKgadfAKR 76
Cdd:COG1136 4 LLELRNLTKSYGTGEgevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLS----ERE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 77 LSILRQEN--------TLTARITVEDLVSFGRYPysHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAM 148
Cdd:COG1136 80 LARLRRRHigfvfqffNLLPELTALENVALPLLL--AGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1150389631 149 VISQNTDYILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFAScYSDLIIALKEGKLV 215
Cdd:COG1136 158 ALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAA-RADRVIRLRDGRIV 223
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
10-200 |
1.06e-45 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 151.23 E-value: 1.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 10 SYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGidvtkakgadfAKRLSILRQENTLTAR 89
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRSEVPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 90 --ITVEDLVSFGRYPY--SHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILLDEPLNN 165
Cdd:NF040873 70 lpLTVRDLVAMGRWARrgLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190
....*....|....*....|....*....|....*
gi 1150389631 166 LDMRHAVSMMKRLRNAADElGKTIIMVMHDLNFAS 200
Cdd:NF040873 150 LDAESRERIIALLAEEHAR-GATVVVVTHDLELVR 183
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-221 |
1.33e-45 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 152.22 E-value: 1.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNSIieDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKakgADFAKR-LSI 79
Cdd:COG3840 1 MLRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTA---LPPAERpVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 80 LRQENTLTARITVEDLVSFGRYPysHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILL 159
Cdd:COG3840 76 LFQENNLFPHLTVAQNIGLGLRP--GLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1150389631 160 DEPLNNLD--MRHavSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPE 221
Cdd:COG3840 154 DEPFSALDpaLRQ--EMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTA 215
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-224 |
1.59e-45 |
|
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: 152.45 E-value: 1.59e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNS-IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSIL 80
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 81 RQENTLTARITVEDLVsfGRYPYSHGVLTKEDKTFVDNAISYLGLDP--YRKRFLDELSGGQRQRAFVAMVISQNTDYIL 158
Cdd:cd03295 81 IQQIGLFPHMTVEENI--ALVPKLLKWPKEKIRERADELLALVGLDPaeFADRYPHELSGGQQQRVGVARALAADPPLLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1150389631 159 LDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVM 224
Cdd:cd03295 159 MDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-215 |
5.90e-45 |
|
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: 151.11 E-value: 5.90e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSY----DDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKR 76
Cdd:COG1124 1 MLEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 77 LSILRQ--ENTLTARITVEDLVSfgrYPY-SHGVLTKEDKtfVDNAISYLGLDP-YRKRFLDELSGGQRQRAFVAMVISQ 152
Cdd:COG1124 81 VQMVFQdpYASLHPRHTVDRILA---EPLrIHGLPDREER--IAELLEQVGLPPsFLDRYPHQLSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1150389631 153 NTDYILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLV 215
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIV 218
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
20-246 |
2.46e-44 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 149.61 E-value: 2.46e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 20 LSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPiTKGRITVDGIDVTKAKGADFAKRLSILRQENTLTARITVEDLVSFG 99
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAELARHRAYLSQQQSPPFAMPVFQYLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 100 rypYSHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQ-----NTD--YILLDEPLNNLDMRHAV 172
Cdd:COG4138 94 ---QPAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptiNPEgqLLLLDEPMNSLDVAQQA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1150389631 173 SMMKRLRNAAdELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMKDEILSAIYDIDIKVKDIDGQK 246
Cdd:COG4138 171 ALDRLLRELC-QQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVFGVKFRRLEVEGHR 243
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-225 |
4.48e-43 |
|
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: 145.89 E-value: 4.48e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFA---KRL 77
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelrRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 78 SILRQENTLTARITVEDLVSFG-RYpysHGVLTKEDKT-FVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTD 155
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVAFPlRE---HTDLSEAEIReLVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1150389631 156 YILLDEPLNNLD---MRHAVSMMKRLRnaaDELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMK 225
Cdd:COG1127 162 ILLYDEPTAGLDpitSAVIDELIRELR---DELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-221 |
7.03e-43 |
|
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: 145.34 E-value: 7.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGAD---FAKRLS 78
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 79 ILRQENTLTARITVEDLVSFgryP-YSHGVLTKEDKT-FVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDY 156
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAF---PlREHTRLSEEEIReIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPEL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1150389631 157 ILLDEPLNNLD---MRHAVSMMKRLRnaaDELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPE 221
Cdd:cd03261 158 LLYDEPTAGLDpiaSGVIDDLIRSLK---KELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPE 222
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-237 |
1.00e-42 |
|
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: 144.54 E-value: 1.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNS----IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAkgadfAKRL 77
Cdd:cd03293 1 LEVRNVSKTYGGGGgavtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP-----GPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 78 SILRQENTLTARITVEDLVSFGryPYSHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYI 157
Cdd:cd03293 76 GYVFQQDALLPWLTVLDNVALG--LELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 158 LLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIalkegklVFSGAPENVmkdeilSAIYDIDI 237
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVV-------VLSARPGRI------VAEVEVDL 220
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-214 |
1.15e-42 |
|
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: 142.92 E-value: 1.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKaKGADFAKRLSILR 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 82 QENTLTARITVEDLVsfgrypyshgvltkedktfvdnaisylgldpyrkrfldELSGGQRQRAFVAMVISQNTDYILLDE 161
Cdd:cd03230 80 EEPSLYENLTVRENL--------------------------------------KLSGGMKQRLALAQALLHDPELLILDE 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1150389631 162 PLNNLDMRHAVSMMKRLRNAADElGKTIIMVMHDLNFASCYSDLIIALKEGKL 214
Cdd:cd03230 122 PTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-213 |
1.26e-42 |
|
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: 143.10 E-value: 1.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKG--ADFAKRLSI 79
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDelPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 80 LRQENTLTARITVEDLVSFGrypyshgvltkedktfvdnaisylgldpyrkrfldeLSGGQRQRAFVAMVISQNTDYILL 159
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG------------------------------------LSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1150389631 160 DEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGK 213
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-215 |
1.71e-42 |
|
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: 144.19 E-value: 1.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNS----IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFA-- 74
Cdd:cd03257 1 LLEVKNLSVSFPTGGgsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 75 -KRLSILRQE--NTLTARITVEDLVSFGryPYSHGVLTKED--KTFVDNAISYLGLDPYR-KRFLDELSGGQRQRAFVAM 148
Cdd:cd03257 81 rKEIQMVFQDpmSSLNPRMTIGEQIAEP--LRIHGKLSKKEarKEAVLLLLVGVGLPEEVlNRYPHELSGGQRQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1150389631 149 VISQNTDYILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLV 215
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-227 |
3.19e-42 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 144.90 E-value: 3.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNS-----IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGadfaKR 76
Cdd:TIGR04521 1 IKLKNVSYIYQPGTpfekkALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKK----KK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 77 LSILRQ---------ENTLTARiTVEDLVSFGryPYSHGVLTKEDKTFVDNAISYLGLDP-YRKR--FldELSGGQRQRA 144
Cdd:TIGR04521 77 LKDLRKkvglvfqfpEHQLFEE-TVYKDIAFG--PKNLGLSEEEAEERVKEALELVGLDEeYLERspF--ELSGGQMRRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 145 FVAMVISQNTDYILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVM 224
Cdd:TIGR04521 152 AIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVF 231
|
...
gi 1150389631 225 KDE 227
Cdd:TIGR04521 232 SDV 234
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-219 |
3.24e-42 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 143.27 E-value: 3.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSY-DDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAK---R 76
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYlrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 77 LSILRQENTLTARITVEDLVSFG-RYpysHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTD 155
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPlRV---TGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1150389631 156 YILLDEPLNNLDMRHAVSMMKRLRnAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGA 219
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLE-EINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEA 220
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
2-218 |
1.42e-41 |
|
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: 141.48 E-value: 1.42e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNSIieDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADfaKRLSILR 81
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSMLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 82 QENTLTARITVEDLVSFGRYPYSHgvLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILLDE 161
Cdd:cd03298 77 QENNLFAHLTVEQNVGLGLSPGLK--LTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1150389631 162 PLNNLD--MRHavSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSG 218
Cdd:cd03298 155 PFAALDpaLRA--EMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-223 |
1.65e-41 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 145.24 E-value: 1.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTkakgaDFA--KR-L 77
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT-----GLPpeKRnV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 78 SILRQENTLTARITVEDLVSFGryPYSHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRafVA----MVIsqN 153
Cdd:COG3842 80 GMVFQDYALFPHLTVAENVAFG--LRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQR--VAlaraLAP--E 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 154 TDYILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENV 223
Cdd:COG3842 154 PRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-226 |
6.24e-41 |
|
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: 146.97 E-value: 6.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSY--DDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPIT---KGRITVDGIDVTKAKGADFAK 75
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 76 RLSILRQEnTLTA--RITVEDLVSFGryPYSHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQN 153
Cdd:COG1123 84 RIGMVFQD-PMTQlnPVTVGDQIAEA--LENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1150389631 154 TDYILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMKD 226
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-227 |
1.35e-40 |
|
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: 139.49 E-value: 1.35e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAkRLSILR 81
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIA-RLGIGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 82 --QENTLTARITVEDLV-----SFGRYPYSHGVLTKEDKTFVDNA---ISYLGLDPYRKRFLDELSGGQRQRAFVAMVIS 151
Cdd:cd03219 80 tfQIPRLFPELTVLENVmvaaqARTGSGLLLARARREEREARERAeelLERVGLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1150389631 152 QNTDYILLDEPLNNLDMRHAVSMMKRLRNAADElGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMKDE 227
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNP 234
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-213 |
2.38e-40 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 136.22 E-value: 2.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 3 EISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSILRQ 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 83 entltaritvedlvsfgrypyshgvltkedktfvdnaisylgldpyrkrfldeLSGGQRQRAFVAMVISQNTDYILLDEP 162
Cdd:cd00267 81 -----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1150389631 163 LNNLDMRHAVSMMKRLRNAADElGKTIIMVMHDLNFASCYSDLIIALKEGK 213
Cdd:cd00267 108 TSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-227 |
5.19e-40 |
|
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: 138.63 E-value: 5.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKR---- 76
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLgiar 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 77 ----------LSILrqENTLTARI------TVEDLVSFGRYPYSHGVLTKEdktfVDNAISYLGLDPYRKRFLDELSGGQ 140
Cdd:COG0411 84 tfqnprlfpeLTVL--ENVLVAAHarlgrgLLAALLRLPRARREEREARER----AEELLERVGLADRADEPAGNLSYGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 141 RQRAFVAMVISQNTDYILLDEP---LNNLDMRHavsMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFS 217
Cdd:COG0411 158 QRRLEIARALATEPKLLLLDEPaagLNPEETEE---LAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAE 234
|
250
....*....|
gi 1150389631 218 GAPENVMKDE 227
Cdd:COG0411 235 GTPAEVRADP 244
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-223 |
5.29e-40 |
|
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: 137.75 E-value: 5.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTkakGADFAKR-LSIL 80
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT---NLPPHKRpVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 81 RQENTLTARITVEDLVSFGRYpySHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILLD 160
Cdd:cd03300 78 FQNYALFPHLTVFENIAFGLR--LKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1150389631 161 EPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENV 223
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-164 |
1.35e-39 |
|
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: 134.31 E-value: 1.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 17 IEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSILRQENTLTARITVEDLV 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1150389631 97 SFGRYPYshGVLTKEDKTFVDNAISYLGLDPYRKRFLD----ELSGGQRQRAFVAMVISQNTDYILLDEPLN 164
Cdd:pfam00005 81 RLGLLLK--GLSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-201 |
2.42e-39 |
|
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: 135.30 E-value: 2.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAkGADFAKRLSIL 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDA-REDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 81 RQENTLTARITVEDLVSFgrypYS--HGVLTKEDKtfVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYIL 158
Cdd:COG4133 81 GHADGLKPELTVRENLRF----WAalYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1150389631 159 LDEPLNNLDmRHAVSMMKRLRNAADELGKTIIMVMHD-LNFASC 201
Cdd:COG4133 155 LDEPFTALD-AAGVALLAELIAAHLARGGAVLLTTHQpLELAAA 197
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-214 |
2.58e-39 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 135.33 E-value: 2.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSILR 81
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 82 QENTLTARiTVEDLVSFGrYPYSHGVLTKEDktfVDNAISYLGLDPYrkrFLD----ELSGGQRQRAFVAMVISQNTDYI 157
Cdd:COG4619 81 QEPALWGG-TVRDNLPFP-FQLRERKFDRER---ALELLERLGLPPD---ILDkpveRLSGGERQRLALIRALLLQPDVL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 158 LLDEPLNNLD---MRHAVSMMKRLRNAAdelGKTIIMVMHDLNFASCYSDLIIALKEGKL 214
Cdd:COG4619 153 LLDEPTSALDpenTRRVEELLREYLAEE---GRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-243 |
6.56e-39 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 135.60 E-value: 6.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKG-RITV-----DGIDVTKAKgadfa 74
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLfgerrGGEDVWELR----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 75 KRLSIL--RQENTLTARITVEDLV------SFGRYPYshgvLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFV 146
Cdd:COG1119 78 KRIGLVspALQLRFPRDETVLDVVlsgffdSIGLYRE----PTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 147 --AMVIsqNTDYILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLN-FASCYSDLIIaLKEGKLVFSGAPENV 223
Cdd:COG1119 154 arALVK--DPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEeIPPGITHVLL-LKDGRVVAAGPKEEV 230
|
250 260
....*....|....*....|
gi 1150389631 224 MKDEILSAIYDIDIKVKDID 243
Cdd:COG1119 231 LTSENLSEAFGLPVEVERRD 250
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-196 |
1.73e-38 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 134.83 E-value: 1.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNS----IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGadfakR 76
Cdd:COG1116 7 ALELRGVSKRFPTGGggvtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP-----D 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 77 LSILRQENTLTARITVEDLVSFGryPYSHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDY 156
Cdd:COG1116 82 RGVVFQEPALLPWLTVLDNVALG--LELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1150389631 157 ILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDL 196
Cdd:COG1116 160 LLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDV 199
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-215 |
1.90e-38 |
|
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: 133.15 E-value: 1.90e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADfaKRLSILR 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 82 QENTLTARITVEDLVSFGRypYSHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILLDE 161
Cdd:cd03301 79 QNYALYPHMTVYDNIAFGL--KLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1150389631 162 PLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLV 215
Cdd:cd03301 157 PLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-223 |
8.64e-38 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 135.20 E-value: 8.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTkakGADFAKRlsil 80
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVT---DLPPKDR---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 81 rqentltaRI-------------TVEDLVSFG----RYPyshgvltKED-KTFVDNAISYLGLDPYRKRFLDELSGGQRQ 142
Cdd:COG3839 76 --------NIamvfqsyalyphmTVYENIAFPlklrKVP-------KAEiDRRVREAAELLGLEDLLDRKPKQLSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 143 RafVAM--VISQNTDYILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHD----LNFAscysDLIIALKEGKLVF 216
Cdd:COG3839 141 R--VALgrALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDqveaMTLA----DRIAVMNDGRIQQ 214
|
....*..
gi 1150389631 217 SGAPENV 223
Cdd:COG3839 215 VGTPEEL 221
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-218 |
2.01e-37 |
|
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: 130.78 E-value: 2.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNSIIEDLSLQIPKGgMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGAdFAKRLSILR 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-LRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 82 QENTLTARITVEDLVSfgrypYS---HGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYIL 158
Cdd:cd03264 79 QEFGVYPNFTVREFLD-----YIawlKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1150389631 159 LDEPLNNLDMRHAVsmmkRLRNAADELG--KTIIMVMHDL-NFASCYSDLIIaLKEGKLVFSG 218
Cdd:cd03264 154 VDEPTAGLDPEERI----RFRNLLSELGedRIVILSTHIVeDVESLCNQVAV-LNKGKLVFEG 211
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
20-246 |
2.54e-37 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 131.59 E-value: 2.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 20 LSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPiTKGRITVDGIDVTKAKGADFAKRLSILRQENTLTARITVEDLVSFG 99
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 100 RYPyshGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQ-------NTDYILLDEPLNNLDMRHAV 172
Cdd:PRK03695 94 QPD---KTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDVAQQA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1150389631 173 SMmKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMKDEILSAIYDIDIKVKDIDGQK 246
Cdd:PRK03695 171 AL-DRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVFGVNFRRLDVEGHP 243
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-222 |
2.90e-36 |
|
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: 127.87 E-value: 2.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKaKGADFAKRLSILR 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 82 Q----ENTLTARitvEDLVSFGRYpysHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYI 157
Cdd:cd03265 80 QdlsvDDELTGW---ENLYIHARL---YGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1150389631 158 LLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPEN 222
Cdd:cd03265 154 FLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-218 |
2.90e-36 |
|
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: 127.87 E-value: 2.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNS----IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKgADFAKR 76
Cdd:cd03266 1 MITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEP-AEARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 77 LSILRQENTLTARITV-EDLVSFGRYpysHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTD 155
Cdd:cd03266 80 LGFVSDSTGLYDRLTArENLEYFAGL---YGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1150389631 156 YILLDEPLNNLDM---RHAVSMMKRLRnaadELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSG 218
Cdd:cd03266 157 VLLLDEPTTGLDVmatRALREFIRQLR----ALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-223 |
6.36e-36 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 127.42 E-value: 6.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKgadfaKRLSIL 80
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSK-----KDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 81 RQE--------NtLTARITVEDLVSFGryPYSHGVLTKEDKTfvDNAISYL---GLDPYRKRFLDELSGGQRQR-AFV-- 146
Cdd:COG1126 76 RRKvgmvfqqfN-LFPHLTVLENVTLA--PIKVKKMSKAEAE--ERAMELLervGLADKADAYPAQLSGGQQQRvAIAra 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 147 -AMvisqNTDYILLDEPLNNLD--MRHAV-SMMKRLrnaADElGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPEN 222
Cdd:COG1126 151 lAM----EPKVMLFDEPTSALDpeLVGEVlDVMRDL---AKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEE 222
|
.
gi 1150389631 223 V 223
Cdd:COG1126 223 F 223
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-244 |
8.74e-36 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 128.02 E-value: 8.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLP--------ITKGRITVDGIDVTKAKGAD 72
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTLNGEPLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 73 FAKRLSILRQENTLTARITVEDLVSFGRYPYSH--GVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVI 150
Cdd:PRK13547 81 LARLRAVLPQAAQPAFAFSAREIVLLGRYPHARraGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 151 SQ---------NTDYILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPE 221
Cdd:PRK13547 161 AQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPA 240
|
250 260
....*....|....*....|...
gi 1150389631 222 NVMKDEILSAIYDIDIKVKDIDG 244
Cdd:PRK13547 241 DVLTPAHIARCYGFAVRLVDAGD 263
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-225 |
1.52e-35 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 129.45 E-value: 1.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKgadFAKR-LSIL 80
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRS---IQQRdICMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 81 RQENTLTARITVEDLVSFGRypYSHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILLD 160
Cdd:PRK11432 84 FQSYALFPHMSLGENVGYGL--KMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1150389631 161 EPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMK 225
Cdd:PRK11432 162 EPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYR 226
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-231 |
4.22e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 126.39 E-value: 4.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSY-DDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSIL 80
Cdd:PRK13647 5 IEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 81 RQE-NTLTARITVEDLVSFGryPYSHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILL 159
Cdd:PRK13647 85 FQDpDDQVFSSTVWDDVAFG--PVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1150389631 160 DEPLNNLDMRHAVSMMKRLrNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMKDEILSA 231
Cdd:PRK13647 163 DEPMAYLDPRGQETLMEIL-DRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIVEQ 233
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-227 |
1.13e-34 |
|
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: 130.27 E-value: 1.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNS--IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSI 79
Cdd:COG4987 334 LELEDVSFRYPGAGrpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 80 LRQ----------ENTLTAR--ITVEDLVSfgrypyshgVLTK---EDktFVDNAISylGLDpyrkRFLDE----LSGGQ 140
Cdd:COG4987 414 VPQrphlfdttlrENLRLARpdATDEELWA---------ALERvglGD--WLAALPD--GLD----TWLGEggrrLSGGE 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 141 RQRAFVAMVISQNTDYILLDEPLNNLDMRHAVSMMKRLRNAADelGKTIIMVMHDLNFAScYSDLIIALKEGKLVFSGAP 220
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLE-RMDRILVLEDGRIVEQGTH 553
|
....*..
gi 1150389631 221 ENVMKDE 227
Cdd:COG4987 554 EELLAQN 560
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-213 |
2.04e-34 |
|
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: 121.72 E-value: 2.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNS--IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSI 79
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 80 LRQENTLtaritvedlvsFgrypyshgvltkeDKTFVDNaIsylgldpyrkrfldeLSGGQRQRAFVAMVISQNTDYILL 159
Cdd:cd03228 81 VPQDPFL-----------F-------------SGTIREN-I---------------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1150389631 160 DEPLNNLDMRHAVSMMKRLRNAADelGKTIIMVMHDLNFASCYsDLIIALKEGK 213
Cdd:cd03228 121 DEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIRDA-DRIIVLDDGR 171
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-243 |
5.38e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 123.56 E-value: 5.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNS--IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLS 78
Cdd:PRK13632 7 MIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 79 ILRQ--ENTLTArITVEDLVSFG----RYPyshgvlTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQ 152
Cdd:PRK13632 87 IIFQnpDNQFIG-ATVEDDIAFGlenkKVP------PKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 153 NTDYILLDEPLNNLD---MRHAVSMMKRLRNAADelgKTIIMVMHDLNFAsCYSDLIIALKEGKLVFSGAPENVMKDE-- 227
Cdd:PRK13632 160 NPEIIIFDESTSMLDpkgKREIKKIMVDLRKTRK---KTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEILNNKei 235
|
250 260
....*....|....*....|..
gi 1150389631 228 ILSA------IYDIDIKVKDID 243
Cdd:PRK13632 236 LEKAkidspfIYKLSKKLKGID 257
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-227 |
7.91e-34 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 127.95 E-value: 7.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHV-FKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSIL 80
Cdd:COG4988 337 IELEDVsFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 81 RQENTLTArITVEDLVSFGRypyshGVLTKED------KTFVDNAISYL--GLDpyrkRFLDE----LSGGQRQRAFVAM 148
Cdd:COG4988 417 PQNPYLFA-GTIRENLRLGR-----PDASDEEleaaleAAGLDEFVAALpdGLD----TPLGEggrgLSGGQAQRLALAR 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1150389631 149 VISQNTDYILLDEPLNNLDMRHAVSMMKRLRNAADelGKTIIMVMHDLNFASCYsDLIIALKEGKLVFSGAPENVMKDE 227
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQA-DRILVLDDGRIVEQGTHEELLAKN 562
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
21-228 |
1.54e-33 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 121.23 E-value: 1.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 21 SLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGadfAKR-LSILRQENTLTARITVEDLVSFG 99
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPP---SRRpVSMLFQENNLFSHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 100 RYPyshGV-LTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILLDEPLNNLD--MRHavSMMK 176
Cdd:PRK10771 96 LNP---GLkLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDpaLRQ--EMLT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1150389631 177 RLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMKDEI 228
Cdd:PRK10771 171 LVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKA 222
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-225 |
1.68e-33 |
|
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: 127.64 E-value: 1.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNS--IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSI 79
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 80 LRQENTLTARiTVEDLVSFGRyPYshgvLTKEDktfVDNAISYLGLDPYRKRF-------LDE----LSGGQRQRAFVAM 148
Cdd:COG2274 554 VLQDVFLFSG-TIRENITLGD-PD----ATDEE---IIEAARLAGLHDFIEALpmgydtvVGEggsnLSGGQRQRLAIAR 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1150389631 149 VISQNTDYILLDEPLNNLDMRHAVSMMKRLRNAADelGKTIIMVMHDLNFAScYSDLIIALKEGKLVFSGAPENVMK 225
Cdd:COG2274 625 ALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIR-LADRIIVLDKGRIVEDGTHEELLA 698
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-223 |
2.17e-33 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 120.91 E-value: 2.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADfaKRLSILR 81
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 82 QENTLTARITVEDLVSFG--RYPYSHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILL 159
Cdd:cd03296 81 QHYALFRHMTVFDNVAFGlrVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1150389631 160 DEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENV 223
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-214 |
4.58e-33 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 119.17 E-value: 4.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKgadfaKRLSILR 81
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDK-----KNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 82 QEN-------TLTARITVEDLVSFGryPYShgVLTKEDKTFVDNAISYL---GLDPYRKRFLDELSGGQRQRAFVAMVIS 151
Cdd:cd03262 76 QKVgmvfqqfNLFPHLTVLENITLA--PIK--VKGMSKAEAEERALELLekvGLADKADAYPAQLSGGQQQRVAIARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1150389631 152 QNTDYILLDEPLNNLD--MRHAV-SMMKRLrnaADElGKTIIMVMHDLNFASCYSDLIIALKEGKL 214
Cdd:cd03262 152 MNPKVMLFDEPTSALDpeLVGEVlDVMKDL---AEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-218 |
5.72e-33 |
|
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: 118.92 E-value: 5.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAkrlsILR 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIG----YLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 82 QENTLTARITVED-LVSFGRYpysHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRA-FVAMVISQnTDYILL 159
Cdd:cd03269 77 EERGLYPKMKVIDqLVYLAQL---KGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVqFIAAVIHD-PELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1150389631 160 DEPLNNLDMRHAVSMMKRLRNAADElGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSG 218
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-225 |
6.36e-33 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 120.89 E-value: 6.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNS--IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSI 79
Cdd:PRK13635 6 IRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 80 LRQ--ENTLTArITVEDLVSFGRYpySHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYI 157
Cdd:PRK13635 86 VFQnpDNQFVG-ATVQDDVAFGLE--NIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1150389631 158 LLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFAScYSDLIIALKEGKLVFSGAPENVMK 225
Cdd:PRK13635 163 ILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAA-QADRVIVMNKGEILEEGTPEEIFK 229
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
11-214 |
7.93e-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: 118.81 E-value: 7.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 11 YDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAkgADFAKRLSILRQENTLTARI 90
Cdd:TIGR01277 8 YEYEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGL--APYQRPVSMLFQENNLFAHL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 91 TVEDLVSFGRYPyshGV-LTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILLDEPLNNLDMR 169
Cdd:TIGR01277 86 TVRQNIGLGLHP---GLkLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1150389631 170 HAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKL 214
Cdd:TIGR01277 163 LREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-221 |
1.06e-32 |
|
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: 118.82 E-value: 1.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITK-----GRITVDGIDVTKAKGADFA-- 74
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPgapdeGEVLLDGKDIYDLDVDVLElr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 75 KRLSILRQENTLTaRITVEDLVSFGryPYSHGVLTKED-KTFVDNAISYLGLDPYRKRFLD--ELSGGQRQRAFVAMVIS 151
Cdd:cd03260 81 RRVGMVFQKPNPF-PGSIYDNVAYG--LRLHGIKLKEElDERVEEALRKAALWDEVKDRLHalGLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 152 QNTDYILLDEPLNNLDMRHAVSMMKRLRNAADELgkTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPE 221
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTE 225
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-227 |
1.12e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 120.18 E-value: 1.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSY-DDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDG--IDVTKAKGADFAKRL 77
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 78 SILRQ--ENTLTARiTVEDLVSFGryPYSHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTD 155
Cdd:PRK13639 81 GIVFQnpDDQLFAP-TVEEDVAFG--PLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1150389631 156 YILLDEPLNNLDMRHAVSMMKRLRNAADElGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMKDE 227
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-220 |
1.94e-32 |
|
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: 117.99 E-value: 1.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSY--DDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFaKRLSI 79
Cdd:cd03263 1 LQIRNLTKTYkkGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAAR-QSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 80 LRQENTLTARITVEDLVSFgrypYS--HGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYI 157
Cdd:cd03263 80 CPQFDALFDELTVREHLRF----YArlKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1150389631 158 LLDEPLNNLD--MRHAV-SMMKRLRnaadeLGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAP 220
Cdd:cd03263 156 LLDEPTSGLDpaSRRAIwDLILEVR-----KGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSP 216
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-213 |
2.38e-32 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 117.35 E-value: 2.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDN-SIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAK---R 76
Cdd:TIGR02673 1 MIEFHNVSKAYPGGvAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLlrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 77 LSILRQENTLTARITVEDLVSFgryPYS-HGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTD 155
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVAL---PLEvRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1150389631 156 YILLDEPLNNLDMRHAVSMMkRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGK 213
Cdd:TIGR02673 158 LLLADEPTGNLDPDLSERIL-DLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-218 |
5.39e-32 |
|
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: 116.55 E-value: 5.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGAdfAKRLSILR 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA--LRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 82 QENTLTARIT-VEDLVSFGRYpysHGVLTKEdktfVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILLD 160
Cdd:cd03268 79 EAPGFYPNLTaRENLRLLARL---LGIRKKR----IDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1150389631 161 EPLNNLDMRHAVSMMKRLRNAADElGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSG 218
Cdd:cd03268 152 EPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-226 |
6.74e-32 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 117.12 E-value: 6.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLS-- 78
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 79 ILRQENTLTARITVEDLVSFGryPYSHGVLTKED-KTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYI 157
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFG--PLRVRGASKEEaEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1150389631 158 LLDEPLNNLD--MRHAVsmMKRLRNAADElGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMKD 226
Cdd:PRK09493 159 LFDEPTSALDpeLRHEV--LKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKN 226
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-226 |
7.16e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 118.27 E-value: 7.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNS------IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGA-DF 73
Cdd:PRK13633 4 MIKCKNVSYKYESNEesteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 74 AKRLSILRQ--ENTLTARITVEDlVSFGryPYSHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVIS 151
Cdd:PRK13633 84 RNKAGMVFQnpDNQIVATIVEED-VAFG--PENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1150389631 152 QNTDYILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFAScYSDLIIALKEGKLVFSGAPENVMKD 226
Cdd:PRK13633 161 MRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAV-EADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-226 |
1.29e-31 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 115.99 E-value: 1.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKR-LSIL 80
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 81 RQENTLTARITVEDLVSFGRYPyshgvLTKEDKTFVDNAIsyLGLDPYRKRFLD----ELSGGQRQRAFVAMVISQNTDY 156
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYA-----RRRAKRKARLERV--YELFPRLKERRKqlagTLSGGEQQMLAIARALMSRPKL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1150389631 157 ILLDEPLNNL--DMRHAVS-MMKRLRnaadELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMKD 226
Cdd:cd03224 154 LLLDEPSEGLapKIVEEIFeAIRELR----DEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-223 |
1.50e-31 |
|
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: 116.14 E-value: 1.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNS----IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGAD---F 73
Cdd:cd03258 1 MIELKNVSKVFGDTGgkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 74 AKRLS-ILRQENTLTARiTVEDLVSfgrYPYS-HGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVIS 151
Cdd:cd03258 81 RRRIGmIFQHFNLLSSR-TVFENVA---LPLEiAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1150389631 152 QNTDYILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENV 223
Cdd:cd03258 157 NNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-226 |
2.67e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 116.63 E-value: 2.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNS-IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTK-AKGADFAKRLS 78
Cdd:PRK13644 1 MIRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDfSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 79 ILRQ--ENTLTARiTVEDLVSFGryPYSHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDY 156
Cdd:PRK13644 81 IVFQnpETQFVGR-TVEEDLAFG--PENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPEC 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 157 ILLDEPLNNLDMRHAVSMMKRLRNaADELGKTIIMVMHDLNFASCySDLIIALKEGKLVFSGAPENVMKD 226
Cdd:PRK13644 158 LIFDEVTSMLDPDSGIAVLERIKK-LHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVLSD 225
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
17-225 |
1.04e-30 |
|
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: 113.97 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 17 IEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADfaKRLSILRQENTLTARITVEDLV 96
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK--RDISYVPQNYALFPHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 97 SFG----RYPyshgvlTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILLDEPLNNLDMRHAV 172
Cdd:cd03299 93 AYGlkkrKVD------KKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1150389631 173 SMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMK 225
Cdd:cd03299 167 KLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFK 219
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-227 |
1.18e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 114.94 E-value: 1.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNS-IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDG--IDVTKAKGADFAKRL 77
Cdd:PRK13636 5 ILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 78 SILRQ--ENTLTARITVEDlVSFGryPYSHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTD 155
Cdd:PRK13636 85 GMVFQdpDNQLFSASVYQD-VSFG--AVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPK 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1150389631 156 YILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMKDE 227
Cdd:PRK13636 162 VLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-223 |
3.10e-30 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 115.70 E-value: 3.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAkgADFAKRLSIL 80
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV--PPYQRPINMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 81 RQENTLTARITVEDLVSFGrypyshgvlTKEDK-------TFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQN 153
Cdd:PRK11607 97 FQSYALFPHMTVEQNIAFG---------LKQDKlpkaeiaSRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 154 TDYILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENV 223
Cdd:PRK11607 168 PKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2-232 |
4.08e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 113.58 E-value: 4.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNSIIE-----DLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGAdfaKR 76
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFErralyDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKN---KK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 77 LSILRQ---------ENTLTARiTVEDLVSFGryPYSHGVLTKEDKTFVDNAISYLGLDP-YRKRFLDELSGGQRQRAFV 146
Cdd:PRK13634 80 LKPLRKkvgivfqfpEHQLFEE-TVEKDICFG--PMNFGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 147 AMVISQNTDYILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMKD 226
Cdd:PRK13634 157 AGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFAD 236
|
....*..
gi 1150389631 227 -EILSAI 232
Cdd:PRK13634 237 pDELEAI 243
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-220 |
7.11e-30 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 114.66 E-value: 7.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADfakrlsilR 81
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN--------R 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 82 QENT------LTARITVEDLVSFG-RYpysHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNT 154
Cdd:PRK09452 87 HVNTvfqsyaLFPHMTVFENVAFGlRM---QKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1150389631 155 DYILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAP 220
Cdd:PRK09452 164 KVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTP 229
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-218 |
7.64e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 113.28 E-value: 7.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKgadfAKRLSIL 80
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIGYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 81 RQENTLTARITVED-LVSFGRYpysHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRA-FVAMVISqNTDYIL 158
Cdd:COG4152 77 PEERGLYPKMKVGEqLVYLARL---KGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVqLIAALLH-DPELLI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1150389631 159 LDEPLNNLDmRHAVSMMKR-LRNAADElGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSG 218
Cdd:COG4152 153 LDEPFSGLD-PVNVELLKDvIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSG 211
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-215 |
8.03e-30 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 110.81 E-value: 8.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 3 EISHV-FKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGidvTKAKGADFAKRLSILR 81
Cdd:cd03226 1 RIENIsFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 82 QE-NTLTARITVEDLVSFGRYPYShgvltkEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILLD 160
Cdd:cd03226 78 QDvDYQLFTDSVREELLLGLKELD------AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1150389631 161 EPLNNLDMRHAVSMMKRLRNAADElGKTIIMVMHDLNFASCYSDLIIALKEGKLV 215
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-226 |
1.01e-29 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 114.03 E-value: 1.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADfaKRLSILR 81
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 82 QENTLTARITVEDLVSFG-------RYPYSHGVLTKedktfVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNT 154
Cdd:PRK10851 81 QHYALFRHMTVFDNIAFGltvlprrERPNAAAIKAK-----VTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1150389631 155 DYILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMKD 226
Cdd:PRK10851 156 QILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWRE 227
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-225 |
1.36e-29 |
|
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: 110.78 E-value: 1.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYD-DNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSIL 80
Cdd:cd03254 3 IEFENVNFSYDeKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 81 RQENTLTARiTVEDLVSFGRyPYShgvlTKEDktfVDNAISYLGLDPYRKRF---LDE--------LSGGQRQRAFVAMV 149
Cdd:cd03254 83 LQDTFLFSG-TIMENIRLGR-PNA----TDEE---VIEAAKEAGAHDFIMKLpngYDTvlgenggnLSQGERQLLAIARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1150389631 150 ISQNTDYILLDEPLNNLDmrhaVSMMKRLRNAADEL--GKTIIMVMHDLNFAScYSDLIIALKEGKLVFSGAPENVMK 225
Cdd:cd03254 154 MLRDPKILILDEATSNID----TETEKLIQEALEKLmkGRTSIIIAHRLSTIK-NADKILVLDDGKIIEEGTHDELLA 226
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-229 |
2.04e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 111.82 E-value: 2.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDN--SIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLL---PITKGRITVDGIDVTKAKGADFAKR 76
Cdd:PRK13640 6 VEFKHVSFTYPDSkkPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 77 LSILRQ--ENTLTArITVEDLVSFGRYpySHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNT 154
Cdd:PRK13640 86 VGIVFQnpDNQFVG-ATVGDDVAFGLE--NRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1150389631 155 DYILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFAScYSDLIIALKEGKLVFSGAPENVMKDEIL 229
Cdd:PRK13640 163 KIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPVEIFSKVEM 236
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
17-229 |
2.31e-29 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 111.51 E-value: 2.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 17 IEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSiLRQENTLTARITVEDLV 96
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVP-QSEEVDWSFPVLVEDVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 97 SFGRYPYShGVL---TKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILLDEPLNNLDMRHAVS 173
Cdd:PRK15056 102 MMGRYGHM-GWLrraKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEAR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1150389631 174 MMKRLRNAADElGKTIIMVMHDLNFASCYSDLIIALKeGKLVFSGAPENVMKDEIL 229
Cdd:PRK15056 181 IISLLRELRDE-GKTMLVSTHNLGSVTEFCDYTVMVK-GTVLASGPTETTFTAENL 234
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
19-218 |
2.74e-29 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 109.69 E-value: 2.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 19 DLSLQIPkGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDG-IDVTKAKGADFA---KRLSILRQENTLTARITVED 94
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtVLFDSRKKINLPpqqRKIGLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 95 LVSFGRYPYShgvlTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQR-AFVAMVISQnTDYILLDEPLNNLDMRHAVS 173
Cdd:cd03297 95 NLAFGLKRKR----NREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRvALARALAAQ-PELLLLDEPFSALDRALRLQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1150389631 174 MMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSG 218
Cdd:cd03297 170 LLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-216 |
3.53e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 110.56 E-value: 3.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNSIIE-----DLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAK 75
Cdd:COG1101 1 MLELKNLSKTFNPGTVNEkraldGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 76 RLSILRQENTL-TA-RITVED--LVSFGR---YPYSHGVLTKEDKTFVDN-AISYLGLDpyrKRfLDE----LSGGQRQR 143
Cdd:COG1101 81 YIGRVFQDPMMgTApSMTIEEnlALAYRRgkrRGLRRGLTKKRRELFRELlATLGLGLE---NR-LDTkvglLSGGQRQA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1150389631 144 AFVAMVISQNTDYILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVF 216
Cdd:COG1101 157 LSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIIL 229
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
19-229 |
7.56e-29 |
|
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: 109.66 E-value: 7.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 19 DLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADF----AKRLSILRQENTLTARITVED 94
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLPHRTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 95 LVSFGRYpySHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILLDEPLNNLDMRHAVSM 174
Cdd:cd03294 122 NVAFGLE--VQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREM 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1150389631 175 MKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPEnvmkdEIL 229
Cdd:cd03294 200 QDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPE-----EIL 249
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-214 |
1.08e-28 |
|
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: 107.88 E-value: 1.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNSI-IEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGadfaKRLSIL 80
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRG----RAIPYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 81 R-------QENTLTARITVEDLVSFGRYPYSHGvlTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQN 153
Cdd:cd03292 77 RrkigvvfQDFRLLPDRNVYENVAFALEVTGVP--PREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1150389631 154 TDYILLDEPLNNLDMRHAVSMMkRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKL 214
Cdd:cd03292 155 PTILIADEPTGNLDPDTTWEIM-NLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
17-232 |
1.47e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 109.37 E-value: 1.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 17 IEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVT--KAKGADFAKRLSILRQ--ENTLTARiTV 92
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIRKKVGLVFQypEYQLFEE-TI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 93 EDLVSFGryPYSHGVLTKEDKTFVDNAISYLGLD--PYRKRFLDELSGGQRQRAFVAMVISQNTDYILLDEPLNNLDMRH 170
Cdd:PRK13637 102 EKDIAFG--PINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKG 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1150389631 171 AVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMKD-EILSAI 232
Cdd:PRK13637 180 RDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEvETLESI 242
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-233 |
2.20e-28 |
|
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: 107.76 E-value: 2.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKR-LSI 79
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 80 LRQENTLTARITVEDLVSFGRYPYSHGVLTKEDKTFVdnaisyLGLDPYRKRFLD----ELSGGQRQ-----RAFVAmvi 150
Cdd:COG0410 83 VPEGRRIFPSLTVEENLLLGAYARRDRAEVRADLERV------YELFPRLKERRRqragTLSGGEQQmlaigRALMS--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 151 sqNTDYILLDEPLNNL------DMRHAVsmmKRLRnaadELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVM 224
Cdd:COG0410 154 --RPKLLLLDEPSLGLapliveEIFEII---RRLN----REGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELL 224
|
....*....
gi 1150389631 225 KDEILSAIY 233
Cdd:COG0410 225 ADPEVREAY 233
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-221 |
3.30e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 108.28 E-value: 3.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNS---IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRL 77
Cdd:PRK13650 4 IIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 78 SILRQ--ENTLTArITVEDLVSFGRYpySHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTD 155
Cdd:PRK13650 84 GMVFQnpDNQFVG-ATVEDDVAFGLE--NKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1150389631 156 YILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFAScYSDLIIALKEGKLVFSGAPE 221
Cdd:PRK13650 161 IIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPR 225
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-218 |
3.47e-28 |
|
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: 106.97 E-value: 3.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 16 IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLP---ITKGRITVDGIDVTKAKgadFAKRLSILRQENTLTARITV 92
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQPRKPDQ---FQKCVAYVRQDDILLPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 93 EDLVSF-----GRYPYSHGVLTKEDktfVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILLDEPLNNLD 167
Cdd:cd03234 99 RETLTYtailrLPRKSSDAIRKKRV---EDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1150389631 168 MRHAVSMMKRLRNAADElGKTIIMVMH----DLnfascYS--DLIIALKEGKLVFSG 218
Cdd:cd03234 176 SFTALNLVSTLSQLARR-NRIVILTIHqprsDL-----FRlfDRILLLSSGEIVYSG 226
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-224 |
7.45e-28 |
|
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: 106.55 E-value: 7.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNS-IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSIL 80
Cdd:cd03253 1 IEFENVTFAYDPGRpVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 81 RQENTLTARiTVEDLVSFGRYPyshgvLTKEDktfVDNAISYLGLDPYRKRFLD-----------ELSGGQRQRAFVAMV 149
Cdd:cd03253 81 PQDTVLFND-TIGYNIRYGRPD-----ATDEE---VIEAAKAAQIHDKIMRFPDgydtivgerglKLSGGEKQRVAIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1150389631 150 ISQNTDYILLDEPLNNLDMRHAVSMMKRLRNAADelGKTIIMVMHDLNFAScYSDLIIALKEGKLVFSGAPENVM 224
Cdd:cd03253 152 ILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIV-NADKIIVLKDGRIVERGTHEELL 223
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-228 |
1.02e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 108.38 E-value: 1.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDV-TKAKGAdfAKRLSIL 80
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVpARARLA--RARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 81 RQENTLTARITV-EDLVSFGRYpysHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILL 159
Cdd:PRK13536 120 PQFDNLDLEFTVrENLLVFGRY---FGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1150389631 160 DEPLNNLD--MRHAVsmMKRLRnAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMKDEI 228
Cdd:PRK13536 197 DEPTTGLDphARHLI--WERLR-SLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHI 264
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-225 |
1.57e-27 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 110.25 E-value: 1.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNS-IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSIL 80
Cdd:COG1132 340 IEFENVSFSYPGDRpVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 81 RQENTLTARiTVEDLVSFGRYPYshgvlTKEDktfVDNAISYLGLDPYRKRF---LD--------ELSGGQRQ-----RA 144
Cdd:COG1132 420 PQDTFLFSG-TIRENIRYGRPDA-----TDEE---VEEAAKAAQAHEFIEALpdgYDtvvgergvNLSGGQRQriaiaRA 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 145 FVAmvisqNTDYILLDEPLNNLDMRHAvsmmKRLRNAADEL--GKTIIMVMHDLN---FAscysDLIIALKEGKLVFSGA 219
Cdd:COG1132 491 LLK-----DPPILILDEATSALDTETE----ALIQEALERLmkGRTTIVIAHRLStirNA----DRILVLDDGRIVEQGT 557
|
....*.
gi 1150389631 220 PENVMK 225
Cdd:COG1132 558 HEELLA 563
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-196 |
3.25e-27 |
|
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: 109.37 E-value: 3.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNSIIED-LSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSIL 80
Cdd:TIGR02868 335 LELRDLSAGYPGAPPVLDgVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 81 RQENTLTARiTVEDLVSFGRypyshGVLTKEDktfVDNAISYLGLDPYRKRFLD-----------ELSGGQRQRAFVAMV 149
Cdd:TIGR02868 415 AQDAHLFDT-TVRENLRLAR-----PDATDEE---LWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARA 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1150389631 150 ISQNTDYILLDEPLNNLDMRHAVSMMKRLRnAADElGKTIIMVMHDL 196
Cdd:TIGR02868 486 LLADAPILLLDEPTEHLDAETADELLEDLL-AALS-GRTVVLITHHL 530
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-209 |
5.15e-27 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 108.53 E-value: 5.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDD-NSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSIL 80
Cdd:TIGR02857 322 LEFSGVSVAYPGrRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 81 RQENTLTARiTVEDLVSFGRyPYShgvltkeDKTFVDNAISYLGLDPYRK-------RFLDE----LSGGQRQRAFVAMV 149
Cdd:TIGR02857 402 PQHPFLFAG-TIAENIRLAR-PDA-------SDAEIREALERAGLDEFVAalpqgldTPIGEggagLSGGQAQRLALARA 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 150 ISQNTDYILLDEPLNNLDMRHAVSMMKRLRNAADelGKTIIMVMHDLNFASCYsDLIIAL 209
Cdd:TIGR02857 473 FLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALA-DRIVVL 529
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-196 |
5.97e-27 |
|
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: 105.91 E-value: 5.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNS----IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLP---ITKGRITVDGIDVTKAKGADF 73
Cdd:COG0444 1 LLEVRNLKVYFPTRRgvvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 74 ----AKRLSILRQE--NTLTARITVEDLVSFG-RYpysHGVLTKEDKTfvDNAISYL---GLdPYRKRFLD----ELSGG 139
Cdd:COG0444 81 rkirGREIQMIFQDpmTSLNPVMTVGDQIAEPlRI---HGGLSKAEAR--ERAIELLervGL-PDPERRLDryphELSGG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1150389631 140 QRQRAFVAMVISQNTDYILLDEPLNNLDmrhaVS-------MMKRLRnaaDELGKTIIMVMHDL 196
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALD----VTiqaqilnLLKDLQ---RELGLAILFITHDL 211
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
19-232 |
7.00e-27 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 106.35 E-value: 7.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 19 DLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDV-TKAKGADFA---KRLSILRQENTLTARITV-E 93
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfDSRKGIFLPpekRRIGYVFQEARLFPHLSVrG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 94 DLvsfgRYPYSHgVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILLDEPLNNLDMRHAVS 173
Cdd:TIGR02142 95 NL----RYGMKR-ARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1150389631 174 MMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMKDEILSAI 232
Cdd:TIGR02142 170 ILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWL 228
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-195 |
9.30e-27 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 105.55 E-value: 9.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNS----IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGadfaKR 76
Cdd:COG1135 1 MIELENLSKTFPTKGgpvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSE----RE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 77 LSILRQE--------NTLTARiTVEDLVSFgryPYSH-GVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVA 147
Cdd:COG1135 77 LRAARRKigmifqhfNLLSSR-TVAENVAL---PLEIaGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1150389631 148 MVISQNTDYILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHD 195
Cdd:COG1135 153 RALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHE 200
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-195 |
9.49e-27 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 104.17 E-value: 9.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNS----IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTkAKGADFAkr 76
Cdd:COG4525 3 MLTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVT-GPGADRG-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 77 lsILRQENTLTARITVEDLVSFG---RypyshGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQN 153
Cdd:COG4525 80 --VVFQKDALLPWLNVLDNVAFGlrlR-----GVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAAD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1150389631 154 TDYILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHD 195
Cdd:COG4525 153 PRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
17-226 |
1.01e-26 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 106.66 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 17 IEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFA----KRLSILRQENTLTARITV 92
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 93 EDLVSFGRYpySHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILLDEPLNNLDMRHAV 172
Cdd:PRK10070 124 LDNTAFGME--LAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1150389631 173 SMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMKD 226
Cdd:PRK10070 202 EMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
4-220 |
2.46e-26 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 105.11 E-value: 2.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 4 ISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGI---DVTKAKgadfaKRLSIL 80
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmnDVPPAE-----RGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 81 RQENTLTARITVEDLVSFGRYpyshgvLTKEDKT----FVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDY 156
Cdd:PRK11000 81 FQSYALYPHLSVAENMSFGLK------LAGAKKEeinqRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1150389631 157 ILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAP 220
Cdd:PRK11000 155 FLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKP 218
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-199 |
2.69e-26 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 102.86 E-value: 2.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVtKAKGADfakRLSIL 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV-EGPGAE---RGVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 81 RQENTLTARiTVEDLVSFGRypYSHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILLD 160
Cdd:PRK11248 77 QNEGLLPWR-NVQDNVAFGL--QLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLD 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 1150389631 161 EPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFA 199
Cdd:PRK11248 154 EPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEA 192
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
19-197 |
2.78e-26 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 104.04 E-value: 2.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 19 DLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKrlsiLRQE---------NTLTAR 89
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRP----LRRRmqmvfqdpyASLNPR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 90 ITVEDLVSFGryPYSHGVLTKED-KTFVDNAISYLGLDP-YRKRFLDELSGGQRQRAFVAMVISQNTDYILLDEPLNNLD 167
Cdd:COG4608 112 MTVGDIIAEP--LRIHGLASKAErRERVAELLELVGLRPeHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
170 180 190
....*....|....*....|....*....|....*..
gi 1150389631 168 mrhaVS-------MMKRLRnaaDELGKTIIMVMHDLN 197
Cdd:COG4608 190 ----VSiqaqvlnLLEDLQ---DELGLTYLFISHDLS 219
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
32-226 |
2.81e-26 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 104.11 E-value: 2.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 32 IIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAkgADFAKRLSILRQENTLTARITVEDLVSFGRYpySHGVLTKE 111
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNV--PPHLRHINMVFQSYALFPHMTVEENVAFGLK--MRKVPRAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 112 DKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIM 191
Cdd:TIGR01187 77 IKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVF 156
|
170 180 190
....*....|....*....|....*....|....*
gi 1150389631 192 VMHDLNFASCYSDLIIALKEGKLVFSGAPENVMKD 226
Cdd:TIGR01187 157 VTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEE 191
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-221 |
2.89e-26 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 102.78 E-value: 2.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLL---PITKGRITVDGIDVTKAK--GADFAK 75
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQREGrlARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 76 RLS----ILRQENtLTARITVEDLV---SFGRYPYSHGVL---TKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAF 145
Cdd:PRK09984 84 SRAntgyIFQQFN-LVNRLSVLENVligALGSTPFWRTCFswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1150389631 146 VAMVISQNTDYILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPE 221
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQ 238
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-223 |
3.97e-26 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 104.07 E-value: 3.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTkakgadfakrlsilr 81
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF--------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 82 qeNTLTAR----------------ITVEDLVSFGryPYSHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRaf 145
Cdd:COG1118 68 --TNLPPRerrvgfvfqhyalfphMTVAENIAFG--LRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQR-- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 146 VAM--VISQNTDYILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENV 223
Cdd:COG1118 142 VALarALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
17-242 |
6.84e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 102.55 E-value: 6.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 17 IEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTkAKGADfaKRLSILRQENTLTARI------ 90
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIT-HKTKD--KYIRPVRKRIGMVFQFpesqlf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 91 --TVEDLVSFGryPYSHGVLTKEDKTFVDNAISYLG-------LDPYrkrfldELSGGQRQRAFVAMVISQNTDYILLDE 161
Cdd:PRK13646 100 edTVEREIIFG--PKNFKMNLDEVKNYAHRLLMDLGfsrdvmsQSPF------QMSGGQMRKIAIVSILAMNPDIIVLDE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 162 PLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMKDeiLSAIYDIDIKVKD 241
Cdd:PRK13646 172 PTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD--KKKLADWHIGLPE 249
|
.
gi 1150389631 242 I 242
Cdd:PRK13646 250 I 250
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-226 |
1.09e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 102.12 E-value: 1.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNS-----IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGAD--- 72
Cdd:PRK13643 1 MIKFEKVNYTYQPNSpfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeik 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 73 -FAKRLSILRQ--ENTLTARITVEDlVSFGryPYSHGVLTKEDKTFVDNAISYLGLDpyrKRFLD----ELSGGQRQRAF 145
Cdd:PRK13643 81 pVRKKVGVVFQfpESQLFEETVLKD-VAFG--PQNFGIPKEKAEKIAAEKLEMVGLA---DEFWEkspfELSGGQMRRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 146 VAMVISQNTDYILLDEPLNNLDMRHAVSMMKrLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMK 225
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQ-LFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
.
gi 1150389631 226 D 226
Cdd:PRK13643 234 E 234
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-233 |
1.13e-25 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 100.70 E-value: 1.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKA---KGAdfakRLS 78
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLpmhKRA----RLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 79 I--LRQENTLTARITVED-LVSFGRYpysHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTD 155
Cdd:cd03218 77 IgyLPQEASIFRKLTVEEnILAVLEI---RGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 156 YILLDEPLNNLDMRhAVS----MMKRLRNaadelgKTIIMVMHDLN----FASCysDLIIALKEGKLVFSGAPENVMKDE 227
Cdd:cd03218 154 FLLLDEPFAGVDPI-AVQdiqkIIKILKD------RGIGVLITDHNvretLSIT--DRAYIIYEGKVLAEGTPEEIAANE 224
|
....*.
gi 1150389631 228 ILSAIY 233
Cdd:cd03218 225 LVRKVY 230
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
17-226 |
4.26e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 100.29 E-value: 4.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 17 IEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGA----DFAKRLSILRQ--ENTLTARI 90
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNknlkKLRKKVSLVFQfpEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 91 TVEDlVSFGryPYSHGVLTKEDKTFVDNAISYLGLD-------PYrkrfldELSGGQRQRAFVAMVISQNTDYILLDEPL 163
Cdd:PRK13641 103 VLKD-VEFG--PKNFGFSEDEAKEKALKWLKKVGLSedlisksPF------ELSGGQMRRVAIAGVMAYEPEILCLDEPA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1150389631 164 NNLDMRHAVSMMKRLRNAADElGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMKD 226
Cdd:PRK13641 174 AGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSD 235
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-195 |
4.64e-25 |
|
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: 103.09 E-value: 4.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVdGIDVtkakgadfakRLSILR 81
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------KLAYVD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 82 QE-NTLTARITVEDLVSFGrypysHGVLTKEDKTFvdNAISYLGLDPYR----KRFLDELSGGQRQRAFVAMVISQNTDY 156
Cdd:TIGR03719 392 QSrDALDPNKTVWEEISGG-----LDIIKLGKREI--PSRAYVGRFNFKgsdqQKKVGQLSGGERNRVHLAKTLKSGGNV 464
|
170 180 190
....*....|....*....|....*....|....*....
gi 1150389631 157 ILLDEPLNNLDmrhaVSMMKRLRNAADELGKTIIMVMHD 195
Cdd:TIGR03719 465 LLLDEPTNDLD----VETLRALEEALLNFAGCAVVISHD 499
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-195 |
6.65e-25 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 101.07 E-value: 6.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYD-DNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGAD------F 73
Cdd:PRK11650 3 GLKLQAVRKSYDgKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADrdiamvF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 74 akrlsilrQENTLTARITVEDLVSFG---RypyshGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRafVAM-- 148
Cdd:PRK11650 83 --------QNYALYPHMSVRENMAYGlkiR-----GMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQR--VAMgr 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1150389631 149 VISQNTDYILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHD 195
Cdd:PRK11650 148 AIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHD 194
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
22-235 |
6.76e-25 |
|
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: 98.38 E-value: 6.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 22 LQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAkgadfakRLSI----LRQENTLTARITVEDLVS 97
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKG-------WRHIgyvpQRHEFAWDFPISVAHTVM 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 98 FGRYPYShGVL---TKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILLDEPLNNLDMRHAVSM 174
Cdd:TIGR03771 74 SGRTGHI-GWLrrpCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1150389631 175 MKRLRNAADElGKTIIMVMHDLNFASCYSDLIIaLKEGKLVFSGAPENVMKDEILSAIYDI 235
Cdd:TIGR03771 153 TELFIELAGA-GTAILMTTHDLAQAMATCDRVV-LLNGRVIADGTPQQLQDPAPWMTTFGV 211
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-214 |
7.57e-25 |
|
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: 96.90 E-value: 7.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNS--IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSI 79
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 80 LRQENTLtaritvedlvsFgrypyshgvltkeDKTFVDNAisylgldpyrkrfldeLSGGQRQRAFVAMVISQNTDYILL 159
Cdd:cd03246 81 LPQDDEL-----------F-------------SGSIAENI----------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1150389631 160 DEPLNNLD------MRHAVSMMKrlrnaadELGKTIIMVMHDLN-FASCysDLIIALKEGKL 214
Cdd:cd03246 121 DEPNSHLDvegeraLNQAIAALK-------AAGATRIVIAHRPEtLASA--DRILVLEDGRV 173
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-218 |
7.83e-25 |
|
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: 98.05 E-value: 7.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDD--NSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSI 79
Cdd:cd03245 3 IEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 80 LRQENTLTARiTVEDLVSFGRyPYShgvltkeDKTFVDNAISYLGLDPYRKRF---LD--------ELSGGQRQRAFVAM 148
Cdd:cd03245 83 VPQDVTLFYG-TLRDNITLGA-PLA-------DDERILRAAELAGVTDFVNKHpngLDlqigergrGLSGGQRQAVALAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 149 VISQNTDYILLDEPLNNLDMRHAVSMMKRLRNAADelGKTIIMVMHDLNFAScYSDLIIALKEGKLVFSG 218
Cdd:cd03245 154 ALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLLD-LVDRIIVMDSGRIVADG 220
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-227 |
8.66e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 99.06 E-value: 8.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHV-FKSYDDNSI-IEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLS 78
Cdd:PRK13648 7 IIVFKNVsFQYQSDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 79 ILRQ--ENTLTARITVEDlVSFGRYpySHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDY 156
Cdd:PRK13648 87 IVFQnpDNQFVGSIVKYD-VAFGLE--NHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSV 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1150389631 157 ILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFAScYSDLIIALKEGKLVFSGAPENVMKDE 227
Cdd:PRK13648 164 IILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAM-EADHVIVMNKGTVYKEGTPTEIFDHA 233
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-213 |
1.18e-24 |
|
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: 95.21 E-value: 1.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGidvtkakgadfakrlsilr 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 82 qentltaritvedlvsfgrypyshgvltkedktfvDNAISYlgldpyrkrfLDELSGGQRQRAFVAMVISQNTDYILLDE 161
Cdd:cd03221 62 -----------------------------------TVKIGY----------FEQLSGGEKMRLALAKLLLENPNLLLLDE 96
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1150389631 162 PLNNLDMRHAVSmmkrLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGK 213
Cdd:cd03221 97 PTNHLDLESIEA----LEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-218 |
1.53e-24 |
|
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: 96.23 E-value: 1.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNS--IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGAdFAKRLSI 79
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 80 LRQEntltaritvedlvsfgryPYSHgvltkeDKTFVDNaisyLGldpyrKRFldelSGGQRQRAFVAMVISQNTDYILL 159
Cdd:cd03247 80 LNQR------------------PYLF------DTTLRNN----LG-----RRF----SGGERQRLALARILLQDAPIVLL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1150389631 160 DEPLNNLDMRHAVSMMKRLRNAADElgKTIIMVMHDLNFAScYSDLIIALKEGKLVFSG 218
Cdd:cd03247 123 DEPTVGLDPITERQLLSLIFEVLKD--KTLIWITHHLTGIE-HMDKILFLENGKIIMQG 178
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-227 |
1.89e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 99.00 E-value: 1.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNSIIE-----DLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRI------------------ 58
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTElkaldNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 59 TVDGIDVTKAKGADFAKRLSILRQ--------ENTLTARiTVEDLVSFGryPYSHGVLTKEDKTFVDNAISYLGLD-PYR 129
Cdd:PRK13651 83 VLEKLVIQKTRFKKIKKIKEIRRRvgvvfqfaEYQLFEQ-TIEKDIIFG--PVSMGVSKEEAKKRAAKYIELVGLDeSYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 130 KRFLDELSGGQRQRAFVAMVISQNTDYILLDEPLNNLDMRHAVSMMKRLRNAADElGKTIIMVMHDLNFASCYSDLIIAL 209
Cdd:PRK13651 160 QRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFF 238
|
250
....*....|....*...
gi 1150389631 210 KEGKLVFSGAPENVMKDE 227
Cdd:PRK13651 239 KDGKIIKDGDTYDILSDN 256
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-215 |
1.90e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 101.29 E-value: 1.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVdGIDVtkakgadfakRLSIL 80
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------KIGYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 81 RQEN-TLTARITVEDLVSfgryPYSHGVLTKEdktfvdnAISYLGldpyrkRFL---DE-------LSGGQRQRAFVAMV 149
Cdd:COG0488 384 DQHQeELDPDKTVLDELR----DGAPGGTEQE-------VRGYLG------RFLfsgDDafkpvgvLSGGEKARLALAKL 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1150389631 150 ISQNTDYILLDEPLNNLDM--RHAvsmmkrLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLV 215
Cdd:COG0488 447 LLSPPNVLLLDEPTNHLDIetLEA------LEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-224 |
2.24e-24 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 97.73 E-value: 2.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGAD-----FAK- 75
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDgqlkvADKn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 76 -------RLSILRQENTLTARITVedLVSFGRYPYSHGVLTKEDKTfvDNAISYL---GLDPY-RKRFLDELSGGQRQRA 144
Cdd:PRK10619 86 qlrllrtRLTMVFQHFNLWSHMTV--LENVMEAPIQVLGLSKQEAR--ERAVKYLakvGIDERaQGKYPVHLSGGQQQRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 145 FVAMVISQNTDYILLDEPLNNLDMRHAVSMMKRLRNAADElGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVM 224
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLF 240
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-212 |
2.42e-24 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 97.15 E-value: 2.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 17 IEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTkAKGADfakRLSILrQENTLTARITVEDLV 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQIT-EPGPD---RMVVF-QNYSLLPWLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 97 SFGRYPYSHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILLDEPLNNLDMRHAVSMMK 176
Cdd:TIGR01184 76 ALAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQE 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 1150389631 177 RLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEG 212
Cdd:TIGR01184 156 ELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
12-231 |
2.78e-24 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 101.10 E-value: 2.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 12 DDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSILRQENTL---TA 88
Cdd:TIGR03375 476 QETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNIGYVPQDPRLfygTL 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 89 RitvEDLVSFGRYPYSHGVLTKEDKTFVDNAISYL--GLDpyrkRFLDE----LSGGQRQRAFVAMVISQNTDYILLDEP 162
Cdd:TIGR03375 556 R---DNIALGAPYADDEEILRAAELAGVTEFVRRHpdGLD----MQIGErgrsLSGGQRQAVALARALLRDPPILLLDEP 628
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1150389631 163 LNNLDMRHAVSMMKRLRNAAdeLGKTIIMVMHDLNFAScYSDLIIALKEGKLVFSGApenvmKDEILSA 231
Cdd:TIGR03375 629 TSAMDNRSEERFKDRLKRWL--AGKTLVLVTHRTSLLD-LVDRIIVMDNGRIVADGP-----KDQVLEA 689
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
16-218 |
3.19e-24 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 95.70 E-value: 3.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 16 IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMIS--RLLPITKGRITVDGIDVTKAKgadFAKRLSILRQENTLTARITVE 93
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLDKRS---FRKIIGYVPQDDILHPTLTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 94 DLVSFgrypyshgvltkedktfvdNAIsylgldpyrkrfLDELSGGQRQRAFVAMVISQNTDYILLDEPLNNLDMRHAVS 173
Cdd:cd03213 101 ETLMF-------------------AAK------------LRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1150389631 174 MMKRLRNAADElGKTIIMVMH---DLNFASCysDLIIALKEGKLVFSG 218
Cdd:cd03213 150 VMSLLRRLADT-GRTIICSIHqpsSEIFELF--DKLLLLSQGRVIYFG 194
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1-215 |
4.91e-24 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 97.18 E-value: 4.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNS---------IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGA 71
Cdd:TIGR02769 2 LLEVRDVTHTYRTGGlfgakqrapVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 72 D---FAKRLSILRQE--NTLTARITVEDLVsfgRYPYSHgvLTKEDKTFVDNAISYL----GLDP-YRKRFLDELSGGQR 141
Cdd:TIGR02769 82 QrraFRRDVQLVFQDspSAVNPRMTVRQII---GEPLRH--LTSLDESEQKARIAELldmvGLRSeDADKLPRQLSGGQL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1150389631 142 QRAFVAMVISQNTDYILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLV 215
Cdd:TIGR02769 157 QRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIV 230
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-228 |
8.68e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 97.18 E-value: 8.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAkgADFAK-RLSIL 80
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSR--ARHARqRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 81 RQENTLTARITV-EDLVSFGRYpysHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILL 159
Cdd:PRK13537 86 PQFDNLDPDFTVrENLLVFGRY---FGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1150389631 160 DEPLNNLD--MRHAvsMMKRLRNAADElGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMKDEI 228
Cdd:PRK13537 163 DEPTTGLDpqARHL--MWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEI 230
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
9-215 |
1.07e-23 |
|
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: 95.11 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 9 KSYDDNS----IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAK----RLSIL 80
Cdd:TIGR02211 9 KRYQEGKldtrVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKlrnkKLGFI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 81 RQENTLTARITVEDLVSFgryPYSHGVLTKED-KTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILL 159
Cdd:TIGR02211 89 YQFHHLLPDFTALENVAM---PLLIGKKSVKEaKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1150389631 160 DEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYsDLIIALKEGKLV 215
Cdd:TIGR02211 166 DEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQLF 220
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
3-233 |
1.30e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 96.03 E-value: 1.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 3 EISHVFKSydDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSILRQ 82
Cdd:PRK13652 8 DLCYSYSG--SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 83 E-NTLTARITVEDLVSFGryPYSHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILLDE 161
Cdd:PRK13652 86 NpDDQIFSPTVEQDIAFG--PINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1150389631 162 PLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENV-MKDEILSAIY 233
Cdd:PRK13652 164 PTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIfLQPDLLARVH 236
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-227 |
1.68e-23 |
|
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: 94.99 E-value: 1.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSY--DDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSI 79
Cdd:cd03251 1 VEFKNVTFRYpgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 80 LRQENTL------------TARITVEDLVSFGRYPYSHGVLTKEDKTFvDNAISYLGLdpyrkrfldELSGGQRQRAFVA 147
Cdd:cd03251 81 VSQDVFLfndtvaeniaygRPGATREEVEEAARAANAHEFIMELPEGY-DTVIGERGV---------KLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 148 MVISQNTDYILLDEPLNNLDMRHAvsmmKRLRNAADEL--GKTIIMVMHDLNFAScYSDLIIALKEGKLVFSGAPENVMK 225
Cdd:cd03251 151 RALLKDPPILILDEATSALDTESE----RLVQAALERLmkNRTTFVIAHRLSTIE-NADRIVVLEDGKIVERGTHEELLA 225
|
..
gi 1150389631 226 DE 227
Cdd:cd03251 226 QG 227
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
9-233 |
1.70e-23 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 94.96 E-value: 1.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 9 KSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKR-LSILRQENTLT 87
Cdd:PRK10895 11 KAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgIGYLPQEASIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 88 ARITVEDLVsFGRYPYSHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILLDEPLNNLD 167
Cdd:PRK10895 91 RRLSVYDNL-MAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1150389631 168 MRHAVSMMKRLRNAADElGKTIIMVMHDL--NFASCYSDLIIAlkEGKLVFSGAPENVMKDEILSAIY 233
Cdd:PRK10895 170 PISVIDIKRIIEHLRDS-GLGVLITDHNVreTLAVCERAYIVS--QGHLIAHGTPTEILQDEHVKRVY 234
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-231 |
1.86e-23 |
|
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: 94.86 E-value: 1.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSY--DDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSI 79
Cdd:cd03252 1 ITFEHVRFRYkpDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 80 LRQENTLTARITVEDLVSFGRYPYSHGVLTKEDKTFVDNAISYL--GLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYI 157
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELpeGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1150389631 158 LLDEPLNNLDMRHAVSMMKRLRNAADelGKTIIMVMHDLNFASCySDLIIALKEGKLVFSGApenvmKDEILSA 231
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGS-----HDELLAE 226
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-197 |
3.10e-23 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 93.70 E-value: 3.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLP---ITKGRITVDGIDVTKakGADFAKRL 77
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGRRLTA--LPAEQRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 78 SILRQENTLTARITVEDLVSFGrypYSHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYI 157
Cdd:COG4136 79 GILFQDDLLFPHLSVGENLAFA---LPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1150389631 158 LLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLN 197
Cdd:COG4136 156 LLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEE 195
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
9-213 |
8.83e-23 |
|
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: 92.15 E-value: 8.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 9 KSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGidvtkakgadfakRLSILRQE----N 84
Cdd:cd03250 13 GEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------SIAYVSQEpwiqN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 85 TltariTVEDLVSFGrYPYshgvltkeDKTFVDNAISYLGLDPYRKRF--LDE---------LSGGQRQRAFVAMVISQN 153
Cdd:cd03250 80 G-----TIRENILFG-KPF--------DEERYEKVIKACALEPDLEILpdGDLteigekginLSGGQKQRISLARAVYSD 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 154 TDYILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFAScYSDLIIALKEGK 213
Cdd:cd03250 146 ADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQLLP-HADQIVVLDNGR 204
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
2-218 |
1.05e-22 |
|
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: 92.78 E-value: 1.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNS---------------------IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITV 60
Cdd:cd03267 1 IEVSNLSKSYRVYSkepgligslkslfkrkyreveALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 61 DGIDVTKAKGAdFAKRLS-ILRQENTLTARITVEDLVSFGRYPYshGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGG 139
Cdd:cd03267 81 AGLVPWKRRKK-FLRRIGvVFGQKTQLWWDLPVIDSFYLLAAIY--DLPPARFKKRLDELSELLDLEELLDTPVRQLSLG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 140 QRQRAFVAMVISQNTDYILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDL-NFASCYSDLIIaLKEGKLVFSG 218
Cdd:cd03267 158 QRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMkDIEALARRVLV-IDKGRLLYDG 236
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-223 |
1.39e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 93.23 E-value: 1.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNSIIEDL---SLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRL 77
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQLngvSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 78 SILRQ--ENTLTArITVEDLVSFGRYpySHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTD 155
Cdd:PRK13642 84 GMVFQnpDNQFVG-ATVEDDVAFGME--NQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1150389631 156 YILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCySDLIIALKEGKLVFSGAPENV 223
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSEL 227
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-224 |
2.16e-22 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 92.56 E-value: 2.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDG--IDVTKAKG-----ADF 73
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGeeIRLKPDRDgelvpADR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 74 AK------RLSILRQENTLTARITVEDLVSFGryPYsHgVLTKEDKTFVDNAISYL---GLDPYRKRFLDELSGGQRQRA 144
Cdd:COG4598 88 RQlqrirtRLGMVFQSFNLWSHMTVLENVIEA--PV-H-VLGRPKAEAIERAEALLakvGLADKRDAYPAHLSGGQQQRA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 145 FVAMVISQNTDYILLDEPLNNLDMRHAVSMMKRLRNAADElGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVM 224
Cdd:COG4598 164 AIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVF 242
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-227 |
3.46e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 91.72 E-value: 3.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAkRLSIL 80
Cdd:COG4674 10 ILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIA-RLGIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 81 R--QENTLTARITVED--LVSFGRYpysHGV-------LTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMV 149
Cdd:COG4674 89 RkfQKPTVFEELTVFEnlELALKGD---RGVfaslfarLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGML 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 150 ISQNTDYILLDEPlnnldmrhAVSMMKRLRNAADEL------GKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENV 223
Cdd:COG4674 166 LAQDPKLLLLDEP--------VAGMTDAETERTAELlkslagKHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGSLDEV 237
|
....
gi 1150389631 224 MKDE 227
Cdd:COG4674 238 QADP 241
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-194 |
5.32e-22 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 92.94 E-value: 5.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYD--DNSII--EDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADfakr 76
Cdd:PRK11153 1 MIELKNISKVFPqgGRTIHalNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKE---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 77 LSILRQE--------NTLTARiTVEDLVSFgryPYShgvLTKEDKTFVDNAISYL----GLDPYRKRFLDELSGGQRQRA 144
Cdd:PRK11153 77 LRKARRQigmifqhfNLLSSR-TVFDNVAL---PLE---LAGTPKAEIKARVTELlelvGLSDKADRYPAQLSGGQKQRV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1150389631 145 FVAMVISQNTDYILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMH 194
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITH 199
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-226 |
6.24e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 91.73 E-value: 6.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 19 DLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVT-KAKGADFA---KRLSILRQ--ENTLTARITV 92
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITsTSKNKDIKqirKKVGLVFQfpESQLFEETVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 93 EDlVSFGryPYSHGVLTKEDKTFVDNAISYLGLDP-YRKRFLDELSGGQRQRAFVAMVISQNTDYILLDEPLNNLD---M 168
Cdd:PRK13649 105 KD-VAFG--PQNFGVSQEEAEALAREKLALVGISEsLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDpkgR 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1150389631 169 RHAVSMMKRLRnaadELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMKD 226
Cdd:PRK13649 182 KELMTLFKKLH----QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-195 |
8.74e-22 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 93.64 E-value: 8.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVdGIDVtkakgadfakRLSILR 81
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV----------KLAYVD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 82 QE-NTLTARITVEDLVSFGrypysHGVLTKEDKTFvdNAISYLGldpyrkRF----------LDELSGGQRQRAFVAMVI 150
Cdd:PRK11819 394 QSrDALDPNKTVWEEISGG-----LDIIKVGNREI--PSRAYVG------RFnfkggdqqkkVGVLSGGERNRLHLAKTL 460
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1150389631 151 SQNTDYILLDEPLNNLDmrhaVSMMKRLRNAADELGKTIIMVMHD 195
Cdd:PRK11819 461 KQGGNVLLLDEPTNDLD----VETLRALEEALLEFPGCAVVISHD 501
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-225 |
1.43e-21 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 89.76 E-value: 1.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSY----------------------DDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRI 58
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 59 TVDG-----IDVtkakGADFAKRLSiLRqENT-LTARItvedlvsfgrypysHGVLTKEDKTFVDNAISYLGLdpyrKRF 132
Cdd:COG1134 84 EVNGrvsalLEL----GAGFHPELT-GR-ENIyLNGRL--------------LGLSRKEIDEKFDEIVEFAEL----GDF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 133 LDE----LSGGQRQR-AFvAMVISQNTDYILLDEPLnnldmrhAV---SMMKRLRNAADEL---GKTIIMVMHDLNFASC 201
Cdd:COG1134 140 IDQpvktYSSGMRARlAF-AVATAVDPDILLVDEVL-------AVgdaAFQKKCLARIRELresGRTVIFVSHSMGAVRR 211
|
250 260
....*....|....*....|....
gi 1150389631 202 YSDLIIALKEGKLVFSGAPENVMK 225
Cdd:COG1134 212 LCDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
9-218 |
2.45e-21 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 88.74 E-value: 2.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 9 KSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDG-----IDVtkakGADFAKRLSILrqE 83
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGrvsslLGL----GGGFNPELTGR--E 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 84 NT-LTARItvedlvsfgrypysHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQR-AFvAMVISQNTDYILLDE 161
Cdd:cd03220 104 NIyLNGRL--------------LGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARlAF-AIATALEPDILLIDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1150389631 162 PLNNLDMRHAVSMMKRLRNaADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSG 218
Cdd:cd03220 169 VLAVGDAAFQEKCQRRLRE-LLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-225 |
4.95e-21 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 88.37 E-value: 4.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYD---DNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLS 78
Cdd:cd03249 1 IEFKNVSFRYPsrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 79 ILRQENTLTArITVEDLVSFGRYPYShgVLTKEDKTFVDNAISYLGLDPYRkrfLD--------ELSGGQRQRAFVAMVI 150
Cdd:cd03249 81 LVSQEPVLFD-GTIAENIRYGKPDAT--DEEVEEAAKKANIHDFIMSLPDG---YDtlvgergsQLSGGQKQRIAIARAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1150389631 151 SQNTDYILLDEPLNNLDmrhAVSmMKRLRNAADEL--GKTIIMVMHDLNFAScYSDLIIALKEGKLVFSGAPENVMK 225
Cdd:cd03249 155 LRNPKILLLDEATSALD---AES-EKLVQEALDRAmkGRTTIVIAHRLSTIR-NADLIAVLQNGQVVEQGTHDELMA 226
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-223 |
5.73e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 88.57 E-value: 5.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVD------GIDVTKAKGADFA 74
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDgkvlyfGKDIFQIDAIKLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 75 KRLSILRQENTLTARITVEDLVSfgrYPY-SHGVLTK-EDKTFVDNAISYLGLDPYRKRFLD----ELSGGQRQRAFVAM 148
Cdd:PRK14246 90 KEVGMVFQQPNPFPHLSIYDNIA---YPLkSHGIKEKrEIKKIVEECLRKVGLWKEVYDRLNspasQLSGGQQQRLTIAR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1150389631 149 VISQNTDYILLDEPLNNLDMRHAVSMMKRLRNAADELgkTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENV 223
Cdd:PRK14246 167 ALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-218 |
5.91e-21 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 88.27 E-value: 5.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRL-SI 79
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQKGLiRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 80 LRQE--------NTLTARITVEDLVSfgrypySHGVLTKEDKtfvDNAISY-------LGL----DPYRKRfldeLSGGQ 140
Cdd:PRK11264 83 LRQHvgfvfqnfNLFPHRTVLENIIE------GPVIVKGEPK---EEATARarellakVGLagkeTSYPRR----LSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1150389631 141 RQRAFVAMVISQNTDYILLDEPLNNLDMRHAVSMMKRLRNAADElGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSG 218
Cdd:PRK11264 150 QQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-195 |
7.22e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.89 E-value: 7.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 4 ISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISrllpitkGRITVDGIDVTKAKGAdfakRLSILRQE 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILA-------GELEPDSGEVSIPKGL----RIGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 84 NTLTARITVEDLVSFGRYPYS------HGVLTKEDKTFVD--------------NAISY----------LGL---DPYRK 130
Cdd:COG0488 70 PPLDDDLTVLDTVLDGDAELRaleaelEELEAKLAEPDEDlerlaelqeefealGGWEAearaeeilsgLGFpeeDLDRP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1150389631 131 rfLDELSGGQRQRAFVAMVISQNTDYILLDEPLNNLDMrHAV----SMMKRLRNaadelgkTIIMVMHD 195
Cdd:COG0488 150 --VSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL-ESIewleEFLKNYPG-------TVLVVSHD 208
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-215 |
9.78e-21 |
|
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: 85.56 E-value: 9.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADfAKRLSIlr 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD-ARRAGI-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 82 qentltaritvedlvsfgrypyshgvltkedktfvdnAISYlgldpyrkrfldELSGGQRQRAFVAMVISQNTDYILLDE 161
Cdd:cd03216 78 -------------------------------------AMVY------------QLSVGERQMVEIARALARNARLLILDE 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1150389631 162 PLNNLDMRHAVSMMKRLRNAADElGKTIIMVMHDLNFASCYSDLIIALKEGKLV 215
Cdd:cd03216 109 PTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
2-231 |
1.67e-20 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 90.19 E-value: 1.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNS--IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSI 79
Cdd:TIGR01846 456 ITFENIRFRYAPDSpeVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGV 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 80 LRQENTLTARITVEDL------VSFGRYPYSHGVLTKEDktFVdnaisyLGLDPYRKRFLDE----LSGGQRQRAFVAMV 149
Cdd:TIGR01846 536 VLQENVLFSRSIRDNIalcnpgAPFEHVIHAAKLAGAHD--FI------SELPQGYNTEVGEkganLSGGQRQRIAIARA 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 150 ISQNTDYILLDEPLNNLDMRHAVSMMKRLRNAADelGKTIIMVMHDLNfASCYSDLIIALKEGKLVFSGAPENVMKDEIL 229
Cdd:TIGR01846 608 LVGNPRILIFDEATSALDYESEALIMRNMREICR--GRTVIIIAHRLS-TVRACDRIIVLEKGQIAESGRHEELLALQGL 684
|
..
gi 1150389631 230 SA 231
Cdd:TIGR01846 685 YA 686
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
19-232 |
2.24e-20 |
|
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: 88.62 E-value: 2.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 19 DLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDG---------IDVTKAKgadfaKRLSILRQENTLTAR 89
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlqdsargIFLPPHR-----RRIGYVFQEARLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 90 ITVEDLVSFGRypysHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRafVAM---VISQnTDYILLDEPLNNL 166
Cdd:COG4148 92 LSVRGNLLYGR----KRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQR--VAIgraLLSS-PRLLLMDEPLAAL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1150389631 167 DMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMKDEILSAI 232
Cdd:COG4148 165 DLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPL 230
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
17-226 |
2.90e-20 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 89.48 E-value: 2.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 17 IEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITV----DGIDVTKaKGADF---AKR-LSILRQENTL-- 86
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTK-PGPDGrgrAKRyIGILHQEYDLyp 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 87 --------TARITVEDLVSFGRypySHGVLTKEDKTFVDN-AISYLgldpyrKRFLDELSGGQRQRAFVAMVISQNTDYI 157
Cdd:TIGR03269 379 hrtvldnlTEAIGLELPDELAR---MKAVITLKMVGFDEEkAEEIL------DKYPDELSEGERHRVALAQVLIKEPRIV 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1150389631 158 LLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMKD 226
Cdd:TIGR03269 450 ILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-223 |
2.93e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 86.98 E-value: 2.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGidvtkaKGADFAKR-LSI 79
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQG------KPLDYSKRgLLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 80 LRQENTLT-----ARITVEDLVSFGRYPYSH-GVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQN 153
Cdd:PRK13638 75 LRQQVATVfqdpeQQIFYTDIDSDIAFSLRNlGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 154 TDYILLDEPLNNLDMRHAVSMMKRLRNAADElGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENV 223
Cdd:PRK13638 155 ARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV 223
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-221 |
3.36e-20 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 86.74 E-value: 3.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDV---TKAKGADFAKRL 77
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamSRSRLYTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 78 SILRQENTLTARITVEDLVSfgrYPY-SHGVLTKED-KTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTD 155
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVA---YPLrEHTQLPAPLlHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1150389631 156 YILLDEPLNNLD---MRHAVSMMKRLRNAadeLGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPE 221
Cdd:PRK11831 164 LIMFDEPFVGQDpitMGVLVKLISELNSA---LGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQ 229
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-162 |
6.74e-20 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 85.08 E-value: 6.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKA---KGAdfakRL 77
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLpmhKRA----RL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 78 SI--LRQENTLTARITVED-------LVSFGRypyshgvltKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAM 148
Cdd:COG1137 79 GIgyLPQEASIFRKLTVEDnilavleLRKLSK---------KEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIAR 149
|
170
....*....|....
gi 1150389631 149 VISQNTDYILLDEP 162
Cdd:COG1137 150 ALATNPKFILLDEP 163
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
10-227 |
7.07e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 88.36 E-value: 7.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 10 SYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPItKGRITVDGIDVTKAKGADFAKRLSILRQENTLTAR 89
Cdd:PRK11174 359 SPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIELRELDPESWRKHLSWVGQNPQLPHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 90 iTVEDLVSFGRYPYSHGVLTKE-DKTFVDNAISYL--GLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILLDEPLNNL 166
Cdd:PRK11174 438 -TLRDNVLLGNPDASDEQLQQAlENAWVSEFLPLLpqGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASL 516
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1150389631 167 DMRHAVSMMKRLRNAAdeLGKTIIMVMHDLNFASCYsDLIIALKEGKLVFSGAPENVMKDE 227
Cdd:PRK11174 517 DAHSEQLVMQALNAAS--RRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
17-232 |
8.90e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 85.83 E-value: 8.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 17 IEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLpITKGRITVDGiDVTKAKGADFAKRLSILRQENTLTARI------ 90
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLI-ISETGQTIVG-DYAIPANLKKIKEVKRLRKEIGLVFQFpeyqlf 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 91 --TVEDLVSFGryPYSHGVLTKEDKTFVDNAISYLGL-DPYRKRFLDELSGGQRQRAFVAMVISQNTDYILLDEPLNNLD 167
Cdd:PRK13645 105 qeTIEKDIAFG--PVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1150389631 168 MRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMKD-EILSAI 232
Cdd:PRK13645 183 PKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNqELLTKI 248
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-227 |
1.30e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 87.47 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSY---DDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLS 78
Cdd:TIGR00958 479 IEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 79 ILRQENTLTARiTVEDLVSFG-RYPYSHGVLTKEDKTFVDNAISYL--GLDPYRKRFLDELSGGQRQRAFVAMVISQNTD 155
Cdd:TIGR00958 559 LVGQEPVLFSG-SVRENIAYGlTDTPDEEIMAAAKAANAHDFIMEFpnGYDTEVGEKGSQLSGGQKQRIAIARALVRKPR 637
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1150389631 156 YILLDEPLNNLDMRhAVSMMKRLRNAADelgKTIIMVMHDLNFAScYSDLIIALKEGKLVFSGAPENVMKDE 227
Cdd:TIGR00958 638 VLILDEATSALDAE-CEQLLQESRSRAS---RTVLLIAHRLSTVE-RADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-224 |
1.39e-19 |
|
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: 87.46 E-value: 1.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSY--DDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSI 79
Cdd:TIGR02203 331 VEFRNVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 80 LRQE-----NTLTARITVEDLVSFGRYPYSHGVLTKEDKTFVDNaiSYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNT 154
Cdd:TIGR02203 411 VSQDvvlfnDTIANNIAYGRTEQADRAEIERALAAAYAQDFVDK--LPLGLDTPIGENGVLLSGGQRQRLAIARALLKDA 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1150389631 155 DYILLDEPLNNLDmrhavSMMKRLRNAA-DEL--GKTIIMVMHDLNFAScYSDLIIALKEGKLVFSGAPENVM 224
Cdd:TIGR02203 489 PILILDEATSALD-----NESERLVQAAlERLmqGRTTLVIAHRLSTIE-KADRIVVMDDGRIVERGTHNELL 555
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-240 |
2.93e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 86.38 E-value: 2.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKR-LSI 79
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 80 LRQENTLTARITVEDLVSFGRYPyshgvlTKedKTFVDNAISY-------------LGLDPYRKRFLDELSGGQRQRAFV 146
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIGRHL------TK--KVCGVNIIDWremrvraammllrVGLKVDLDEKVANLSISHKQMLEI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 147 AMVISQNTDYILLDEP---LNNLDMRHAVSMMKRLRNAadelGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENV 223
Cdd:PRK09700 157 AKTLMLDAKVIIMDEPtssLTNKEVDYLFLIMNQLRKE----GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
250
....*....|....*..
gi 1150389631 224 MKDEILSAIYDIDIKVK 240
Cdd:PRK09700 233 SNDDIVRLMVGRELQNR 249
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-226 |
3.59e-19 |
|
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: 86.28 E-value: 3.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 19 DLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPiTKGRITVDGIDVTKAKGADFA---KRLSILRQE--NTLTARITVE 93
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRALRplrRRMQVVFQDpfGSLSPRMTVG 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 94 DLVSFGRypYSHGV-LTKEDKT-FVDNAISYLGLDP-YRKRFLDELSGGQRQRAFVA--MVIsqNTDYILLDEPLNNLDM 168
Cdd:COG4172 383 QIIAEGL--RVHGPgLSAAERRaRVAEALEEVGLDPaARHRYPHEFSGGQRQRIAIAraLIL--EPKLLVLDEPTSALDV 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1150389631 169 RHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMKD 226
Cdd:COG4172 459 SVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-227 |
6.62e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 84.13 E-value: 6.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNS-----IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGI------------ 63
Cdd:PRK13631 21 ILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIyigdkknnheli 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 64 -DVTKAKGADFA---KRLSILRQ--ENTLTaRITVEDLVSFGryPYSHGVLTKEDKTFVDNAISYLGLD-PYRKRFLDEL 136
Cdd:PRK13631 101 tNPYSKKIKNFKelrRRVSMVFQfpEYQLF-KDTIEKDIMFG--PVALGVKKSEAKKLAKFYLNKMGLDdSYLERSPFGL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 137 SGGQRQRAFVAMVISQNTDYILLDEPLNNLDMRHAVSMMKRLRNAADElGKTIIMVMHDLNFASCYSDLIIALKEGKLVF 216
Cdd:PRK13631 178 SGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKILK 256
|
250
....*....|.
gi 1150389631 217 SGAPENVMKDE 227
Cdd:PRK13631 257 TGTPYEIFTDQ 267
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-215 |
9.86e-19 |
|
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: 82.10 E-value: 9.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNS----IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTK----AKGAD 72
Cdd:COG4181 8 IIELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAldedARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 73 FAKRLSILRQE----NTLTARITV----EdlvsfgrypyshgvLTKEDKTFvDNAISYLG-------LDPYRKrfldELS 137
Cdd:COG4181 88 RARHVGFVFQSfqllPTLTALENVmlplE--------------LAGRRDAR-ARARALLErvglghrLDHYPA----QLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 138 GGQRQ-----RAFVAmvisqNTDYILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFAS-CysDLIIALKE 211
Cdd:COG4181 149 GGEQQrvalaRAFAT-----EPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAArC--DRVLRLRA 221
|
....
gi 1150389631 212 GKLV 215
Cdd:COG4181 222 GRLV 225
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-220 |
1.16e-18 |
|
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: 81.39 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNS--IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSI 79
Cdd:cd03244 3 IEFKNVSLRYRPNLppVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 80 LRQENTL---TARitvEDLVSFGRYPYS--HGVLtkED---KTFVDNAISYLGLDpyrkrfLDE----LSGGQRQRAFVA 147
Cdd:cd03244 83 IPQDPVLfsgTIR---SNLDPFGEYSDEelWQAL--ERvglKEFVESLPGGLDTV------VEEggenLSVGQRQLLCLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1150389631 148 MVISQNTDYILLDEPLNNLDMRHAVSMMKRLRNA-ADelgKTIIMVMHDLNfASCYSDLIIALKEGKLVFSGAP 220
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPETDALIQKTIREAfKD---CTVLTIAHRLD-TIIDSDRILVLDKGRVVEFDSP 221
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-226 |
1.20e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 82.20 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPIT-----KGRITVDGIDV--TKAKGADFA 74
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIysPDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 75 KRLSILRQENTLTARITVEDLVSFGrYPYSHGVLTKED-KTFVDNAISYLGL-DPYRKRFLD---ELSGGQRQRAFVAMV 149
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIG-VKLNGLVKSKKElDERVEWALKKAALwDEVKDRLNDypsNLSGGQRQRLVIARA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1150389631 150 ISQNTDYILLDEPLNNLDMRHAVSMMKRLRNAADELgkTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMKD 226
Cdd:PRK14267 164 LAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFEN 238
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-218 |
3.39e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 83.34 E-value: 3.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDN--SIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTkakgaDFAkrlsi 79
Cdd:PRK11160 339 LTLNNVSFTYPDQpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIA-----DYS----- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 80 lrqENTLTARITVedlVSFGRYPYSHG-----VLTKEDKTfvDNAI---------SYL-----GLDPYrkrfLDE----L 136
Cdd:PRK11160 409 ---EAALRQAISV---VSQRVHLFSATlrdnlLLAAPNAS--DEALievlqqvglEKLleddkGLNAW----LGEggrqL 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 137 SGGQRQRAFVAMVISQNTDYILLDEPLNNLDMRHAVSMMKRLRNAADelGKTIIMVMHDLNfASCYSDLIIALKEGKLVF 216
Cdd:PRK11160 477 SGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLT-GLEQFDRICVMDNGQIIE 553
|
..
gi 1150389631 217 SG 218
Cdd:PRK11160 554 QG 555
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
24-220 |
3.41e-18 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 80.92 E-value: 3.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 24 IPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVtkakgadfakrlSILRQENTLTARITVEDLVS-----F 98
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV------------SYKPQYIKADYEGTVRDLLSsitkdF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 99 GRYPYshgvltkedktFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILLDEPLNNLDMRHAVSMMKRL 178
Cdd:cd03237 90 YTHPY-----------FKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVI 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1150389631 179 RNAADELGKTIIMVMHDLNFASCYSDLIIalkegklVFSGAP 220
Cdd:cd03237 159 RRFAENNEKTAFVVEHDIIMIDYLADRLI-------VFEGEP 193
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-194 |
5.20e-18 |
|
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: 78.35 E-value: 5.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHV-FKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRItvdgidvtkakgadfakrlSIL 80
Cdd:cd03223 1 IELENLsLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-------------------GMP 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 81 RQENTLtaritvedLVSfgRYPY-SHGVLtKEdktfvdnAISYlgldPYRkrflDELSGGQRQR-AFvAMVISQNTDYIL 158
Cdd:cd03223 62 EGEDLL--------FLP--QRPYlPLGTL-RE-------QLIY----PWD----DVLSGGEQQRlAF-ARLLLHKPKFVF 114
|
170 180 190
....*....|....*....|....*....|....*.
gi 1150389631 159 LDEPLNNLDmrhaVSMMKRLRNAADELGKTIIMVMH 194
Cdd:cd03223 115 LDEATSALD----EESEDRLYQLLKELGITVISVGH 146
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
15-222 |
9.60e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 82.02 E-value: 9.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 15 SIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMIS-RLLPITK--GRITVDGIDVTKAKgadFAKRLSILRQEN----TLT 87
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAfRSPKGVKgsGSVLLNGMPIDAKE---MRAISAYVQQDDlfipTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 88 ARitvEDLVSFGRYPYSHGVLTKEDKTFVDNAISYLGL---------DPYRKRfldELSGGQRQR-AFVAMVIsqnTDYI 157
Cdd:TIGR00955 116 VR---EHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLrkcantrigVPGRVK---GLSGGERKRlAFASELL---TDPP 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1150389631 158 LL--DEPLNNLDMRHAVSMMKRLRNAADElGKTIIMVMH----DL--NFascysDLIIALKEGKLVFSGAPEN 222
Cdd:TIGR00955 187 LLfcDEPTSGLDSFMAYSVVQVLKGLAQK-GKTIICTIHqpssELfeLF-----DKIILMAEGRVAYLGSPDQ 253
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-223 |
9.70e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 79.57 E-value: 9.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLL-----PITKGRITVDGIDVTKAKGADFAKR 76
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIFKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 77 LSILRQENTLTARITVEDLVSFGRYPYSHGVLTKEDKTFVDNAISYLGLDPYRKRFLD----ELSGGQRQRAFVAMVISQ 152
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALGLKLNRLVKSKKELQERVRWALEKAQLWDEVKDRLDapagKLSGGQQQRLCIARALAF 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1150389631 153 NTDYILLDEPLNNLDMRHAVsmmkRLRNAADELGK--TIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENV 223
Cdd:PRK14247 164 QPEVLLADEPTANLDPENTA----KIESLFLELKKdmTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
16-201 |
1.22e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 78.38 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 16 IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTkakGADFAKRLSILRQENTLTARITVEDL 95
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID---DPDVAEACHYLGHRNAMKPALTVAEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 96 VSFGRypyshGVLTKEDkTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILLDEPLNNLDmRHAVSMM 175
Cdd:PRK13539 94 LEFWA-----AFLGGEE-LDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD-AAAVALF 166
|
170 180
....*....|....*....|....*..
gi 1150389631 176 KRLRNAADELGKTIIMVMH-DLNFASC 201
Cdd:PRK13539 167 AELIRAHLAQGGIVIAATHiPLGLPGA 193
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-221 |
1.32e-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: 78.34 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRlLP---ITKGRITVDGIDVTKAKGADFAkRLS 78
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPkyeVTEGEILFKGEDITDLPPEERA-RLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 79 IlrqentltaritvedLVSFGRYPYSHGVLTKEdktfvdnaisYLgldpyrkRFLDE-LSGGQRQRAFVAMVISQNTDYI 157
Cdd:cd03217 79 I---------------FLAFQYPPEIPGVKNAD----------FL-------RYVNEgFSGGEKKRNEILQLLLLEPDLA 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1150389631 158 LLDEPLNNLDMrHAVSMMKRLRNAADELGKTIIMVMHD---LNFAScySDLIIALKEGKLVFSGAPE 221
Cdd:cd03217 127 ILDEPDSGLDI-DALRLVAEVINKLREEGKSVLIITHYqrlLDYIK--PDRVHVLYDGRIVKSGDKE 190
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-232 |
1.40e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 81.22 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADfAKRL--S 78
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRD-AQAAgiA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 79 ILRQENTLTARITVEDLVSFGRYPYSHGVL--------TKEdktfvdnAISYLGL--DPYRKrfLDELSGGQRQrafvaM 148
Cdd:COG1129 83 IIHQELNLVPNLSVAENIFLGREPRRGGLIdwramrrrARE-------LLARLGLdiDPDTP--VGDLSVAQQQ-----L 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 149 V-----ISQNTDYILLDEP---LNNLDMRHAVSMMKRLRnaadELGKTIIMVMHDLN--FASCysDLIIALKEGKLVFSG 218
Cdd:COG1129 149 VeiaraLSRDARVLILDEPtasLTEREVERLFRIIRRLK----AQGVAIIYISHRLDevFEIA--DRVTVLRDGRLVGTG 222
|
250
....*....|....
gi 1150389631 219 APENVMKDEILSAI 232
Cdd:COG1129 223 PVAELTEDELVRLM 236
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
13-214 |
1.46e-17 |
|
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: 78.67 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 13 DNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSILRQENTLTARiTV 92
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVLFAR-SL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 93 EDLVSFGRYPYSHGVLTK-EDKTFVDNAISYLGLDPYRKrfLDE----LSGGQRQRAFVAMVISQNTDYILLDEPLNNLD 167
Cdd:cd03248 105 QDNIAYGLQSCSFECVKEaAQKAHAHSFISELASGYDTE--VGEkgsqLSGGQKQRVAIARALIRNPQVLILDEATSALD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1150389631 168 MRHAVSMMKRLRNAADElgKTIIMVMHDLNFAScYSDLIIALKEGKL 214
Cdd:cd03248 183 AESEQQVQQALYDWPER--RTVLVIAHRLSTVE-RADQILVLDGGRI 226
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-218 |
1.51e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 80.13 E-value: 1.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 17 IEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKgADFAKRLS-ILRQENTLTARITVEDl 95
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRR-KEFARRIGvVFGQRSQLWWDLPAID- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 96 vSFGRYPYSHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILLDEPLNNLDmrhaVSMM 175
Cdd:COG4586 116 -SFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLD----VVSK 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1150389631 176 KRLRNAADEL----GKTIIMVMHDLN--FASCysDLIIALKEGKLVFSG 218
Cdd:COG4586 191 EAIREFLKEYnrerGTTILLTSHDMDdiEALC--DRVIVIDHGRIIYDG 237
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
16-232 |
1.53e-17 |
|
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: 81.24 E-value: 1.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 16 IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSILRQENTLTARITVEDL 95
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 96 VSFGRYPYSHGVLTKEDKTFVDNAISYL--GLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILLDEPLNNLDMRHAVS 173
Cdd:TIGR01842 413 ARFGENADPEKIIEAAKLAGVHELILRLpdGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQA 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1150389631 174 MMKRLRnAADELGKTIIMVMHDLNFASCySDLIIALKEGKLVFSGApenvmKDEILSAI 232
Cdd:TIGR01842 493 LANAIK-ALKARGITVVVITHRPSLLGC-VDKILVLQDGRIARFGE-----RDEVLAKL 544
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
17-220 |
3.55e-17 |
|
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: 80.83 E-value: 3.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 17 IEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGAdFAKRLSILRQENTLTARITVEDLV 96
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDA-VRQSLGMCPQHNILFHHLTVAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 97 SFgrYPYSHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILLDEPLNNLD---MRHAVS 173
Cdd:TIGR01257 1025 LF--YAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDpysRRSIWD 1102
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1150389631 174 MMKRLRNaadelGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAP 220
Cdd:TIGR01257 1103 LLLKYRS-----GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-215 |
3.68e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 80.54 E-value: 3.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSY----DDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKr 76
Cdd:PRK10535 4 LLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQ- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 77 lsiLRQEN------------TLTARITVEDLVSFGrypyshGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRA 144
Cdd:PRK10535 83 ---LRREHfgfifqryhllsHLTAAQNVEVPAVYA------GLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1150389631 145 FVAMVISQNTDYILLDEPLNNLDMRHAVSMMKRLRNAADElGKTIIMVMHDLNFAScYSDLIIALKEGKLV 215
Cdd:PRK10535 154 SIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVAA-QAERVIEIRDGEIV 222
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
4-224 |
3.98e-17 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 80.31 E-value: 3.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 4 ISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPIT--KGRITVDGIDVTKakgaDFAKRLSILR 81
Cdd:PLN03211 71 ISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTK----QILKRTGFVT 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 82 QENTLTARITVED---LVSFGRYPYShgvLTKEDKTFV-DNAISYLGLDPYRK-----RFLDELSGGQRQRAFVAMVISQ 152
Cdd:PLN03211 147 QDDILYPHLTVREtlvFCSLLRLPKS---LTKQEKILVaESVISELGLTKCENtiignSFIRGISGGERKRVSIAHEMLI 223
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1150389631 153 NTDYILLDEPLNNLDMRHAVSMMKRLRNAADElGKTIIMVMHDLNfASCYS--DLIIALKEGKLVFSGAPENVM 224
Cdd:PLN03211 224 NPSLLILDEPTSGLDATAAYRLVLTLGSLAQK-GKTIVTSMHQPS-SRVYQmfDSVLVLSEGRCLFFGKGSDAM 295
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-218 |
5.95e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 79.62 E-value: 5.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNS-IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSIL 80
Cdd:PRK13657 335 VEFDDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 81 RQENTLTARiTVEDLVSFGRYPYSHGVLTKEDKT-----FVDNAISylGLDPY---RKRfldELSGGQRQRAFVAMVISQ 152
Cdd:PRK13657 415 FQDAGLFNR-SIEDNIRVGRPDATDEEMRAAAERaqahdFIERKPD--GYDTVvgeRGR---QLSGGERQRLAIARALLK 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1150389631 153 NTDYILLDEPLNNLDmrhaVSMMKRLRNAADEL--GKTIIMVMHDLNFAScYSDLIIALKEGKLVFSG 218
Cdd:PRK13657 489 DPPILILDEATSALD----VETEAKVKAALDELmkGRTTFIIAHRLSTVR-NADRILVFDNGRVVESG 551
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-215 |
6.51e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 76.84 E-value: 6.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSY-DDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGAD--FAKR- 76
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpFLRRq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 77 LSILRQENTLTARITVEDLVSFgryPYSHGVLTKED-KTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTD 155
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAI---PLIIAGASGDDiRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 156 YILLDEPLNNLDMRHAVSMMkRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLV 215
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGIL-RLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-218 |
7.47e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 76.54 E-value: 7.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 16 IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVtkakgaDFAKRLSILRQentltaritvedl 95
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDN------QFGREASLIDA------------- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 96 vsfgrypyshgVLTKEDKTFVDNAISYLGL-DP--YRKRFlDELSGGQRQRAFVAMVISQNTDYILLDEPLNNLDMRHAV 172
Cdd:COG2401 106 -----------IGRKGDFKDAVELLNAVGLsDAvlWLRRF-KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAK 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1150389631 173 SMMKRLRNAADELGKTIImvmhdlnFASCYSDLIIALKEGKLVFSG 218
Cdd:COG2401 174 RVARNLQKLARRAGITLV-------VATHHYDVIDDLQPDLLIFVG 212
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-218 |
7.48e-17 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 79.40 E-value: 7.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNS-IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSIL 80
Cdd:TIGR01193 474 IVINDVSYSYGYGSnILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 81 RQENTLTARITVEDLVSFGRYPYSHGVLTK-----EDKTFVDNAisYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTD 155
Cdd:TIGR01193 554 PQEPYIFSGSILENLLLGAKENVSQDEIWAaceiaEIKDDIENM--PLGYQTELSEEGSSISGGQKQRIALARALLTDSK 631
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1150389631 156 YILLDEPLNNLDMRHAVSMMKRLRNAADelgKTIIMVMHDLNFAScYSDLIIALKEGKLVFSG 218
Cdd:TIGR01193 632 VLILDESTSNLDTITEKKIVNNLLNLQD---KTIIFVAHRLSVAK-QSDKIIVLDHGKIIEQG 690
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
19-215 |
1.19e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 78.80 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 19 DLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGAD-FAKRLSILRQENTLTARITVEDLVS 97
Cdd:PRK11288 22 DISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAaLAAGVAIIYQELHLVPEMTVAENLY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 98 FGRYPYSHGVLTKED-KTFVDNAISYLG--LDPYRKrfLDELSGGQRQRAFVAMVISQNTDYILLDEPLNNLDMRHAVSM 174
Cdd:PRK11288 102 LGQLPHKGGIVNRRLlNYEAREQLEHLGvdIDPDTP--LKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1150389631 175 MKRLRNAADElGKTIIMVMHDLN--FASCysDLIIALKEGKLV 215
Cdd:PRK11288 180 FRVIRELRAE-GRVILYVSHRMEeiFALC--DAITVFKDGRYV 219
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1-220 |
1.26e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 78.70 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNSIIEDlSLQIPKGGMVSIIGPNGAGKSTLLTMISrllpitkGRITVDGIDVtkakgaDFAKRLSIL 80
Cdd:PRK13409 340 LVEYPDLTKKLGDFSLEVE-GGEIYEGEVIGIVGPNGIGKTTFAKLLA-------GVLKPDEGEV------DPELKISYK 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 81 RQENTLTARITVEDLVSfgrypyshGVLTKEDKTFVDNAISY-LGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILL 159
Cdd:PRK13409 406 PQYIKPDYDGTVEDLLR--------SITDDLGSSYYKSEIIKpLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLL 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1150389631 160 DEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIalkegklVFSGAP 220
Cdd:PRK13409 478 DEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLM-------VFEGEP 531
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
16-225 |
1.28e-16 |
|
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: 78.64 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 16 IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSILRQENTLTArITVEDL 95
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFD-GTIAEN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 96 VS-FGRyPYSHGVLTKEDKTFVDNAIsyLGL-DPYRKRfLDE----LSGGQRQ-----RAFvamvisqntdY-----ILL 159
Cdd:COG4618 426 IArFGD-ADPEKVVAAAKLAGVHEMI--LRLpDGYDTR-IGEggarLSGGQRQriglaRAL----------YgdprlVVL 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1150389631 160 DEPLNNLDMRHAVSMMKRLRNAADElGKTIIMVMHDLNFASCySDLIIALKEGKLVFSGAPENVMK 225
Cdd:COG4618 492 DEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSLLAA-VDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-218 |
2.27e-16 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 75.82 E-value: 2.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADfAKRLSILR 81
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPS-EKAIRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 82 -------QENTLTARITV-EDLVSfgrYPYSHGVLTKEDKTF-VDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQ 152
Cdd:COG4161 82 qkvgmvfQQYNLWPHLTVmENLIE---APCKVLGLSKEQAREkAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1150389631 153 NTDYILLDEPLNNLD---MRHAVSMMKRLRnaadELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSG 218
Cdd:COG4161 159 EPQVLLFDEPTAALDpeiTAQVVEIIRELS----QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG 223
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
15-220 |
3.02e-16 |
|
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: 74.76 E-value: 3.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 15 SIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSILRQENTLTARITVED 94
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQDPTLFSGTIRSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 95 LVSFGRYpyshgvltKEDKTFVDNAISYLGLDpyrkrfldeLSGGQRQRAFVAMVISQNTDYILLDEPLNNLDMRHAVSM 174
Cdd:cd03369 102 LDPFDEY--------SDEEIYGALRVSEGGLN---------LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1150389631 175 MKRLRNAADelGKTIIMVMHDLNFASCYsDLIIALKEGKLVFSGAP 220
Cdd:cd03369 165 QKTIREEFT--NSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDHP 207
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-214 |
3.20e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 75.48 E-value: 3.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 4 ISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLtmisRLLPitkgritvdGIDVTKAkGADFAKR--LSILR 81
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLL----RLLA---------GLETPSA-GELLAGTapLAEAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 82 QENTLT---ARI----TVEDLVSFGrypyshgvLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNT 154
Cdd:PRK11247 81 EDTRLMfqdARLlpwkKVIDNVGLG--------LKGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 155 DYILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKL 214
Cdd:PRK11247 153 GLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-218 |
3.64e-16 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 75.05 E-value: 3.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISrLLPITK-GRITVDG--IDVTKAKGAdfaKRLS 78
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLN-LLEMPRsGTLNIAGnhFDFSKTPSD---KAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 79 ILR-------QENTLTARITV-EDLVsfgRYPYSHGVLTKED-KTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMV 149
Cdd:PRK11124 79 ELRrnvgmvfQQYNLWPHLTVqQNLI---EAPCRVLGLSKDQaLARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1150389631 150 ISQNTDYILLDEPLNNLD---MRHAVSMMKRLRnaadELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSG 218
Cdd:PRK11124 156 LMMEPQVLLFDEPTAALDpeiTAQIVSIIRELA----ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-220 |
5.27e-16 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 76.75 E-value: 5.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNSIIEDlSLQIPKGGMVSIIGPNGAGKSTLLTMISrllpitkGRITVDGIDVtkakgaDFAKRLSILR 81
Cdd:COG1245 342 VEYPDLTKSYGGFSLEVE-GGEIREGEVLGIVGPNGIGKTTFAKILA-------GVLKPDEGEV------DEDLKISYKP 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 82 QENTLTARITVEDLvsfgrypyshgvLTKEDKTFVDNAISY------LGLDPYRKRFLDELSGGQRQRAFVAMVISQNTD 155
Cdd:COG1245 408 QYISPDYDGTVEEF------------LRSANTDDFGSSYYKteiikpLGLEKLLDKNVKDLSGGELQRVAIAACLSRDAD 475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1150389631 156 YILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIalkegklVFSGAP 220
Cdd:COG1245 476 LYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLM-------VFEGEP 533
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
16-200 |
5.32e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 74.47 E-value: 5.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 16 IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTK----AKGADFAKRLSILRQENTLTARIT 91
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlssaAKAELRNQKLGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 92 VEDLVSFgryPYSHG-VLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILLDEPLNNLDMRH 170
Cdd:PRK11629 104 ALENVAM---PLLIGkKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN 180
|
170 180 190
....*....|....*....|....*....|
gi 1150389631 171 AVSMMKRLRNAADELGKTIIMVMHDLNFAS 200
Cdd:PRK11629 181 ADSIFQLLGELNRLQGTAFLVVTHDLQLAK 210
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-215 |
6.85e-16 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 74.69 E-value: 6.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISR---LLPITK--GRITVDGIDVtkakgadFAKR 76
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRmndLIPGARveGEILLDGEDI-------YDPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 77 LSIlrqeNTLTARI------------TVEDLVSFGryPYSHGVLTKEDktfVDNAI-SYLgldpyRKRFL-DE------- 135
Cdd:COG1117 85 VDV----VELRRRVgmvfqkpnpfpkSIYDNVAYG--LRLHGIKSKSE---LDEIVeESL-----RKAALwDEvkdrlkk 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 136 ----LSGGQRQRAFVAMVISQNTDYILLDEPLNNLDmrhAVSMMKrLRNAADELGK--TIIMVMHDLNFASCYSDLIIAL 209
Cdd:COG1117 151 salgLSGGQQQRLCIARALAVEPEVLLMDEPTSALD---PISTAK-IEELILELKKdyTIVIVTHNMQQAARVSDYTAFF 226
|
....*.
gi 1150389631 210 KEGKLV 215
Cdd:COG1117 227 YLGELV 232
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
12-197 |
7.53e-16 |
|
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: 73.68 E-value: 7.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 12 DDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGAdFAKRLSILRQENTLTARIT 91
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDS-IARGLLYLGHAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 92 VEDLVSFgrYPYSHGVLTKEDktfvdnAISYLGLDPYRKRFLDELSGGQRQRAFVA-MVISQNTDYIlLDEPLNNLDMRH 170
Cdd:cd03231 90 VLENLRF--WHADHSDEQVEE------ALARVGLNGFEDRPVAQLSAGQQRRVALArLLLSGRPLWI-LDEPTTALDKAG 160
|
170 180
....*....|....*....|....*..
gi 1150389631 171 AVSMMKRLRNAADELGKTIIMVMHDLN 197
Cdd:cd03231 161 VARFAEAMAGHCARGGMVVLTTHQDLG 187
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
15-212 |
7.63e-16 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 73.90 E-value: 7.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 15 SIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRI--TVDGIDVTKAKGADFAKRLSI-LRQENTLTARIT 91
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwSNKNESEPSFEATRSRNRYSVaYAAQKPWLLNAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 92 VEDLVSFGRyPYShgvltKEDKTFVDNAISY---LGLDPYR------KRFLDeLSGGQRQRAFVAMVISQNTDYILLDEP 162
Cdd:cd03290 95 VEENITFGS-PFN-----KQRYKAVTDACSLqpdIDLLPFGdqteigERGIN-LSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1150389631 163 LNNLDMRHAVSMMKR--LRNAADElGKTIIMVMHDLNFAScYSDLIIALKEG 212
Cdd:cd03290 168 FSALDIHLSDHLMQEgiLKFLQDD-KRTLVLVTHKLQYLP-HADWIIAMKDG 217
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-218 |
8.64e-16 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 76.08 E-value: 8.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRItvdgidvtkaKGAdfakrlsilr 81
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV----------KWS---------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 82 qENtltARItvedlvsfGRYPYSHGVLTKEDKTFVD------------NAI-SYLGldpyrkRFL---DE-------LSG 138
Cdd:PRK15064 380 -EN---ANI--------GYYAQDHAYDFENDLTLFDwmsqwrqegddeQAVrGTLG------RLLfsqDDikksvkvLSG 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 139 GQRQRAFVAMVISQNTDYILLDEPLNNLDMRHAVSmmkrLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLV-FS 217
Cdd:PRK15064 442 GEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIES----LNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVdFS 517
|
.
gi 1150389631 218 G 218
Cdd:PRK15064 518 G 518
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
22-206 |
1.00e-15 |
|
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: 74.33 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 22 LQIPKGGMV-SIIGPNGAGKSTLLTMISRLLPITKGRITV----DGIdVTKAKGADFAKRLSILRqENTLTARITVE--D 94
Cdd:cd03236 20 LPVPREGQVlGLVGPNGIGKSTALKILAGKLKPNLGKFDDppdwDEI-LDEFRGSELQNYFTKLL-EGDVKVIVKPQyvD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 95 LVSFGRYPYSHGVLTKEDKT-FVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILLDEPLNNLDMRHAVS 173
Cdd:cd03236 98 LIPKAVKGKVGELLKKKDERgKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLN 177
|
170 180 190
....*....|....*....|....*....|...
gi 1150389631 174 MMKRLRNAADElGKTIIMVMHDLNFASCYSDLI 206
Cdd:cd03236 178 AARLIRELAED-DNYVLVVEHDLAVLDYLSDYI 209
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
1-226 |
1.71e-15 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 73.71 E-value: 1.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITV---DGIDVTKAKGADfAKRL 77
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYimrSGAELELYQLSE-AERR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 78 SILR------QENTLTA-RITV-------EDLVSFGRYPYSHGVLTKEDktfvdnAISYLGLDPYRkrfLDEL----SGG 139
Cdd:TIGR02323 82 RLMRtewgfvHQNPRDGlRMRVsaganigERLMAIGARHYGNIRATAQD------WLEEVEIDPTR---IDDLprafSGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 140 QRQRAFVAMVISQNTDYILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGA 219
Cdd:TIGR02323 153 MQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGL 232
|
....*..
gi 1150389631 220 PENVMKD 226
Cdd:TIGR02323 233 TDQVLDD 239
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
16-227 |
2.94e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 75.01 E-value: 2.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 16 IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSILRQENTLtaritVEDL 95
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVL-----FSGT 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 96 VSFGRYPYSH----GVLTKEDKTFVDNAI--SYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILLDEPLNNLDMR 169
Cdd:PLN03232 1326 VRFNIDPFSEhndaDLWEALERAHIKDVIdrNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVR 1405
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1150389631 170 HAVSMMKRLRNAADELgkTIIMVMHDLN-FASCysDLIIALKEGKLVFSGAPENVMKDE 227
Cdd:PLN03232 1406 TDSLIQRTIREEFKSC--TMLVIAHRLNtIIDC--DKILVLSSGQVLEYDSPQELLSRD 1460
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
12-194 |
3.55e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 74.46 E-value: 3.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 12 DDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGidvtkakgadfAKRLSILRQEN-----TL 86
Cdd:COG4178 374 DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPA-----------GARVLFLPQRPylplgTL 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 87 TARITvedlvsfgrYPYSHGVLTKEDktfVDNAISYLGLDPYRKRfLDE-------LSGGQRQR-AFvAMVISQNTDYIL 158
Cdd:COG4178 443 REALL---------YPATAEAFSDAE---LREALEAVGLGHLAER-LDEeadwdqvLSLGEQQRlAF-ARLLLHKPDWLF 508
|
170 180 190
....*....|....*....|....*....|....*..
gi 1150389631 159 LDEPLNNLDMRHAVSMMKRLRnaaDEL-GKTIIMVMH 194
Cdd:COG4178 509 LDEATSALDEENEAALYQLLR---EELpGTTVISVGH 542
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
16-197 |
4.20e-15 |
|
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: 71.62 E-value: 4.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 16 IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGaDFAKRLSILRQENTLTARITVEDL 95
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD-EPHENILYLGHLPGLKPELSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 96 VSFgrypySHGVLTKEDKTfVDNAISYLGLDPYRKRFLDELSGGQRQR-AFVAMVISQNTDYIlLDEPLNNLDMRHAVSM 174
Cdd:TIGR01189 94 LHF-----WAAIHGGAQRT-IEDALAAVGLTGFEDLPAAQLSAGQQRRlALARLWLSRRPLWI-LDEPTTALDKAGVALL 166
|
170 180
....*....|....*....|...
gi 1150389631 175 MKRLRNAADELGKTIIMVMHDLN 197
Cdd:TIGR01189 167 AGLLRAHLARGGIVLLTTHQDLG 189
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
12-221 |
1.79e-14 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 70.48 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 12 DDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMIS--RLLPITKGRITVDGIDVTK-------AKG------------ 70
Cdd:COG0396 11 EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMghPKYEVTSGSILLDGEDILElspderaRAGiflafqypveip 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 71 ----ADFAKRLSILRQENTLTARitvedlvsfgrypyshgvltkEDKTFVDNAISYLGLDP-YRKRFLDE-LSGGQRQRA 144
Cdd:COG0396 91 gvsvSNFLRTALNARRGEELSAR---------------------EFLKLLKEKMKELGLDEdFLDRYVNEgFSGGEKKRN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 145 FVAMVISQNTDYILLDEPLNNLD---MRHAVSMMKRLRNAadelGKTIIMVMHD---LNFASCysDLIIALKEGKLVFSG 218
Cdd:COG0396 150 EILQMLLLEPKLAILDETDSGLDidaLRIVAEGVNKLRSP----DRGILIITHYqriLDYIKP--DFVHVLVDGRIVKSG 223
|
...
gi 1150389631 219 APE 221
Cdd:COG0396 224 GKE 226
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-215 |
2.38e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 70.49 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNS---------IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGA 71
Cdd:PRK10419 3 LLNVSGLSHHYAHGGlsgkhqhqtVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 72 D---FAKRLSILRQE--NTLTARITVEDLVsfgRYPYSHgvLTKEDKT----FVDNAISYLGLDP-YRKRFLDELSGGQR 141
Cdd:PRK10419 83 QrkaFRRDIQMVFQDsiSAVNPRKTVREII---REPLRH--LLSLDKAerlaRASEMLRAVDLDDsVLDKRPPQLSGGQL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1150389631 142 QRAFVAMVISQNTDYILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLV 215
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-233 |
3.04e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 69.91 E-value: 3.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKR-LSI 79
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREaVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 80 LRQENTLTARITVEDLVSFGRYpyshgvlTKEDKTFVDNAISYLGLDP----YRKRFLDELSGGQRQRAFVAMVISQNTD 155
Cdd:PRK11614 85 VPEGRRVFSRMTVEENLAMGGF-------FAERDQFQERIKWVYELFPrlheRRIQRAGTMSGGEQQMLAIGRALMSQPR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 156 YILLDEP---LNNLDMRHAVSMMKRLRnaadELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMKDEILSAI 232
Cdd:PRK11614 158 LLLLDEPslgLAPIIIQQIFDTIEQLR----EQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSA 233
|
.
gi 1150389631 233 Y 233
Cdd:PRK11614 234 Y 234
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
12-223 |
3.55e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 71.66 E-value: 3.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 12 DDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPiTKGRITVDGIDV---TKAKGADFAKRLSILRQE--NTL 86
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLhnlNRRQLLPVRHRIQVVFQDpnSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 87 TARITVEDLVSFGRYPYsHGVLTKEDKTF-VDNAISYLGLDP-YRKRFLDELSGGQRQRAFVAMVISQNTDYILLDEPLN 164
Cdd:PRK15134 376 NPRLNVLQIIEEGLRVH-QPTLSAAQREQqVIAVMEEVGLDPeTRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1150389631 165 NLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENV 223
Cdd:PRK15134 455 SLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERV 513
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-218 |
4.04e-14 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 71.20 E-value: 4.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYD--DNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSI 79
Cdd:PRK11176 342 IEFRNVTFTYPgkEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 80 LRQENTL-------------TARITVEDLVSFGRYPYSHGVLTKEDKTFvDNAISYLGLdpyrkrfldELSGGQRQRAFV 146
Cdd:PRK11176 422 VSQNVHLfndtianniayarTEQYSREQIEEAARMAYAMDFINKMDNGL-DTVIGENGV---------LLSGGQRQRIAI 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1150389631 147 AMVISQNTDYILLDEPLNNLDMRHAVSMMKrlrnAADELGK--TIIMVMHDLNFAScYSDLIIALKEGKLVFSG 218
Cdd:PRK11176 492 ARALLRDSPILILDEATSALDTESERAIQA----ALDELQKnrTSLVIAHRLSTIE-KADEILVVEDGEIVERG 560
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-223 |
4.94e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 69.74 E-value: 4.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 15 SIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKG-----RITVDGIDVTKAKGA-DFAKRLSILRQENTLTA 88
Cdd:PRK14271 35 TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVlEFRRRVGMLFQRPNPFP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 89 RITVEDLVSFGRypySHGVLTKEDKTFVDNA-ISYLGL-DPYRKRFLD---ELSGGQRQRAFVAMVISQNTDYILLDEPL 163
Cdd:PRK14271 115 MSIMDNVLAGVR---AHKLVPRKEFRGVAQArLTEVGLwDAVKDRLSDspfRLSGGQQQLLCLARTLAVNPEVLLLDEPT 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 164 NNLDMRHAVSMMKRLRNAADELgkTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENV 223
Cdd:PRK14271 192 SALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
16-218 |
5.21e-14 |
|
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: 68.42 E-value: 5.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 16 IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMIS--RLLPITKGRITVDGidvtKAKGADFAKRLSILRQENTLTARITVE 93
Cdd:cd03232 22 LLNNISGYVKPGTLTALMGESGAGKTTLLDVLAgrKTAGVITGEILING----RPLDKNFQRSTGYVEQQDVHSPNLTVR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 94 DLVSFGRYpyshgvltkedktfvdnaisylgldpyrkrfLDELSGGQRQRAFVAMVISQNTDYILLDEPLNNLDMRHAVS 173
Cdd:cd03232 98 EALRFSAL-------------------------------LRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYN 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1150389631 174 MMKRLRNAADElGKTIIMVMHDLN---FAscYSDLIIALKE-GKLVFSG 218
Cdd:cd03232 147 IVRFLKKLADS-GQAILCTIHQPSasiFE--KFDRLLLLKRgGKTVYFG 192
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-215 |
5.65e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 71.13 E-value: 5.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGiDVTKAKgadfakrlsiL 80
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQ-DLIVAR----------L 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 81 RQENTLTARITVEDLVSFG---------RYPY-SHGVLTKE-DKTF-----------------VDNAIS----YLGLDPY 128
Cdd:PRK11147 72 QQDPPRNVEGTVYDFVAEGieeqaeylkRYHDiSHLVETDPsEKNLnelaklqeqldhhnlwqLENRINevlaQLGLDPD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 129 RKrfLDELSGGQRQRAFVAMVISQNTDYILLDEPLNNLDmrhaVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIA 208
Cdd:PRK11147 152 AA--LSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD----IETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVD 225
|
....*..
gi 1150389631 209 LKEGKLV 215
Cdd:PRK11147 226 LDRGKLV 232
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-228 |
5.65e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 70.83 E-value: 5.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDD---NsiiEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADfAKRL 77
Cdd:COG3845 5 ALELRGITKRFGGvvaN---DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRD-AIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 78 SI--LRQENTLTARITVEDLVSFGRYPYSHGVL-TKEDKTFVDnAIS--Y-LGLDPYRKrfLDELSGGQRQRAFVAMVIS 151
Cdd:COG3845 81 GIgmVHQHFMLVPNLTVAENIVLGLEPTKGGRLdRKAARARIR-ELSerYgLDVDPDAK--VEDLSVGEQQRVEILKALY 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1150389631 152 QNTDYILLDEPLNNLDMRHAVSMMKRLRNAADElGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMKDEI 228
Cdd:COG3845 158 RGARILILDEPTAVLTPQEADELFEILRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEEL 233
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-225 |
6.56e-14 |
|
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: 71.13 E-value: 6.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 16 IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSILRQENTLTARITVEDL 95
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 96 VSFGRYpyshgvlTKED----------KTFVDNAISylGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILLDEPLNN 165
Cdd:TIGR00957 1381 DPFSQY-------SDEEvwwalelahlKTFVSALPD--KLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAA 1451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 166 LDMRHAVSMMKRLRNAADELgkTIIMVMHDLNFASCYSDLIIaLKEGKLVFSGAPENVMK 225
Cdd:TIGR00957 1452 VDLETDNLIQSTIRTQFEDC--TVLTIAHRLNTIMDYTRVIV-LDKGEVAEFGAPSNLLQ 1508
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
2-224 |
7.29e-14 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 70.76 E-value: 7.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNS--IIEDLSLQIPKGGMVSIIGPNGAGKSTLLtmisRLL-----PITkGRITVDGIDVTKAKGADFA 74
Cdd:TIGR03797 452 IEVDRVTFRYRPDGplILDDVSLQIEPGEFVAIVGPSGSGKSTLL----RLLlgfetPES-GSVFYDGQDLAGLDVQAVR 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 75 KRLSILRQENTLTARITVEDLVSfgrypysHGVLTKEDktfVDNAISYLGLDPYRKRF-------LDE----LSGGQRQR 143
Cdd:TIGR03797 527 RQLGVVLQNGRLMSGSIFENIAG-------GAPLTLDE---AWEAARMAGLAEDIRAMpmgmhtvISEgggtLSGGQRQR 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 144 AFVAMVISQNTDYILLDEPLNNLDMR--HAVSmmkrlrNAADELGKTIIMVMHDLN-FASCysDLIIALKEGKLVFSGAP 220
Cdd:TIGR03797 597 LLIARALVRKPRILLFDEATSALDNRtqAIVS------ESLERLKVTRIVIAHRLStIRNA--DRIYVLDAGRVVQQGTY 668
|
....
gi 1150389631 221 ENVM 224
Cdd:TIGR03797 669 DELM 672
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-201 |
1.49e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.14 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAkGADFAKRLSIL 80
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQ-RDEYHQDLLYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 81 RQENTLTARIT-VEDLVSFGRYpysHGVLTKEDktfVDNAISYLGLdpyrKRFLD----ELSGGQRQRAFVA-MVISQNT 154
Cdd:PRK13538 80 GHQPGIKTELTaLENLRFYQRL---HGPGDDEA---LWEALAQVGL----AGFEDvpvrQLSAGQQRRVALArLWLTRAP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1150389631 155 DYIlLDEPLNNLDmRHAVSMMKRLRNAADELGKTIIMVMH-DLNFASC 201
Cdd:PRK13538 150 LWI-LDEPFTAID-KQGVARLEALLAQHAEQGGMVILTTHqDLPVASD 195
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-197 |
1.82e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 67.43 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSIL 80
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 81 RQENTLTARiTVEDLVSFgryPYSHGVLTKEDKTFVDNaISYLGL-DPYRKRFLDELSGGQRQRafVAMVisQNTDY--- 156
Cdd:PRK10247 87 AQTPTLFGD-TVYDNLIF---PWQIRNQQPDPAIFLDD-LERFALpDTILTKNIAELSGGEKQR--ISLI--RNLQFmpk 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1150389631 157 -ILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLN 197
Cdd:PRK10247 158 vLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKD 199
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
13-218 |
1.83e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 69.36 E-value: 1.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 13 DNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSILRQENTLTARiTV 92
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSD-TV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 93 EDLVSFGRyPYShgvlTKEDKTFVDNAISY----LGLDPYRKRFLDE----LSGGQRQRAFVAMVISQNTDYILLDEPLN 164
Cdd:PRK10789 406 ANNIALGR-PDA----TQQEIEHVARLASVhddiLRLPQGYDTEVGErgvmLSGGQKQRISIARALLLNAEILILDDALS 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1150389631 165 NLDMRHAVSMMKRLRNAADelGKTIIMVMHDLNfASCYSDLIIALKEGKLVFSG 218
Cdd:PRK10789 481 AVDGRTEHQILHNLRQWGE--GRTVIISAHRLS-ALTEASEILVMQHGHIAQRG 531
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
10-168 |
2.15e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 67.18 E-value: 2.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 10 SYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSILrqeNTLTAr 89
Cdd:PRK13543 20 SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHL---PGLKA- 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1150389631 90 itveDLVSFGRYPYSHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILLDEPLNNLDM 168
Cdd:PRK13543 96 ----DLSTLENLHFLCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-196 |
2.34e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 66.90 E-value: 2.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGAdFAKRLSIL 80
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCT-YQKQLCFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 81 RQENTLTARITVEDLVSFGRYpYSHGVLTkedktfVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILLD 160
Cdd:PRK13540 80 GHRSGINPYLTLRENCLYDIH-FSPGAVG------ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLD 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 1150389631 161 EPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDL 196
Cdd:PRK13540 153 EPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQDL 188
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
16-223 |
2.37e-13 |
|
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: 68.94 E-value: 2.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 16 IIEDLSLQIPKGGMVSIIGPNGAGKStlLTMIS--RLLP----ITKGRITVDGIDVTKAKGADFAK----RLSILRQE-- 83
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKS--VTALSilRLLPdpaaHPSGSILFDGQDLLGLSERELRRirgnRIAMIFQEpm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 84 ---NTLtarITVED-------LvsfgrypysHGVLTKEDKTfvDNAISYLGL----DPYR--KRFLDELSGGQRQRAFVA 147
Cdd:COG4172 103 tslNPL---HTIGKqiaevlrL---------HRGLSGAAAR--ARALELLERvgipDPERrlDAYPHQLSGGQRQRVMIA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 148 MVISQNTDYILLDEPLNNLDmrhaVS-------MMKRLRnaaDELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAP 220
Cdd:COG4172 169 MALANEPDLLIADEPTTALD----VTvqaqildLLKDLQ---RELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPT 241
|
...
gi 1150389631 221 ENV 223
Cdd:COG4172 242 AEL 244
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
17-226 |
2.64e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 68.19 E-value: 2.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 17 IEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADF-AKRLSI--LRQE--NTLTARIT 91
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWrAVRSDIqmIFQDplASLNPRMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 92 VEDLVSFGRYPYsHGVLTKED-KTFVDNAISYLGLDPYR-KRFLDELSGGQRQRAFVAMVISQNTDYILLDEPLNNLDMR 169
Cdd:PRK15079 117 IGEIIAEPLRTY-HPKLSRQEvKDRVKAMMLKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 170 ---HAVSMMKRLRNaadELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMKD 226
Cdd:PRK15079 196 iqaQVVNLLQQLQR---EMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHN 252
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-249 |
2.90e-13 |
|
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: 68.68 E-value: 2.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRL--LPITKGRI--------------------- 58
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 59 ------------TVDGIDVTKAKGADFAKRLSILRQEntltaritvedlvSFGRYpyshgvltkEDKTFVDNAISYLGLD 126
Cdd:TIGR03269 81 pcpvcggtlepeEVDFWNLSDKLRRRIRKRIAIMLQR-------------TFALY---------GDDTVLDNVLEALEEI 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 127 PYR-----KRFLD----------------ELSGGQRQRAFVAMVISQNTDYILLDEPLNNLDMRHAVSMMKRLRNAADEL 185
Cdd:TIGR03269 139 GYEgkeavGRAVDliemvqlshrithiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKAS 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1150389631 186 GKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVM-----------KDEILSAIYDIdIKVKDIDGQKIAV 249
Cdd:TIGR03269 219 GISMVLTSHWPEVIEDLSDKAIWLENGEIKEEGTPDEVVavfmegvseveKECEVEVGEPI-IKVRNVSKRYISV 292
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
16-218 |
3.06e-13 |
|
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: 66.52 E-value: 3.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 16 IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPIT---KGRITVDGIDVTKAKgaDFAKRLSILRQENTL-TARIT 91
Cdd:cd03233 22 ILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFA--EKYPGEIIYVSEEDVhFPTLT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 92 VEDLVSFgrypyshgvltkedktfvdnAISYLGldpyrKRFLDELSGGQRQRAFVAMVISQNTDYILLDEPLNNLDMRHA 171
Cdd:cd03233 100 VRETLDF--------------------ALRCKG-----NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1150389631 172 VSMMKRLRNAADELGKTiimvmhdlNFASCYS---------DLIIALKEGKLVFSG 218
Cdd:cd03233 155 LEILKCIRTMADVLKTT--------TFVSLYQasdeiydlfDKVLVLYEGRQIYYG 202
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
21-196 |
3.18e-13 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 68.66 E-value: 3.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 21 SLQIPKGGMVS-IIGPNGAGKSTLLTMISRLLPITKGRITVDGI--DVTKA-KGADFAKRLSILRqENTLTARI------ 90
Cdd:COG1245 92 GLPVPKKGKVTgILGPNGIGKSTALKILSGELKPNLGDYDEEPSwdEVLKRfRGTELQDYFKKLA-NGEIKVAHkpqyvd 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 91 --------TVEDLvsfgrypyshgvLTKED-KTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILLDE 161
Cdd:COG1245 171 lipkvfkgTVREL------------LEKVDeRGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190
....*....|....*....|....*....|....*
gi 1150389631 162 PLNNLDMRHAVSMMKRLRNAADElGKTIIMVMHDL 196
Cdd:COG1245 239 PSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDL 272
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
19-223 |
3.72e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 67.98 E-value: 3.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 19 DLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDG-IDVTKAKGADFA---KRLSILRQENTLTARITVED 94
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrVLFDAEKGICLPpekRRIGYVFQDARLFPHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 95 LVSFGrypyshgvLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILLDEPLNNLDMRHAVSM 174
Cdd:PRK11144 96 NLRYG--------MAKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKREL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1150389631 175 MKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENV 223
Cdd:PRK11144 168 LPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
12-214 |
3.77e-13 |
|
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: 68.82 E-value: 3.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 12 DDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGI-----------DVTKAKGADFAKRLSIL 80
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSvayvpqqawiqNDSLRENILFGKALNEK 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 81 RQENTLTARITVEDLvsfgrypyshGVLTKEDKTfvdnAISYLGLDpyrkrfldeLSGGQRQRAFVAMVISQNTDYILLD 160
Cdd:TIGR00957 729 YYQQVLEACALLPDL----------EILPSGDRT----EIGEKGVN---------LSGGQKQRVSLARAVYSNADIYLFD 785
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1150389631 161 EPLNNLD-------MRHAVSMMKRLRNaadelgKTIIMVMHDLNFAScYSDLIIALKEGKL 214
Cdd:TIGR00957 786 DPLSAVDahvgkhiFEHVIGPEGVLKN------KTRILVTHGISYLP-QVDVIIVMSGGKI 839
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-205 |
6.05e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 66.60 E-value: 6.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPItKGRITVDGiDVTKAKGADFAKRLSI-- 79
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNEL-ESEVRVEG-RVEFFNQNIYERRVNLnr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 80 LRQENTLTA------RITVEDLVSFG-RYPYSHGVLTKEDktFVDNAISYLGL-DPYRKRFLD---ELSGGQRQRAFVAM 148
Cdd:PRK14258 86 LRRQVSMVHpkpnlfPMSVYDNVAYGvKIVGWRPKLEIDD--IVESALKDADLwDEIKHKIHKsalDLSGGQQQRLCIAR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1150389631 149 VISQNTDYILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDL 205
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDF 220
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
11-215 |
6.32e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 66.34 E-value: 6.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 11 YDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISR---LLP--ITKGRITVDGIDV--TKAKGADFAKRLS-ILRQ 82
Cdd:PRK14239 15 YNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRmndLNPevTITGSIVYNGHNIysPRTDTVDLRKEIGmVFQQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 83 ENTLTARItVEDLVsfgrypYSHGVLTKEDKTFVDNAI--SYLGL---DPYRKRFLDE---LSGGQRQRAFVAMVISQNT 154
Cdd:PRK14239 95 PNPFPMSI-YENVV------YGLRLKGIKDKQVLDEAVekSLKGAsiwDEVKDRLHDSalgLSGGQQQRVCIARVLATSP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1150389631 155 DYILLDEPLNNLDMRHAVSMMKRLRNAADELgkTIIMVMHDLNFASCYSDLIIALKEGKLV 215
Cdd:PRK14239 168 KIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLI 226
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
21-196 |
6.65e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 67.91 E-value: 6.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 21 SLQIPKGGMVS-IIGPNGAGKSTLLTMIS-RLLP---ITKGRITVDGIdVTKAKGA---DFAKRLSilrqENTLTARI-- 90
Cdd:PRK13409 92 GLPIPKEGKVTgILGPNGIGKTTAVKILSgELIPnlgDYEEEPSWDEV-LKRFRGTelqNYFKKLY----NGEIKVVHkp 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 91 ------------TVEDLvsfgrypyshgvLTKEDKTFV-DNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYI 157
Cdd:PRK13409 167 qyvdlipkvfkgKVREL------------LKKVDERGKlDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFY 234
|
170 180 190
....*....|....*....|....*....|....*....
gi 1150389631 158 LLDEPLNNLDMRHAVSMMKRLRNAADelGKTIIMVMHDL 196
Cdd:PRK13409 235 FFDEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHDL 271
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
2-221 |
8.32e-13 |
|
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: 65.74 E-value: 8.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMIS--RLLPITKGRITVDGIDVTKAKGADFAKR-LS 78
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAghPSYEVTSGTILFKGQDLLELEPDERARAgLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 79 ILRQENTLTARITVEDLV-----SFGRYPYSHGVLTKEDKTFVDNAISYLGLDP-YRKRFLDE-LSGGQRQRAFVAMVIS 151
Cdd:TIGR01978 81 LAFQYPEEIPGVSNLEFLrsalnARRSARGEEPLDLLDFEKLLKEKLALLDMDEeFLNRSVNEgFSGGEKKRNEILQMAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1150389631 152 QNTDYILLDEPLNNLD---MRHAVSMMKRLRNAadelGKTIIMVMHDLN-FASCYSDLIIALKEGKLVFSGAPE 221
Cdd:TIGR01978 161 LEPKLAILDEIDSGLDidaLKIVAEGINRLREP----DRSFLIITHYQRlLNYIKPDYVHVLLDGRIVKSGDVE 230
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-198 |
1.04e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 67.28 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 3 EISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLT-MISRLLPiTKGRITVDgidvTKAKGADFAKRLSILR 81
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKlMLGQLQA-DSGRIHCG----TKLEVAYFDQHRAELD 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 82 QENtltariTVEDLVSFGrypyshgvltKEDKTfVD----NAISYLG---LDPYRKRF-LDELSGGQRQRAFVAMVISQN 153
Cdd:PRK11147 396 PEK------TVMDNLAEG----------KQEVM-VNgrprHVLGYLQdflFHPKRAMTpVKALSGGERNRLLLARLFLKP 458
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1150389631 154 TDYILLDEPLNNLDmrhaVSMMKRLRNAADELGKTIIMVMHDLNF 198
Cdd:PRK11147 459 SNLLILDEPTNDLD----VETLELLEELLDSYQGTVLLVSHDRQF 499
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
9-226 |
1.39e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 65.33 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 9 KSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADF--AKRLSILR----- 81
Cdd:PRK11701 14 KLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseAERRRLLRtewgf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 82 -QENTLTA-RITV-------EDLVSFGRYPYSHgvltkedktFVDNAISYLG---LDPYRkrfLDEL----SGGQRQRAF 145
Cdd:PRK11701 94 vHQHPRDGlRMQVsaggnigERLMAVGARHYGD---------IRATAGDWLErveIDAAR---IDDLpttfSGGMQQRLQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 146 VAMVISQNTDYILLDEPLNNLDmrhaVSMMKRL----RNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPE 221
Cdd:PRK11701 162 IARNLVTHPRLVFMDEPTGGLD----VSVQARLldllRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTD 237
|
....*
gi 1150389631 222 NVMKD 226
Cdd:PRK11701 238 QVLDD 242
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-66 |
1.52e-12 |
|
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: 66.77 E-value: 1.52e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1150389631 2 IEISHVFKSYD-DNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVT 66
Cdd:COG5265 358 VRFENVSFGYDpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIR 423
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-230 |
1.59e-12 |
|
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: 66.39 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLP--ITKGRITVDG-------IDVTKAKGa 71
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGsplkasnIRDTERAG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 72 dfakrLSILRQENTLTARITVEDLVSFGRYPYSHGVLTKEDKTF--VDNAISYLGLDPYR-KRFLDELSGGQRQRAFVAM 148
Cdd:TIGR02633 80 -----IVIIHQELTLVPELSVAENIFLGNEITLPGGRMAYNAMYlrAKNLLRELQLDADNvTRPVGDYGGGQQQLVEIAK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 149 VISQNTDYILLDEPLNNLDMRHAVSMMKRLRNAADElGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMKDEI 228
Cdd:TIGR02633 155 ALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDI 233
|
..
gi 1150389631 229 LS 230
Cdd:TIGR02633 234 IT 235
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
2-225 |
1.66e-12 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 66.51 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYD--DNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSI 79
Cdd:TIGR03796 478 VELRNITFGYSplEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAM 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 80 LRQENTL---TAR---------ITVEDLVSFGRYPYSHGVLTKEDKTFvDNAISYLGLDpyrkrfldeLSGGQRQRAFVA 147
Cdd:TIGR03796 558 VDQDIFLfegTVRdnltlwdptIPDADLVRACKDAAIHDVITSRPGGY-DAELAEGGAN---------LSGGQRQRLEIA 627
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1150389631 148 MVISQNTDYILLDEPLNNLDMRHAVSMMKRLRnaadELGKTIIMVMHDLN-FASCysDLIIALKEGKLVFSGAPENVMK 225
Cdd:TIGR03796 628 RALVRNPSILILDEATSALDPETEKIIDDNLR----RRGCTCIIVAHRLStIRDC--DEIIVLERGKVVQRGTHEELWA 700
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
11-205 |
2.71e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 64.80 E-value: 2.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 11 YDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISR---LLPITK--GRIT----------VDGIDVTKAKGADFAK 75
Cdd:PRK14243 20 YGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRlndLIPGFRveGKVTfhgknlyapdVDPVEVRRRIGMVFQK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 76 rlsilrqENTLTARITveDLVSFGryPYSHGVLTKEDKtFVDNAISYLGL-----DPYRKRFLdELSGGQRQRAFVAMVI 150
Cdd:PRK14243 100 -------PNPFPKSIY--DNIAYG--ARINGYKGDMDE-LVERSLRQAALwdevkDKLKQSGL-SLSGGQQQRLCIARAI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1150389631 151 SQNTDYILLDEPLNNLDmrhAVSMMkRLRNAADELGK--TIIMVMHDLNFASCYSDL 205
Cdd:PRK14243 167 AVQPEVILMDEPCSALD---PISTL-RIEELMHELKEqyTIIIVTHNMQQAARVSDM 219
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-230 |
2.79e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 64.75 E-value: 2.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGidvtkakgadfAKRLSIL 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG-----------KLRIGYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 81 RQENTL--TARITVEdlvsfgRYPYSHGVLTKEDktfvdnaisylgLDPYRKRF---------LDELSGGQRQRAFVAMV 149
Cdd:PRK09544 73 PQKLYLdtTLPLTVN------RFLRLRPGTKKED------------ILPALKRVqaghlidapMQKLSGGETQRVLLARA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 150 ISQNTDYILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEgKLVFSGAPENV-MKDEI 228
Cdd:PRK09544 135 LLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEVVsLHPEF 213
|
..
gi 1150389631 229 LS 230
Cdd:PRK09544 214 IS 215
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
21-227 |
3.33e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 64.24 E-value: 3.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 21 SLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAkRLSILR--QENTLTARITV-EDL-V 96
Cdd:PRK11300 25 NLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA-RMGVVRtfQHVRLFREMTViENLlV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 97 SFGRY---PYSHGVLT-----KEDKTFVDNAISYL---GLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILLDEP--- 162
Cdd:PRK11300 104 AQHQQlktGLFSGLLKtpafrRAESEALDRAATWLervGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPaag 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1150389631 163 LNNLDMRHAVSMMKRLRnaaDELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMKDE 227
Cdd:PRK11300 184 LNPKETKELDELIAELR---NEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-230 |
3.54e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 65.34 E-value: 3.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLP--ITKGRITVDG-------IDVTKAKGa 71
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgTYEGEIIFEGeelqasnIRDTERAG- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 72 dfakrLSILRQENTLTARITVEDLVSFGRYPYSHGVLtkedktfvDNAISY-----------LGLDPYRKrfLDELSGGQ 140
Cdd:PRK13549 84 -----IAIIHQELALVKELSVLENIFLGNEITPGGIM--------DYDAMYlraqkllaqlkLDINPATP--VGNLGLGQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 141 RQRAFVAMVISQNTDYILLDEPLNNL---DMRHAVSMMKRLRNAadelGKTIIMVMHDLNFASCYSDLIIALKEGKLVFS 217
Cdd:PRK13549 149 QQLVEIAKALNKQARLLILDEPTASLtesETAVLLDIIRDLKAH----GIACIYISHKLNEVKAISDTICVIRDGRHIGT 224
|
250
....*....|...
gi 1150389631 218 GAPENVMKDEILS 230
Cdd:PRK13549 225 RPAAGMTEDDIIT 237
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
17-218 |
5.13e-12 |
|
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: 62.34 E-value: 5.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 17 IEDLSLQIPKGGMVSIIGPNGAGKSTLLTmisrllpitkgritvdgiDVTKAKGAdfakrlsiLRQENTLTaritvedlv 96
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN------------------EGLYASGK--------ARLISFLP--------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 97 sfgRYPYSHGVLTKEDKTFVDNAISYLGLDpyrkRFLDELSGGQRQRAFVAMVISQNTDYIL--LDEP---LNNLDMRHA 171
Cdd:cd03238 56 ---KFSRNKLIFIDQLQFLIDVGLGYLTLG----QKLSTLSGGELQRVKLASELFSEPPGTLfiLDEPstgLHQQDINQL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1150389631 172 VSMMKRLRNaadeLGKTIIMVMHDLNFaSCYSDLIIALKE------GKLVFSG 218
Cdd:cd03238 129 LEVIKGLID----LGNTVILIEHNLDV-LSSADWIIDFGPgsgksgGKVVFSG 176
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
20-227 |
5.96e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 65.14 E-value: 5.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 20 LSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSILRQENTLtaritVEDLVSFG 99
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVL-----FSGTVRFN 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 100 RYPYS-HG---VLTKEDKTFVDNAI--SYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILLDEPLNNLDMRHAVS 173
Cdd:PLN03130 1333 LDPFNeHNdadLWESLERAHLKDVIrrNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDAL 1412
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1150389631 174 MMKRLRnaaDELGK-TIIMVMHDLN-FASCysDLIIALKEGKLVFSGAPENVMKDE 227
Cdd:PLN03130 1413 IQKTIR---EEFKScTMLIIAHRLNtIIDC--DRILVLDAGRVVEFDTPENLLSNE 1463
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
16-215 |
6.38e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 64.73 E-value: 6.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 16 IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLP-----ITKGRITVDGIDVTKAKGADF----AKRLSILRQEN-- 84
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPsppvvYPSGDIRFHGESLLHASEQTLrgvrGNKIAMIFQEPmv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 85 TLTARITVE----DLVSFGRypyshGVLTKEDKTFVDNAISYLGLDPYRKRFLD---ELSGGQRQRAFVAMVISQNTDYI 157
Cdd:PRK15134 104 SLNPLHTLEkqlyEVLSLHR-----GMRREAARGEILNCLDRVGIRQAAKRLTDyphQLSGGERQRVMIAMALLTRPELL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1150389631 158 LLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLV 215
Cdd:PRK15134 179 IADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCV 236
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-214 |
1.04e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 62.49 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDN----SIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKr 76
Cdd:PRK10584 6 IVEVHHLKKSVGQGehelSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAK- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 77 lsiLRQEN------------TLTARITVEdLVSFGRypyshGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRA 144
Cdd:PRK10584 85 ---LRAKHvgfvfqsfmlipTLNALENVE-LPALLR-----GESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1150389631 145 FVAMVISQNTDYILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFAS-CysDLIIALKEGKL 214
Cdd:PRK10584 156 ALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAArC--DRRLRLVNGQL 224
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
27-194 |
1.64e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.97 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 27 GGMVSIIGPNGAGKSTLLTMISRLLpiTKGRITvDGIDVTKAKGAD--FAKRLSILRQENTLTARITVEDLVSFG---RY 101
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAERV--TTGVIT-GGDRLVNGRPLDssFQRSIGYVQQQDLHLPTSTVRESLRFSaylRQ 865
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 102 PYShgVLTKEDKTFVDNAISYLGLDPYRKRFLDE----LSGGQRQRAFVAMVISQNTDYIL-LDEPLNNLDMRHAVSMMK 176
Cdd:TIGR00956 866 PKS--VSKSEKMEYVEEVIKLLEMESYADAVVGVpgegLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICK 943
|
170
....*....|....*...
gi 1150389631 177 RLRNAADElGKTIIMVMH 194
Cdd:TIGR00956 944 LMRKLADH-GQAILCTIH 960
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
27-218 |
2.10e-11 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 63.71 E-value: 2.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 27 GGMVSIIGPNGAGKSTLLTMISrllpitkGRIT---VDG---IDVTKAKGADFAKRLSILRQENTLTARITV-EDLV--S 97
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLA-------GRKTggyIEGdirISGFPKKQETFARISGYCEQNDIHSPQVTVrESLIysA 978
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 98 FGRYPYShgvLTKEDK-TFVDNAISYLGLDPYRKRF-----LDELSGGQRQRAFVAMVISQNTDYILLDEPLNNLDMRHA 171
Cdd:PLN03140 979 FLRLPKE---VSKEEKmMFVDEVMELVELDNLKDAIvglpgVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAA 1055
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1150389631 172 VSMMKRLRNAADElGKTIIMVMH--DLNFASCYSDLIIALKEGKLVFSG 218
Cdd:PLN03140 1056 AIVMRTVRNTVDT-GRTVVCTIHqpSIDIFEAFDELLLMKRGGQVIYSG 1103
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
2-229 |
3.18e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.07 E-value: 3.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYD---DNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLT-MISRLLPITKGRITVDGidvtkakGADFAKRL 77
Cdd:PLN03232 615 ISIKNGYFSWDsktSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRG-------SVAYVPQV 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 78 SILRQEntltariTVEDLVSFGRYPYSHGVLTKEDKTFVDNaisylGLDPYRKRFLDEL-------SGGQRQRAFVAMVI 150
Cdd:PLN03232 688 SWIFNA-------TVRENILFGSDFESERYWRAIDVTALQH-----DLDLLPGRDLTEIgergvniSGGQKQRVSMARAV 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 151 SQNTDYILLDEPLNNLD--MRHAV--SMMKrlrnaaDEL-GKTIIMVMHDLNFAScYSDLIIALKEGKLVFSGAPENVMK 225
Cdd:PLN03232 756 YSNSDIYIFDDPLSALDahVAHQVfdSCMK------DELkGKTRVLVTNQLHFLP-LMDRIILVSEGMIKEEGTFAELSK 828
|
....
gi 1150389631 226 DEIL 229
Cdd:PLN03232 829 SGSL 832
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1-230 |
5.15e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.05 E-value: 5.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEIShvfKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDG--IDVTKAKGAdFAKRLS 78
Cdd:PRK10982 1 MSNIS---KSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkeIDFKSSKEA-LENGIS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 79 ILRQENTLTARITVEDLVSFGRYPySHGVLTKEDKTFVDNAISY--LGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDY 156
Cdd:PRK10982 77 MVHQELNLVLQRSVMDNMWLGRYP-TKGMFVDQDKMYRDTKAIFdeLDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1150389631 157 ILLDEPLNNL---DMRHAVSMMKRLRnaadELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMKDEILS 230
Cdd:PRK10982 156 VIMDEPTSSLtekEVNHLFTIIRKLK----ERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIA 228
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
17-214 |
5.45e-11 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 59.75 E-value: 5.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 17 IEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADfAKRLSIlrqentltARITvEDlv 96
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRD-AIRAGI--------AYVP-ED-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 97 sfgryPYSHGVLTkeDKTFVDN-AISYLgldpyrkrfldeLSGGQRQRAFVAMVISQNTDYILLDEPLNNLDMRHAVSMM 175
Cdd:cd03215 84 -----RKREGLVL--DLSVAENiALSSL------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIY 144
|
170 180 190
....*....|....*....|....*....|....*....
gi 1150389631 176 KRLRNAADElGKTIIMVMHDLNFASCYSDLIIALKEGKL 214
Cdd:cd03215 145 RLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
16-194 |
5.65e-11 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 62.07 E-value: 5.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 16 IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDgidvtkAKGADFakrlsILRQENTLTARiTVEDL 95
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKP------AKGKLF-----YVPQRPYMTLG-TLRDQ 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 96 VSfgrYPYS------HGVLTKEDKTFVDNA-ISYL-----GLDPYRKrFLDELSGGQRQRAFVAMVISQNTDYILLDEPL 163
Cdd:TIGR00954 535 II---YPDSsedmkrRGLSDKDLEQILDNVqLTHIleregGWSAVQD-WMDVLSGGEKQRIAMARLFYHKPQFAILDECT 610
|
170 180 190
....*....|....*....|....*....|.
gi 1150389631 164 NNLdmrhAVSMMKRLRNAADELGKTIIMVMH 194
Cdd:TIGR00954 611 SAV----SVDVEGYMYRLCREFGITLFSVSH 637
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-162 |
1.13e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 61.29 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVdgidvtkaKGADFAKRlsilR 81
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEV--------LGGDMADA----R 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 82 QENTLTARI---------------TV-EDLVSFGRYpYSHGvlTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQR-- 143
Cdd:NF033858 70 HRRAVCPRIaympqglgknlyptlSVfENLDFFGRL-FGQD--AAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKlg 146
|
170 180
....*....|....*....|..
gi 1150389631 144 ---AFVamvisQNTDYILLDEP 162
Cdd:NF033858 147 lccALI-----HDPDLLILDEP 163
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-218 |
1.36e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 60.89 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSY-DDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSIL 80
Cdd:PRK10790 341 IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 81 RQENTLTARiTVEDLVSFGRYPYSHGV--------LTKEDKTFVDNAISYLGLDPyrkrflDELSGGQRQRAFVAMVISQ 152
Cdd:PRK10790 421 QQDPVVLAD-TFLANVTLGRDISEEQVwqaletvqLAELARSLPDGLYTPLGEQG------NNLSVGQKQLLALARVLVQ 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1150389631 153 NTDYILLDEPLNNLDMRHAVSMMKRLRNAADElgKTIIMVMHDLNfASCYSDLIIALKEGKLVFSG 218
Cdd:PRK10790 494 TPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAHRLS-TIVEADTILVLHRGQAVEQG 556
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
17-228 |
1.40e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 60.81 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 17 IEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKR-LSIL---RQENTLTARITV 92
Cdd:COG3845 274 LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYIpedRLGRGLVPDMSV 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 93 ED---LVSFGRYPYSHGVLTKEDK--TFVDNAIsylgldpyrKRF----------LDELSGGQRQRAFVAMVISQNTDYI 157
Cdd:COG3845 354 AEnliLGRYRRPPFSRGGFLDRKAirAFAEELI---------EEFdvrtpgpdtpARSLSGGNQQKVILARELSRDPKLL 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1150389631 158 LLDEPLNNLDMRHAVSMMKRLRNAADElGKTIIMVMHDLN--FAscYSDLIIALKEGKLVFSGAPENVMKDEI 228
Cdd:COG3845 425 IAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDeiLA--LSDRIAVMYEGRIVGEVPAAEATREEI 494
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
2-227 |
2.54e-10 |
|
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: 59.15 E-value: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDN--SIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSI 79
Cdd:cd03288 20 IKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 80 LRQENTL---TARITVEDLVSFGRYPYSHGVLTKEDKTFVDNAISylGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDY 156
Cdd:cd03288 100 ILQDPILfsgSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPG--GLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1150389631 157 ILLDEPLNNLDMRHAVSMMKRLRNA-ADelgKTIIMVMHDLNfASCYSDLIIALKEGKLVFSGAPENVMKDE 227
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAfAD---RTVVTIAHRVS-TILDADLVLVLSRGILVECDTPENLLAQE 245
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
16-223 |
2.68e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 58.94 E-value: 2.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 16 IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLP----ITKGRITVDGIDVTkakGADFAKRLSILRQENTLTARIT 91
Cdd:PRK10418 18 LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPagvrQTAGRVLLDGKPVA---PCALRGRKIATIMQNPRSAFNP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 92 VEDLVSFGRYPYSHGVLTKEDKTFVDnAISYLGL-DPYR--KRFLDELSGGQRQRAFVAMVISQNTDYILLDEPLNNLDM 168
Cdd:PRK10418 95 LHTMHTHARETCLALGKPADDATLTA-ALEAVGLeNAARvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1150389631 169 RHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENV 223
Cdd:PRK10418 174 VAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-195 |
3.03e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 59.99 E-value: 3.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYDDNSI-IEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLS-- 78
Cdd:PRK10522 323 LELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSav 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 79 ---------ILRQENTLTARITVEDLVSFgrypyshgvLTKEDK-TFVDNAISYLgldpyrkrfldELSGGQRQRAFVAM 148
Cdd:PRK10522 403 ftdfhlfdqLLGPEGKPANPALVEKWLER---------LKMAHKlELEDGRISNL-----------KLSKGQKKRLALLL 462
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1150389631 149 VISQNTDYILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHD 195
Cdd:PRK10522 463 ALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD 509
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-228 |
3.54e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 59.79 E-value: 3.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 16 IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRItvdgidvtkakgadFAKRlSIL---RQENTLTAriTV 92
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV--------------WAER-SIAyvpQQAWIMNA--TV 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 93 EDLVSFgrypyshgvLTKEDKTFVDNAI--SYL---------GLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILLDE 161
Cdd:PTZ00243 738 RGNILF---------FDEEDAARLADAVrvSQLeadlaqlggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDD 808
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1150389631 162 PLNNLDMRHAVSMMK-----RLRnaadelGKTIIMVMHDLNFAScYSDLIIALKEGKLVFSGAPENVMKDEI 228
Cdd:PTZ00243 809 PLSALDAHVGERVVEecflgALA------GKTRVLATHQVHVVP-RADYVVALGDGRVEFSGSSADFMRTSL 873
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
20-215 |
5.23e-10 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 59.04 E-value: 5.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 20 LSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTkakgadfAKRLSILRQentltaRITV------- 92
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT-------ADNREAYRQ------LFSAvfsdfhl 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 93 -EDLVsfgrypyshGVLTKEDKTFVDNAISYLGLDpyRK------RFLD-ELSGGQRQRafVAMVIS--QNTDYILLDEP 162
Cdd:COG4615 418 fDRLL---------GLDGEADPARARELLERLELD--HKvsvedgRFSTtDLSQGQRKR--LALLVAllEDRPILVFDEW 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1150389631 163 lnnldmrhavsmmkrlrnAAD-----------EL-------GKTIIMVMHDLNFASCySDLIIALKEGKLV 215
Cdd:COG4615 485 ------------------AADqdpefrrvfytELlpelkarGKTVIAISHDDRYFDL-ADRVLKMDYGKLV 536
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-218 |
5.74e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 59.03 E-value: 5.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVdgidvtkAKGAD---FAK-R 76
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-------AKGIKlgyFAQhQ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 77 LSILR-QENTLT--ARITVEDLVSFGRyPYSHGVLTKEDKTfvdnaisylgLDPYRkRFldelSGGQRQRAFVAMVISQN 153
Cdd:PRK10636 385 LEFLRaDESPLQhlARLAPQELEQKLR-DYLGGFGFQGDKV----------TEETR-RF----SGGEKARLVLALIVWQR 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1150389631 154 TDYILLDEPLN--NLDMRHAvsmmkrLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKL-VFSG 218
Cdd:PRK10636 449 PNLLLLDEPTNhlDLDMRQA------LTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVePFDG 510
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-226 |
6.66e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.98 E-value: 6.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYD---DNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLT-MISRLLPITKGRITVDGidvTKAkgadFAKRL 77
Cdd:PLN03130 615 ISIKNGYFSWDskaERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRG---TVA----YVPQV 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 78 SILRQEntltariTVEDLVSFGRyPYshgvltkeDKTFVDNAISYLGLDpyrkRFLDEL---------------SGGQRQ 142
Cdd:PLN03130 688 SWIFNA-------TVRDNILFGS-PF--------DPERYERAIDVTALQ----HDLDLLpggdlteigergvniSGGQKQ 747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 143 RAFVAMVISQNTDYILLDEPLNNLDMRHAVSMMKR-LRnaaDEL-GKTIIMVMHDLNFAScYSDLIIALKEGKLVFSGAP 220
Cdd:PLN03130 748 RVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKcIK---DELrGKTRVLVTNQLHFLS-QVDRIILVHEGMIKEEGTY 823
|
....*.
gi 1150389631 221 ENVMKD 226
Cdd:PLN03130 824 EELSNN 829
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-232 |
1.02e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.14 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADfAKRLSI- 79
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAK-AHQLGIy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 80 -LRQENTLTARITVEDLVSFGrypyshgvLTK--EDKTFVDNAISYLG--LDPYRKRFLDELSggQRQRAFVAMVISQNT 154
Cdd:PRK15439 90 lVPQEPLLFPNLSVKENILFG--------LPKrqASMQKMKQLLAALGcqLDLDSSAGSLEVA--DRQIVEILRGLMRDS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1150389631 155 DYILLDEPLNNLDMRHAVSMMKRLRnAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMKDEILSAI 232
Cdd:PRK15439 160 RILILDEPTASLTPAETERLFSRIR-ELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDIIQAI 236
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-198 |
1.37e-09 |
|
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: 56.67 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSY-----DDNSI--IEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISR-LLPiTKGRITVD----GIDVTKA 68
Cdd:COG4778 4 LLEVENLSKTFtlhlqGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGnYLP-DSGSILVRhdggWVDLAQA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 69 kgadfAKR--LSILRQE-----NTLTA--RITVEDLVSfgrYP-YSHGVLTKEDKTFVDNAISYLGLDPyrkrfldEL-- 136
Cdd:COG4778 83 -----SPReiLALRRRTigyvsQFLRVipRVSALDVVA---EPlLERGVDREEARARARELLARLNLPE-------RLwd 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1150389631 137 ------SGGQRQR-----AFVAmvisqntDY--ILLDEPLNNLDM--RHAV-SMMKRLRNAadelGKTIIMVMHDLNF 198
Cdd:COG4778 148 lppatfSGGEQQRvniarGFIA-------DPplLLLDEPTASLDAanRAVVvELIEEAKAR----GTAIIGIFHDEEV 214
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-223 |
1.53e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.94 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 17 IEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGI------------------DVTKAKGADFAkrls 78
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqvielseqsaaQMRHVRGADMA---- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 79 ILRQE--NTLTARITV-EDLVSFGRYpysHGVLTKEDKTfvdnAISYLGLDPYR--------KRFLDELSGGQRQRAFVA 147
Cdd:PRK10261 108 MIFQEpmTSLNPVFTVgEQIAESIRL---HQGASREEAM----VEAKRMLDQVRipeaqtilSRYPHQLSGGMRQRVMIA 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1150389631 148 MVISQNTDYILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENV 223
Cdd:PRK10261 181 MALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
24-220 |
1.65e-09 |
|
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: 55.66 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 24 IPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTkakgadfakrlsilrqentltaritvedlvsfgrypy 103
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV------------------------------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 104 shgvltkedktfvdnaisylgldpYRKRFLDeLSGGQRQRAFVAMVISQNTDYILLDEPLNNLDMRHAVSMMKRLRNAAD 183
Cdd:cd03222 65 ------------------------YKPQYID-LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSE 119
|
170 180 190
....*....|....*....|....*....|....*..
gi 1150389631 184 ELGKTIIMVMHDLNFASCYSDLIIalkegklVFSGAP 220
Cdd:cd03222 120 EGKKTALVVEHDLAVLDYLSDRIH-------VFEGEP 149
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
17-224 |
1.80e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 56.72 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 17 IEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSILRQE--NTLTARITVED 94
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDpsTSLNPRQRISQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 95 LVSFgryP--YSHGVLTKEDKTFVDNAISYLGLDPYRKRFLDE-LSGGQRQRAFVAMVISQNTDYILLDEPLNNLDMrha 171
Cdd:PRK15112 109 ILDF---PlrLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHmLAPGQKQRLGLARALILRPKVIIADEALASLDM--- 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1150389631 172 vSMMKRLRNAADEL----GKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVM 224
Cdd:PRK15112 183 -SMRSQLINLMLELqekqGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVL 238
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
13-214 |
2.11e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.10 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 13 DNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKR----LSILRQEN---- 84
Cdd:PRK09700 275 DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKgmayITESRRDNgffp 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 85 --TLTARITVEDLVSFGRYPYSHGVLT-KEDKTFVDNAISYLGLDPYR-KRFLDELSGGQRQRAFVAMVISQNTDYILLD 160
Cdd:PRK09700 355 nfSIAQNMAISRSLKDGGYKGAMGLFHeVDEQRTAENQRELLALKCHSvNQNITELSGGNQQKVLISKWLCCCPEVIIFD 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1150389631 161 EPLNNLDMRHAVSMMKRLRNAADElGKTIIMVMHDLNFASCYSDLIIALKEGKL 214
Cdd:PRK09700 435 EPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-226 |
5.71e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.02 E-value: 5.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 17 IEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDG--IDVTKAKGADFAKR-LSILRQE--NTLTARIT 91
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqrIDTLSPGKLQALRRdIQFIFQDpyASLDPRQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 92 VEDlvSFGRYPYSHGVLT-KEDKTFVDNAISYLGLDP-YRKRFLDELSGGQRQRAFVAMVISQNTDYILLDEPLNNLDMR 169
Cdd:PRK10261 420 VGD--SIMEPLRVHGLLPgKAAAARVAWLLERVGLLPeHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVS 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1150389631 170 HAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMKD 226
Cdd:PRK10261 498 IRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFEN 554
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
21-196 |
7.26e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 55.36 E-value: 7.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 21 SLQIPKGGMVSIIGPNGAGKSTL---LTMISrllPITKGRITVDGIDVTKAKGAdfAKRLsiLRQE---------NTLTA 88
Cdd:PRK11308 35 SFTLERGKTLAVVGESGCGKSTLarlLTMIE---TPTGGELYYQGQDLLKADPE--AQKL--LRQKiqivfqnpyGSLNP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 89 RITVEDLVSfgrYPYS-HGVLTK-EDKTFVDNAISYLGLDP-YRKRFLDELSGGQRQRAFVAMVISQNTDYILLDEPLNN 165
Cdd:PRK11308 108 RKKVGQILE---EPLLiNTSLSAaERREKALAMMAKVGLRPeHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSA 184
|
170 180 190
....*....|....*....|....*....|.
gi 1150389631 166 LDMRHAVSMMKRLRNAADELGKTIIMVMHDL 196
Cdd:PRK11308 185 LDVSVQAQVLNLMMDLQQELGLSYVFISHDL 215
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-198 |
9.42e-09 |
|
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: 55.33 E-value: 9.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 4 ISHVFKSYDDN-SIIEDLSLQIPKGGMVSIIGPNGAGKSTLLtmisrllpitkgRItVDGID---VTKAKGADFAKrLSI 79
Cdd:TIGR03719 7 MNRVSKVVPPKkEILKDISLSFFPGAKIGVLGLNGAGKSTLL------------RI-MAGVDkdfNGEARPQPGIK-VGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 80 LRQE----NTLTARITVEDLVS-----FGRYPYSHGVLTKEDKTF-------------------------VDNAISYLGL 125
Cdd:TIGR03719 73 LPQEpqldPTKTVRENVEEGVAeikdaLDRFNEISAKYAEPDADFdklaaeqaelqeiidaadawdldsqLEIAMDALRC 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1150389631 126 DPYRKRfLDELSGGQRQRAFVAMVISQNTDYILLDEPLNNLDmrhAVSmMKRLRNAADELGKTIIMVMHDLNF 198
Cdd:TIGR03719 153 PPWDAD-VTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD---AES-VAWLERHLQEYPGTVVAVTHDRYF 220
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-48 |
1.14e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.02 E-value: 1.14e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1150389631 2 IEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMIS 48
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLIT 307
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-219 |
2.43e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 54.53 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 16 IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGidvtkakgadfakRLSILRQENTLTARiTVEDL 95
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPG-TIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 96 VSFG----RYPYSH-----------GVLTKEDKT-FVDNAISylgldpyrkrfldeLSGGQRQRAFVAMVISQNTDYILL 159
Cdd:TIGR01271 507 IIFGlsydEYRYTSvikacqleediALFPEKDKTvLGEGGIT--------------LSGGQRARISLARAVYKDADLYLL 572
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1150389631 160 DEPLNNLDMRHAVSMMKR-----LRNaadelgKTIIMVMHDLNFAScYSDLIIALKEGKLVFSGA 219
Cdd:TIGR01271 573 DSPFTHLDVVTEKEIFESclcklMSN------KTRILVTSKLEHLK-KADKILLLHEGVCYFYGT 630
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-215 |
3.56e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 53.47 E-value: 3.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVT-KAKGADFAKRLSI 79
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSSQEAGIGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 80 LRQENTLTARITVEDLVSFGRYPYSH--GVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYI 157
Cdd:PRK10762 84 IHQELNLIPQLTIAENIFLGREFVNRfgRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 158 LLDEPLNNLDMRHAVSMMKRLRNAADElGKTIIMVMHDLN--FASCysDLIIALKEGKLV 215
Cdd:PRK10762 164 IMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRLKeiFEIC--DDVTVFRDGQFI 220
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
116-227 |
4.08e-08 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 53.48 E-value: 4.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 116 VDNAISYLGLDpyrkRFLDELSGGQRQRAFVAMVI-SQNTD--YILlDEP---LNNLDMRHAVSMMKRLRNaadeLGKTI 189
Cdd:TIGR00630 473 IDVGLDYLSLS----RAAGTLSGGEAQRIRLATQIgSGLTGvlYVL-DEPsigLHQRDNRRLINTLKRLRD----LGNTL 543
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1150389631 190 IMVMHDLNFAScYSDLIIALKE------GKLVFSGAPENVMKDE 227
Cdd:TIGR00630 544 IVVEHDEDTIR-AADYVIDIGPgagehgGEVVASGTPEEILANP 586
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
17-197 |
8.96e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 52.59 E-value: 8.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 17 IEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSILrqENtltarITVEDLV 96
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTGI--EN-----IELKGLM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 97 SfgrypyshGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILLDEPLNNLDMRHAVSMMK 176
Cdd:PRK13545 113 M--------GLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLD 184
|
170 180
....*....|....*....|.
gi 1150389631 177 RLrNAADELGKTIIMVMHDLN 197
Cdd:PRK13545 185 KM-NEFKEQGKTIFFISHSLS 204
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-167 |
9.51e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 52.71 E-value: 9.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 1 MIEISHVFKSYDDNS--IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKgADFAKRLS 78
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNI-SDVHQNMG 2015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 79 ILRQ----ENTLTARitvEDLVSFGRYpysHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNT 154
Cdd:TIGR01257 2016 YCPQfdaiDDLLTGR---EHLYLYARL---RGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCP 2089
|
170
....*....|...
gi 1150389631 155 DYILLDEPLNNLD 167
Cdd:TIGR01257 2090 PLVLLDEPTTGMD 2102
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
12-167 |
1.00e-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: 52.61 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 12 DDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPiTKGRITVDGIDVTKAKGADFAKRLSILRQENTLTARIT 91
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTF 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 92 VEDLVSFGRYpyshgvlTKEDKTFVDNAIsylGLDPYRKRFLDE-----------LSGGQRQRAFVAMVISQNTDYILLD 160
Cdd:TIGR01271 1309 RKNLDPYEQW-------SDEEIWKVAEEV---GLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLARSILSKAKILLLD 1378
|
....*..
gi 1150389631 161 EPLNNLD 167
Cdd:TIGR01271 1379 EPSAHLD 1385
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
129-196 |
1.00e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 52.03 E-value: 1.00e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1150389631 129 RKR---FLDELSGGQRQRAFVAMVISQNTDYILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDL 196
Cdd:PRK09473 152 RKRmkmYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDL 222
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
14-168 |
1.44e-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: 51.01 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 14 NSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGidvtkakgadfakRLSILRQENTLTARITVE 93
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 94 DL---VSFGRYPYSHGV----LTKEDKTFVDNAISYLGLDPYrkrfldELSGGQRQRAFVAMVISQNTDYILLDEPLNNL 166
Cdd:cd03291 117 NIifgVSYDEYRYKSVVkacqLEEDITKFPEKDNTVLGEGGI------TLSGGQRARISLARAVYKDADLYLLDSPFGYL 190
|
..
gi 1150389631 167 DM 168
Cdd:cd03291 191 DV 192
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
18-215 |
1.48e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 51.84 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 18 EDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADfAKRLSIL-----RQENTLTARITV 92
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRD-AIRAGIMlcpedRKAEGIIPVHSV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 93 EDLVSFG-RYPYSHGVLTKEDKTFVDNAISYLGL----DPYRKRFLDELSGGQRQRAFVAMVISQNTDYILLDEPLNNLD 167
Cdd:PRK11288 349 ADNINISaRRHHLRAGCLINNRWEAENADRFIRSlnikTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGID 428
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1150389631 168 MrHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLV 215
Cdd:PRK11288 429 V-GAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
17-226 |
1.99e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 50.58 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 17 IEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGidvtkakgadfakRLSILRQENTLTARITVEDLV 96
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-------------EVSVIAISAGLSGQLTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 97 SFGRypYSHGVLTKEDKTFVDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVISQNTDYILLDEPLNNLDMRHAVSMMK 176
Cdd:PRK13546 107 EFKM--LCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLD 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1150389631 177 RLRNaADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMKD 226
Cdd:PRK13546 185 KIYE-FKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
56-194 |
2.23e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.57 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 56 GRITVDGIDVTKAKGADFAKRLSILRQENTLTaRITVEDLVSFGRYPYSHGVLTKEDK-TFVDNAISYL------GLDPY 128
Cdd:PTZ00265 1277 GKILLDGVDICDYNLKDLRNLFSIVSQEPMLF-NMSIYENIKFGKEDATREDVKRACKfAAIDEFIESLpnkydtNVGPY 1355
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1150389631 129 RKrfldELSGGQRQRAFVAMVISQNTDYILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMH 194
Cdd:PTZ00265 1356 GK----SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH 1417
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-197 |
3.34e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.80 E-value: 3.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 2 IEISHVFKSYD---DNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITV-DGIDVTKAKGADFAKRL 77
Cdd:PTZ00265 383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 78 SILRQE-----NTLTARI-----TVEDLVSFGRYPYSHGVLTKEDK--------------TFVDNAISYLGLDPYRKRF- 132
Cdd:PTZ00265 463 GVVSQDpllfsNSIKNNIkyslySLKDLEALSNYYNEDGNDSQENKnkrnscrakcagdlNDMSNTTDSNELIEMRKNYq 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 133 ----------------------------------LDELSGGQRQRAFVAMVISQNTDYILLDEPLNNLDMRHAVSMMKRL 178
Cdd:PTZ00265 543 tikdsevvdvskkvlihdfvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
|
250
....*....|....*....
gi 1150389631 179 RNAADELGKTIIMVMHDLN 197
Cdd:PTZ00265 623 NNLKGNENRITIIIAHRLS 641
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
19-195 |
5.14e-07 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 49.18 E-value: 5.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 19 DLSLQIPKGGMVSIIGPNGAGKSTL----------------LTMISRLLPITKGRITVDGIDvtkakgaDFAKRLSILRQ 82
Cdd:cd03270 13 NVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryvesLSAYARQFLGQMDKPDVDSIE-------GLSPAIAIDQK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 83 ENTLTARITV---EDLVSFGRYPYSHGVLTKEDKTFVDNAISYLGLDpyrkRFLDELSGGQRQRAFVAMVISQNTDYIL- 158
Cdd:cd03270 86 TTSRNPRSTVgtvTEIYDYLRLLFARVGIRERLGFLVDVGLGYLTLS----RSAPTLSGGEAQRIRLATQIGSGLTGVLy 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1150389631 159 -LDEP---LNNLDMRHAVSMMKRLRNaadeLGKTIIMVMHD 195
Cdd:cd03270 162 vLDEPsigLHPRDNDRLIETLKRLRD----LGNTVLVVEHD 198
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
4-218 |
7.08e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.11 E-value: 7.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 4 ISHVFKSYDDNS--IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMIS----RLLPITKGRITVDGIDvtkakGADFAKRL 77
Cdd:TIGR00956 62 FRKLKKFRDTKTfdILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGIT-----PEEIKKHY 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 78 ---SILRQENTL-TARITVEDLVSFG---RYPYSHGV-LTKED--KTFVDNAISYLGLDPYRKR-----FLDELSGGQRQ 142
Cdd:TIGR00956 137 rgdVVYNAETDVhFPHLTVGETLDFAarcKTPQNRPDgVSREEyaKHIADVYMATYGLSHTRNTkvgndFVRGVSGGERK 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 143 RAFVAMVISQNTDYILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVM-------HDLnFascysDLIIALKEGKLV 215
Cdd:TIGR00956 217 RVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIyqcsqdaYEL-F-----DKVIVLYEGYQI 290
|
...
gi 1150389631 216 FSG 218
Cdd:TIGR00956 291 YFG 293
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
30-218 |
8.89e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.47 E-value: 8.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 30 VSIIGPNGAGKSTLLTMISRLLPITKGRItvdgidVTKAKgadfaKRLSILRQENTLTARITVEDLVSFGR-YPyshGVL 108
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTV------FRSAK-----VRMAVFSQHHVDGLDLSSNPLLYMMRcFP---GVP 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 109 TKEDKTFVDN--AISYLGLDPyrkrfLDELSGGQRQRAFVAMVISQNTDYILLDEPLNNLDMRHAVSMMKRLrnAADELG 186
Cdd:PLN03073 604 EQKLRAHLGSfgVTGNLALQP-----MYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGL--VLFQGG 676
|
170 180 190
....*....|....*....|....*....|...
gi 1150389631 187 ktIIMVMHDLNFASCYSDLIIALKEGKLV-FSG 218
Cdd:PLN03073 677 --VLMVSHDEHLISGSVDELWVVSEGKVTpFHG 707
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-67 |
8.96e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 48.48 E-value: 8.96e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1150389631 1 MIEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMIS--RLLPITKGRITVDGIDVTK 67
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAghPAYKILEGDILFKGESILD 75
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
114-240 |
1.15e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.44 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 114 TFVDNAISYLGLDpyrkRFLDELSGGQRQRAFVAMVISQNTDYI--LLDEP---LNNLDMRHAVSMMKRLRNAadelGKT 188
Cdd:PRK00635 459 ILIDLGLPYLTPE----RALATLSGGEQERTALAKHLGAELIGItyILDEPsigLHPQDTHKLINVIKKLRDQ----GNT 530
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1150389631 189 IIMVMHDLNFAScYSDLIIALKE------GKLVFSGAPEN-VMKDEILSAIY-----DIDIKVK 240
Cdd:PRK00635 531 VLLVEHDEQMIS-LADRIIDIGPgagifgGEVLFNGSPREfLAKSDSLTAKYlrqelTIPIPEK 593
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
12-207 |
2.15e-06 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 47.54 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 12 DDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPiTKGRITVDGIDVTKAKGADFAKRLSILRQENTLTARIT 91
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 92 VEDLVSFGRYpyshgvlTKEDKTFVDNAIsylGLDPYRKRFLDE-----------LSGGQRQRAFVAMVISQNTDYILLD 160
Cdd:cd03289 94 RKNLDPYGKW-------SDEEIWKVAEEV---GLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSVLSKAKILLLD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1150389631 161 EPLNNLDMRHAVSMMKRLRNAADelGKTIIMVMHDLN-FASCYSDLII 207
Cdd:cd03289 164 EPSAHLDPITYQVIRKTLKQAFA--DCTVILSEHRIEaMLECQRFLVI 209
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
14-194 |
2.99e-06 |
|
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.
Pssm-ID: 463892 [Multi-domain] Cd Length: 193 Bit Score: 46.61 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 14 NSIIEDLslqIPKGGMVSIIGPNGAGKSTLLTMISrlLPITKGRITVDGIDVTKA----------KGADFAKRLSILRQE 83
Cdd:pfam13481 23 RWLIKGL---LPAGGLGLLAGAPGTGKTTLALDLA--AAVATGKPWLGGPRVPEQgkvlyvsaegPADELRRRLRAAGAD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 84 NTLTARITVEDLVSFGRYPY--SHGVLTKEDKTFVDNAIsylgldpyrkrfldelsggqRQRAFVAMVISQNTDYILLDE 161
Cdd:pfam13481 98 LDLPARLLFLSLVESLPLFFldRGGPLLDADVDALEAAL--------------------EEVEDPDLVVIDPLARALGGD 157
|
170 180 190
....*....|....*....|....*....|...
gi 1150389631 162 PLNNLDMRHAVsmmKRLRNAADELGKTIIMVMH 194
Cdd:pfam13481 158 ENSNSDVGRLV---KALDRLARRTGATVLLVHH 187
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
8-198 |
3.10e-06 |
|
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: 46.45 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 8 FKSYDDNSIIEDLSlqipkgGMVSIIGPNGAGKSTLLTMIS-----RLLPITKGRITVDGIDVTKAKGADFAKRLSILRQ 82
Cdd:cd03240 9 IRSFHERSEIEFFS------PLTLIVGQNGAGKTTIIEALKyaltgELPPNSKGGAHDPKLIREGEVRAQVKLAFENANG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 83 EN-TLTARITVEDLVSFGRypyshgvltKEDktfvdnaISYLGLDPyRKRfldeLSGGQRQ------RAFVAMVISQNTD 155
Cdd:cd03240 83 KKyTITRSLAILENVIFCH---------QGE-------SNWPLLDM-RGR----CSGGEKVlasliiRLALAETFGSNCG 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1150389631 156 YILLDEPLNNLD-------MRHAVSMMKRLRNaadelgKTIIMVMHDLNF 198
Cdd:cd03240 142 ILALDEPTTNLDeenieesLAEIIEERKSQKN------FQLIVITHDEEL 185
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
16-214 |
3.96e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.47 E-value: 3.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 16 IIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMIsrllpitKGRITVDGIDVTKAkgADFAkrLSILRQENTLTARITVEDL 95
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALL-------KNEISADGGSYTFP--GNWQ--LAWVNQETPALPQPALEYV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 96 VSFGR--------------------YPYSHGVLTKEDK-TFVDNAISYL-GL---DPYRKRFLDELSGGQRQRAFVAMVI 150
Cdd:PRK10636 85 IDGDReyrqleaqlhdanerndghaIATIHGKLDAIDAwTIRSRAASLLhGLgfsNEQLERPVSDFSGGWRMRLNLAQAL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1150389631 151 SQNTDYILLDEPLNNLDMRHAVSMMKRLRNAADelgkTIIMVMHDLNFASCYSDLIIALKEGKL 214
Cdd:PRK10636 165 ICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG----TLILISHDRDFLDPIVDKIIHIEQQSL 224
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
8-199 |
1.72e-05 |
|
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: 43.89 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 8 FKSYDDNSIIEdlslqIPKGGMVSIIGPNGAGKSTLLTMISRLLPItkgritvdgidvtkaKGADFAKRLSILRQENTlt 87
Cdd:cd03227 7 FPSYFVPNDVT-----FGEGSLTIITGPNGSGKSTILDAIGLALGG---------------AQSATRRRSGVKAGCIV-- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 88 ARITVEDLVsfgrypyshgvltkedktfvdnaisylgldpyrkrFLDELSGGQRQRAFVAMVIS----QNTDYILLDEPL 163
Cdd:cd03227 65 AAVSAELIF-----------------------------------TRLQLSGGEKELSALALILAlaslKPRPLYILDEID 109
|
170 180 190
....*....|....*....|....*....|....*.
gi 1150389631 164 NNLDMRHAVSMMKRLRNAADElGKTIIMVMHDLNFA 199
Cdd:cd03227 110 RGLDPRDGQALAEAILEHLVK-GAQVIVITHLPELA 144
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
17-225 |
1.82e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 45.12 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 17 IEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLP----ITKGRITVDGIDVTKAK--------GAD----FAKRLSIL 80
Cdd:PRK11022 23 VDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQRISekerrnlvGAEvamiFQDPMTSL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 81 RQENTLTARITVEDLVSFGrypyshgvltKEDKTFVDNAISYLGL----DPYRKrfLD----ELSGGQRQRAFVAMVISQ 152
Cdd:PRK11022 103 NPCYTVGFQIMEAIKVHQG----------GNKKTRRQRAIDLLNQvgipDPASR--LDvyphQLSGGMSQRVMIAMAIAC 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1150389631 153 NTDYILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMK 225
Cdd:PRK11022 171 RPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFR 243
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-67 |
2.03e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 44.40 E-value: 2.03e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1150389631 1 MIEISHVFKSYDDNSIIEDLSLQIPKGGMVSIIGPNGAGKSTL-LTMISRL-LPITKGRITVDGIDVTK 67
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLsATLAGREdYEVTGGTVEFKGKDLLE 69
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
13-167 |
4.11e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 43.32 E-value: 4.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 13 DNSIIEDLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKgadfAKRLSILRQENTLTARITV 92
Cdd:PRK13541 12 EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA----KPYCTYIGHNLGLKLEMTV 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1150389631 93 EDLVSFGRYPYShgvltkeDKTFVDNAISYLGLDpyrkRFLDE----LSGGQRQRAFVAMVISQNTDYILLDEPLNNLD 167
Cdd:PRK13541 88 FENLKFWSEIYN-------SAETLYAAIHYFKLH----DLLDEkcysLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
16-194 |
4.51e-05 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 43.74 E-value: 4.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 16 IIEDLslqIPKGGMVSIIGPNGAGKSTLLTMISrlLPITKGRiTVDGIDVTKAK---------GADFAKRLSILRQENTL 86
Cdd:COG3598 5 LVPGL---LPEGGVTLLAGPPGTGKSFLALQLA--AAVAAGG-PWLGRRVPPGKvlylaaeddRGELRRRLKALGADLGL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 87 TARITVEDLvsfgrypyshgvltkedktFVDNAISYLGLDPYRKRFLDELsggqRQRAFVAMVISQNTDYILLDEPLNNl 166
Cdd:COG3598 79 PFADLDGRL-------------------RLLSLAGDLDDTDDLEALERAI----EEEGPDLVVIDPLARVFGGDENDAE- 134
|
170 180
....*....|....*....|....*...
gi 1150389631 167 DMRHAVSMMKRLrnaADELGKTIIMVMH 194
Cdd:COG3598 135 EMRAFLNPLDRL---AERTGAAVLLVHH 159
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
136-231 |
9.40e-05 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 43.27 E-value: 9.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 136 LSGGQRQRAFVAMVISQNTDYILLDEPLNNLDMrHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLV 215
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV-GAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
90
....*....|....*.
gi 1150389631 216 FSGAPENVMKDEILSA 231
Cdd:TIGR02633 483 GDFVNHALTQEQVLAA 498
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
26-198 |
1.02e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 41.59 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 26 KGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVdgIDVTKAKGADFAKRLSILRQENTLtaritvedlvsfgrypysh 105
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY--IDGEDILEEVLDQLLLIIVGGKKA------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 106 gvltkedktfvdnaisylgldpyrkrfldELSGGQRQRAFVAMVISQNTDYILLDEPLNNLDMRHAVSMMKRLRNAAD-- 183
Cdd:smart00382 60 -----------------------------SGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLll 110
|
170
....*....|....*...
gi 1150389631 184 ---ELGKTIIMVMHDLNF 198
Cdd:smart00382 111 lksEKNLTVILTTNDEKD 128
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
20-224 |
1.54e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 42.84 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 20 LSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGADFAKRLSILRQENTL---TARITVEdlv 96
Cdd:PTZ00243 1329 VSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLfdgTVRQNVD--- 1405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 97 sfgryPYSHGVLTKedktfVDNAISYLGLdpyRKRFLDELSG--------------GQRQRAFVA-MVISQNTDYILLDE 161
Cdd:PTZ00243 1406 -----PFLEASSAE-----VWAALELVGL---RERVASESEGidsrvleggsnysvGQRQLMCMArALLKKGSGFILMDE 1472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 162 PLNNLDmrHAV------SMMKRLRNaadelgKTIIMVMHDLNFASCYsDLIIALKEGKLVFSGAP-ENVM 224
Cdd:PTZ00243 1473 ATANID--PALdrqiqaTVMSAFSA------YTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPrELVM 1533
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
24-51 |
1.64e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 38.74 E-value: 1.64e-04
10 20
....*....|....*....|....*...
gi 1150389631 24 IPKGGMVSIIGPNGAGKSTLLTMISRLL 51
Cdd:pfam13555 19 IDPRGNTLLTGPSGSGKSTLLDAIQTLL 46
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
121-227 |
1.91e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 42.32 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 121 SYLGLDpyrkRFLDELSGGQRQRafvamvI---SQ------NTDYILlDEPLNNL---DMRHAVSMMKRLRNaadeLGKT 188
Cdd:COG0178 475 DYLTLD----RSAGTLSGGEAQR------IrlaTQigsglvGVLYVL-DEPSIGLhqrDNDRLIETLKRLRD----LGNT 539
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1150389631 189 IIMVMHD----LNfascySDLIIAL------KEGKLVFSGAPENVMKDE 227
Cdd:COG0178 540 VIVVEHDedtiRA-----ADYIIDIgpgageHGGEVVAQGTPEEILKNP 583
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
16-195 |
2.31e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.03 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 16 IIEDLSLQIPKGGMVSIIGPNGAGKSTLLtmisrllpitkgRItVDGID------VTKAKGAdfakRLSILRQE----NT 85
Cdd:PRK11819 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLL------------RI-MAGVDkefegeARPAPGI----KVGYLPQEpqldPE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 86 LTARITVEDlvsfgrypyshGVltKEDKTFVD--NAIS--YLGLDPYRKRFLDE-------------------------- 135
Cdd:PRK11819 85 KTVRENVEE-----------GV--AEVKAALDrfNEIYaaYAEPDADFDALAAEqgelqeiidaadawdldsqleiamda 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1150389631 136 ------------LSGGQRQRafVAM--VISQNTDYILLDEPLNNLDMrHAVSMMKR-LRNAAdelGkTIIMVMHD 195
Cdd:PRK11819 152 lrcppwdakvtkLSGGERRR--VALcrLLLEKPDMLLLDEPTNHLDA-ESVAWLEQfLHDYP---G-TVVAVTHD 219
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
32-161 |
3.86e-04 |
|
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213243 [Multi-domain] Cd Length: 198 Bit Score: 40.27 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 32 IIGPNGAGKSTLLTMISRLLpitkGritvdgidvTKAKGADFAKRLSILRQENTLTARITVEdLVSFGRYPYSHGVLTKe 111
Cdd:cd03276 26 IVGNNGSGKSAILTALTIGL----G---------GKASDTNRGSSLKDLIKDGESSAKITVT-LKNQGLDANPLCVLSQ- 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1150389631 112 dktfvDNAISYLGLDPYRKRFLDELSGGQRQRAFVAMVIS--QNTD--YILLDE 161
Cdd:cd03276 91 -----DMARSFLTSNKAAVRDVKTLSGGERSFSTVCLLLSlwEVMEspFRCLDE 139
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
17-58 |
4.85e-04 |
|
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: 41.15 E-value: 4.85e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1150389631 17 IEDLSLQIPKGGMVSIIGPNGAGKSTLLTMIsrLLPITKGRI 58
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLINDT--LYPALANRL 663
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
136-227 |
8.16e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.39 E-value: 8.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 136 LSGGQRQR----AFVAMVISQNTDYIlLDEPLNNL---DMRHAVSMMKRLRnaadELGKTIIMVMHDLNFASCySDLIIA 208
Cdd:COG0178 827 LSGGEAQRvklaSELSKRSTGKTLYI-LDEPTTGLhfhDIRKLLEVLHRLV----DKGNTVVVIEHNLDVIKT-ADWIID 900
|
90 100
....*....|....*....|....*
gi 1150389631 209 L------KEGKLVFSGAPENVMKDE 227
Cdd:COG0178 901 LgpeggdGGGEIVAEGTPEEVAKVK 925
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
137-215 |
9.93e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.23 E-value: 9.93e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1150389631 137 SGGQRQRAFVAMVISQNTDYILLDEPLNNLDMrHAVSMmkrLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKLV 215
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDL-HAVLW---LETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKLV 420
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
2-57 |
1.08e-03 |
|
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: 39.60 E-value: 1.08e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1150389631 2 IEISHvFKSyddnsiIEDLSLQIPKGGMVsIIGPNGAGKSTLLTMISRLLPITKGR 57
Cdd:COG3593 6 IKIKN-FRS------IKDLSIELSDDLTV-LVGENNSGKSSILEALRLLLGPSSSR 53
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
2-47 |
1.11e-03 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 38.99 E-value: 1.11e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1150389631 2 IEISHvFKSYDDNSIIEdlslqIPKGgMVSIIGPNGAGKSTLLTMI 47
Cdd:cd03278 4 LELKG-FKSFADKTTIP-----FPPG-LTAIVGPNGSGKSNIIDAI 42
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
8-48 |
1.19e-03 |
|
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213242 [Multi-domain] Cd Length: 247 Bit Score: 39.09 E-value: 1.19e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1150389631 8 FKSYDDNSIIEdlslqiPKGGMVSIIGPNGAGKSTLLTMIS 48
Cdd:cd03275 9 FKSYKGRHVIG------PFDRFTCIIGPNGSGKSNLMDAIS 43
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
135-224 |
1.83e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 39.02 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 135 ELSGGQRQRAFVAMVISQNTDYILLDEPLNNLDMRHAVSMMKRLRNAADELGKTIIMVMHDLNFASCYSDLIIALKEGKL 214
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQT 237
|
90
....*....|
gi 1150389631 215 VFSGAPENVM 224
Cdd:PRK15093 238 VETAPSKELV 247
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
2-44 |
1.97e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 38.25 E-value: 1.97e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1150389631 2 IEISHvFKSYDDNSIieDLSlqipkGGMVSIIGPNGAGKSTLL 44
Cdd:pfam13476 1 LTIEN-FRSFRDQTI--DFS-----KGLTLITGPNGSGKTTIL 35
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2-48 |
2.38e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 39.18 E-value: 2.38e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1150389631 2 IEISHvFKSYDDnSIIEDLSlqipkGGMVSIIGPNGAGKSTLLTMIS 48
Cdd:pfam02463 5 IEIEG-FKSYAK-TVILPFS-----PGFTAIVGPNGSGKSNILDAIL 44
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
19-229 |
2.49e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 38.88 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 19 DLSLQIPKGGMVSIIGPNGAGKSTLLTMISRLLPITKGRITVDGIDVTKAKGAD-FAKRLSIL---RQENTLtariTVED 94
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLpedRQSSGL----YLDA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 95 LVSFGRYPYSHGVLTKEDKTFVDNAIsylgLDPYRK----RFLDE------LSGGQRQRAFVAMVISQNTDYILLDEPLN 164
Cdd:PRK15439 357 PLAWNVCALTHNRRGFWIKPARENAV----LERYRRalniKFNHAeqaartLSGGNQQKVLIAKCLEASPQLLIVDEPTR 432
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1150389631 165 NLDMRHAVSMMKRLRNAADElGKTIIMVMHDLNFASCYSDLIIALKEGKLVFSGAPENVMKDEIL 229
Cdd:PRK15439 433 GVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAINVDTIM 496
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
135-225 |
3.46e-03 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 37.96 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150389631 135 ELSGGQRQRAFVAMVISQNTDYILLDEPLNNLDMRHAVSMMkRLRNAADELGKT-IIMVMHDLNFASCYSDLIIALKEGK 213
Cdd:COG4170 158 ELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIF-RLLARLNQLQGTsILLISHDLESISQWADTITVLYCGQ 236
|
90
....*....|..
gi 1150389631 214 LVFSGAPENVMK 225
Cdd:COG4170 237 TVESGPTEQILK 248
|
|
| PulE-GspE-like |
cd01129 |
PulE-GspE family; PulE and General secretory pathway protein GspE are ATPases of the type II ... |
28-82 |
3.66e-03 |
|
PulE-GspE family; PulE and General secretory pathway protein GspE are ATPases of the type II secretory pathway, the main terminal branch of the general secretory pathway (GSP). PulE is a cytoplasmic protein of the GSP, which contains an ATP binding site and a tetracysteine motif. This subgroup also includes PilB, a type IV pilus assembly ATPase, DotB, an ATPase of the type IVb secretion system, also known as the dot/icm system, Escherichia coli IncI plasmid-encoded conjugative transfer ATPase TraJ, and HofB.
Pssm-ID: 410873 [Multi-domain] Cd Length: 159 Bit Score: 37.08 E-value: 3.66e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1150389631 28 GMVSIIGPNGAGKSTLLTMISRLLPITKGRI---------TVDGI---DVTKAKGADFAKRL-SILRQ 82
Cdd:cd01129 12 GLILVTGPTGSGKTTTLYAMLRELNGPERNIitiedpveyQIPGInqsQVNEKIGLTFADALrAILRQ 79
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
158-223 |
3.79e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 38.66 E-value: 3.79e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1150389631 158 LLDEPLNNLDMRHAVSMMKRLRNAADeLGKTIIMVMHDLNFaSCYSDLIIAL------KEGKLVFSGAPENV 223
Cdd:PRK00635 1725 LLDEIATSLDNQQKSALLVQLRTLVS-LGHSVIYIDHDPAL-LKQADYLIEMgpgsgkTGGKILFSGPPKDI 1794
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-44 |
6.98e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 36.53 E-value: 6.98e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1150389631 2 IEISHvFKSYDDNSIIeDLSlqipkGGMVSIIGPNGAGKSTLL 44
Cdd:COG0419 5 LRLEN-FRSYRDTETI-DFD-----DGLNLIVGPNGAGKSTIL 40
|
|
| |
