|
Name |
Accession |
Description |
Interval |
E-value |
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-255 |
3.99e-141 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 396.06 E-value: 3.99e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAVL 80
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 81 PQVSSLGFSFRVEEVVGMGRMPHGTGQRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQLW-PGEEGST 159
Cdd:PRK13548 82 PQHSSLSFPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQLWePDGPPRW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 160 LLLDEPTSMLDPLHQHTTLEAVRRFA-DCGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPEAALTPAALKAVYGID 238
Cdd:PRK13548 162 LLLDEPTSALDLAHQHHVLRLARQLAhERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPETLRRVYGAD 241
|
250
....*....|....*..
gi 939342971 239 VLVQAHPERGHPLIITR 255
Cdd:PRK13548 242 VLVQPHPETGAPLVLPR 258
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-255 |
3.70e-137 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 386.01 E-value: 3.70e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAVL 80
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 81 PQVSSLGFSFRVEEVVGMGRMPHGTGQRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQLWPGEEGST- 159
Cdd:COG4559 81 PQHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQLWEPVDGGPr 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 160 -LLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPEAALTPAALKAVYGID 238
Cdd:COG4559 161 wLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELLERVYGAD 240
|
250
....*....|....*..
gi 939342971 239 VLVQAHPERGHPLIITR 255
Cdd:COG4559 241 LRVLAHPEGGCPQVLPR 257
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-253 |
1.21e-110 |
|
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: 318.91 E-value: 1.21e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAVL 80
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 81 PQVSSLGFSFRVEEVVGMGRMPH----GTGQRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQlwpgeE 156
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGRYPHlglfGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQ-----E 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 157 GSTLLLDEPTSMLDPLHQHTTLEAVRRFA-DCGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPEAALTPAALKAVY 235
Cdd:COG1120 156 PPLLLLDEPTSHLDLAHQLEVLELLRRLArERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVY 235
|
250
....*....|....*...
gi 939342971 236 GIDVLVQAHPERGHPLII 253
Cdd:COG1120 236 GVEARVIEDPVTGRPLVL 253
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-244 |
6.86e-72 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 219.96 E-value: 6.86e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLAdwagqERARRLAVL 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR-----RARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 81 PQVSSLGFSF--RVEEVVGMGRMPH----GTGQRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQlwpg 154
Cdd:COG1121 81 PQRAEVDWDFpiTVRDVVLMGRYGRrglfRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQ---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 155 eEGSTLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGRcHAFATPEAALTPAALKAV 234
Cdd:COG1121 157 -DPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGL-VAHGPPEEVLTPENLSRA 234
|
250
....*....|
gi 939342971 235 YGIDVLVQAH 244
Cdd:COG1121 235 YGGPVALLAH 244
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
4-219 |
2.73e-71 |
|
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: 216.15 E-value: 2.73e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 4 VEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAVLPQv 83
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 84 sslgfsfrveevvgmgrmphgtgqrrdaeiveaALRAADAWHLVERSYLALSGGERQRVHLARVLAQlwpgeEGSTLLLD 163
Cdd:cd03214 81 ---------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQ-----EPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 939342971 164 EPTSMLDPLHQHTTLEAVRRFAD-CGAAVLVILHDLNLAARYCDRILLLEQGRCHAF 219
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLAReRGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
2-252 |
3.41e-71 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 218.92 E-value: 3.41e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAVLP 81
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVDLHGLSRRARARRVALVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 82 QVSSLGFSFRVEEVVGMGRMPH----GTGQRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQlwpgeEG 157
Cdd:TIGR03873 82 QDSDTAVPLTVRDVVALGRIPHrslwAGDSPHDAAVVDRALARTELSHLADRDMSTLSGGERQRVHVARALAQ-----EP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 158 STLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPEAALTPAALKAVYGI 237
Cdd:TIGR03873 157 KLLLLDEPTNHLDVRAQLETLALVRELAATGVTVVAALHDLNLAASYCDHVVVLDGGRVVAAGPPREVLTPALIRAVYGV 236
|
250
....*....|....*
gi 939342971 238 DVLVQAHPERGHPLI 252
Cdd:TIGR03873 237 DATVLTHPDTGRPII 251
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-254 |
1.66e-70 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 221.64 E-value: 1.66e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAVL 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 81 PQVSSLGFSFRVEEVVGMGRMPH----GTGQRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQLWPgee 156
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVEMGRTPHrsrfDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATP--- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 157 gsTLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPEAALTPAALKAVYG 236
Cdd:PRK09536 160 --VLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFD 237
|
250
....*....|....*...
gi 939342971 237 IDVLVQAHPERGHPLIIT 254
Cdd:PRK09536 238 ARTAVGTDPATGAPTVTP 255
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-253 |
6.24e-70 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 215.33 E-value: 6.24e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAVL 80
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 81 PQVSSLGFSFRVEEVVGMGRMPHGTGQ--RRDAEIVEAALRAADAWHLVERsYL-ALSGGERQRVHLARVLAQlwpgeeg 157
Cdd:COG4604 81 RQENHINSRLTVRELVAFGRFPYSKGRltAEDREIIDEAIAYLDLEDLADR-YLdELSGGQRQRAFIAMVLAQ------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 158 ST--LLLDEPTSMLDPLHQHTTLEAVRRFAD-CGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPEAALTPAALKAV 234
Cdd:COG4604 153 DTdyVLLDEPLNNLDMKHSVQMMKLLRRLADeLGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEVLSDI 232
|
250
....*....|....*....
gi 939342971 235 YGIDVLVQAHPerGHPLII 253
Cdd:COG4604 233 YDTDIEVEEID--GKRICV 249
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-255 |
5.13e-65 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 202.94 E-value: 5.13e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAVL 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 81 PQVSSLGFSFRVEEVVGMGRMPH----GTGQRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQLWPgee 156
Cdd:PRK11231 82 PQHHLTPEGITVRELVAYGRSPWlslwGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTP--- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 157 gsTLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPEAALTPAALKAVYG 236
Cdd:PRK11231 159 --VVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVFD 236
|
250
....*....|....*....
gi 939342971 237 IDVLVQAHPERGHPLIITR 255
Cdd:PRK11231 237 VEAEIHPEPVSGTPMCVVR 255
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-253 |
4.24e-64 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 201.21 E-value: 4.24e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGEL--------APDRGRVTLQGRPLADWAGQE 72
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggaprgARVTGDVTLNGEPLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 73 RARRLAVLPQVSSLGFSFRVEEVVGMGRMPH----GTGQRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVL 148
Cdd:PRK13547 81 LARLRAVLPQAAQPAFAFSAREIVLLGRYPHarraGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 149 AQLWPGEEGST----LLLDEPTSMLDPLHQHTTLEAVRRFA-DCGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPE 223
Cdd:PRK13547 161 AQLWPPHDAAQppryLLLDEPTAALDLAHQHRLLDTVRRLArDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPA 240
|
250 260 270
....*....|....*....|....*....|
gi 939342971 224 AALTPAALKAVYGIDVLVQAHPERGHPLII 253
Cdd:PRK13547 241 DVLTPAHIARCYGFAVRLVDAGDGVPPVIV 270
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-214 |
9.26e-61 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 190.44 E-value: 9.26e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 3 HVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADwagqeRARRLAVLPQ 82
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK-----ERKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 83 VSSLGFSF--RVEEVVGMGRMPHGTGQRR----DAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQlwpgeE 156
Cdd:cd03235 76 RRSIDRDFpiSVRDVVLMGLYGHKGLFRRlskaDKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQ-----D 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 939342971 157 GSTLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQG 214
Cdd:cd03235 151 PDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
20-255 |
1.54e-53 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 173.49 E-value: 1.54e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 20 IHLQLPPGQVVGVLGPNGAGKSSLLSVLCGeLAPDRGRVTLQGRPLADWAGQERARRLAVLPQVSSLGFSFRVEEVVGMG 99
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNGRPLSDWSAAELARHRAYLSQQQSPPFAMPVFQYLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 100 RMPHGTGQRRDAEIVE--AALRAADawhLVERSYLALSGGERQRVHLARVLAQLWPG--EEGSTLLLDEPTSMLDPLHQH 175
Cdd:COG4138 94 QPAGASSEAVEQLLAQlaEALGLED---KLSRPLTQLSGGEWQRVRLAAVLLQVWPTinPEGQLLLLDEPMNSLDVAQQA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 176 TTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPEAALTPAALKAVYGIDvlVQAHPERGHPLIITR 255
Cdd:COG4138 171 ALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVFGVK--FRRLEVEGHRWLIPT 248
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-227 |
2.32e-53 |
|
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: 172.13 E-value: 2.32e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLR-RGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAVL 80
Cdd:COG1122 1 IELENLSFSyPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 81 PQ--VSSLgFSFRVEEVVGMGRMPHGTGQRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQlwpgeEGS 158
Cdd:COG1122 81 FQnpDDQL-FAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAM-----EPE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 939342971 159 TLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPEAALT 227
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFS 223
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
4-215 |
2.66e-50 |
|
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: 163.79 E-value: 2.66e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 4 VEGLYLRRGSNE--VLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAVLP 81
Cdd:cd03225 2 LKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 82 QVSSLGFSF-RVEEVVGMGRMPHGTGQRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAqlwpgEEGSTL 160
Cdd:cd03225 82 QNPDDQFFGpTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLA-----MDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 939342971 161 LLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGR 215
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-235 |
6.95e-49 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 161.00 E-value: 6.95e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERaRRLAVLP 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVR-RRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 82 QVSSLGFSFRVEEVVG-MGRMpHGTGQRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLA---QLwpgeeg 157
Cdd:COG1131 80 QEPALYPDLTVRENLRfFARL-YGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLhdpEL------ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 939342971 158 stLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPEaALTPAALKAVY 235
Cdd:COG1131 153 --LILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPD-ELKARLLEDVF 227
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
16-251 |
1.95e-48 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 160.72 E-value: 1.95e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 16 VLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAVLPQVSSLGFSFRVEEV 95
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGMTVREL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 96 VGMGRMP-HGTGQR---RDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQlwpgeEGSTLLLDEPTSMLDP 171
Cdd:PRK10575 106 VAIGRYPwHGALGRfgaADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQ-----DSRCLLLDEPTSALDI 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 172 LHQHTTLEAVRRFA-DCGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPEAALTPAALKAVYGIDVLVQAHPERGHP 250
Cdd:PRK10575 181 AHQVDVLALVHRLSqERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIYGIPMGILPHPAGAAP 260
|
.
gi 939342971 251 L 251
Cdd:PRK10575 261 V 261
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-253 |
1.59e-46 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 155.91 E-value: 1.59e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAVLP 81
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 82 QVSSLGFSFRVEEVVGMGRMPH----GTGQRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQlwpgeEG 157
Cdd:PRK10253 88 QNATTPGDITVQELVARGRYPHqplfTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQ-----ET 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 158 STLLLDEPTSMLDPLHQHTTLEAVRRF-ADCGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPEAALTPAALKAVYG 236
Cdd:PRK10253 163 AIMLLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYG 242
|
250
....*....|....*..
gi 939342971 237 IDVLVQAHPERGHPLII 253
Cdd:PRK10253 243 LRCMIIDDPVAGTPLVV 259
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-224 |
6.18e-46 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 153.47 E-value: 6.18e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADwAGQERARRLAVL 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK-EPREARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 81 PQVSSLGFSFRVEEVVGMGRMPHGTGQRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQlwpgeEGSTL 160
Cdd:COG4555 80 PDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVH-----DPKVL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 939342971 161 LLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPEA 224
Cdd:COG4555 155 LLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDE 218
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-215 |
8.63e-46 |
|
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: 150.47 E-value: 8.63e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 3 HVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAVLPQ 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 83 vsslgfsfrveevvgmgrmphgtgqrrdaeiveaalraadawhlversylaLSGGERQRVHLARVLAQlwpgeEGSTLLL 162
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLL-----NPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 939342971 163 DEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGR 215
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-215 |
3.30e-45 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 149.47 E-value: 3.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERaRRLAVLP 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVK-RRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 82 QVSSLGFSFRVEEvvgmgrmphgtgqrrdaeiveaalraadawhlversYLALSGGERQRVHLARVL---AQLwpgeegs 158
Cdd:cd03230 80 EEPSLYENLTVRE------------------------------------NLKLSGGMKQRLALAQALlhdPEL------- 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 939342971 159 tLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGR 215
Cdd:cd03230 117 -LILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-236 |
2.05e-44 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 149.82 E-value: 2.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLR-RGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERA---RR 76
Cdd:COG3638 2 MLELRNLSKRyPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRrlrRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 77 LAVLPQ----VSSLgfsfRVEEVVGMGRMPHGTGQR------RDAEIvEAALRAADAWHLVERSYL---ALSGGERQRVH 143
Cdd:COG3638 82 IGMIFQqfnlVPRL----SVLTNVLAGRLGRTSTWRsllglfPPEDR-ERALEALERVGLADKAYQradQLSGGQQQRVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 144 LARVLAQlwpgeEGSTLLLDEPTSMLDPLHQHTTLEAVRRFA-DCGAAVLVILHDLNLAARYCDRILLLEQGRChAFATP 222
Cdd:COG3638 157 IARALVQ-----EPKLILADEPVASLDPKTARQVMDLLRRIArEDGITVVVNLHQVDLARRYADRIIGLRDGRV-VFDGP 230
|
250
....*....|....
gi 939342971 223 EAALTPAALKAVYG 236
Cdd:COG3638 231 PAELTDAVLREIYG 244
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-215 |
3.61e-43 |
|
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: 146.49 E-value: 3.61e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLRRGS----NEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARR 76
Cdd:COG1124 1 MLEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 77 LAVLPQ--VSSLGFSFRVEEVVGMGRMPHGTGQRRdaEIVEAALRAADawhlVERSYL-----ALSGGERQRVHLARVLA 149
Cdd:COG1124 81 VQMVFQdpYASLHPRHTVDRILAEPLRIHGLPDRE--ERIAELLEQVG----LPPSFLdryphQLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 939342971 150 QlwpgeEGSTLLLDEPTSMLDPLHQHTTLEAVRRF-ADCGAAVLVILHDLNLAARYCDRILLLEQGR 215
Cdd:COG1124 155 L-----EPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGR 216
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-238 |
1.47e-42 |
|
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: 151.21 E-value: 1.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGL---YLRRGSNEV--LHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQER-- 73
Cdd:COG1123 260 LLEVRNLskrYPVRGKGGVraVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLre 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 74 -ARRLAVLPQ--VSSLGFSFRVEEVVGMGRMPHGTGQRRDA-EIVEAALRAA--DAWHLvERSYLALSGGERQRVHLARV 147
Cdd:COG1123 340 lRRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLLSRAERrERVAELLERVglPPDLA-DRYPHELSGGQRQRVAIARA 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 148 LAQlwpgeEGSTLLLDEPTSMLDPLHQHTTLEAVRRFAD-CGAAVLVILHDLNLAARYCDRILLLEQGRC-------HAF 219
Cdd:COG1123 419 LAL-----EPKLLILDEPTSALDVSVQAQILNLLRDLQReLGLTYLFISHDLAVVRYIADRVAVMYDGRIvedgpteEVF 493
|
250
....*....|....*....
gi 939342971 220 ATPEAALTPAALKAVYGID 238
Cdd:COG1123 494 ANPQHPYTRALLAAVPSLD 512
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-224 |
5.91e-42 |
|
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: 142.96 E-value: 5.91e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARR-LAVL 80
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 81 PQVSSLGFSFRVEEVVGMGRMPHGTG-------QRRDAEIVEAALRAADAWHLVERSYL---ALSGGERQRVHLARVLAQ 150
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAQARTGSglllaraRREEREARERAEELLERVGLADLADRpagELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 939342971 151 lwpgeEGSTLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPEA 224
Cdd:cd03219 161 -----DPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDE 229
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-215 |
6.62e-42 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 142.26 E-value: 6.62e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAVLP 81
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 82 QVSSLgFSFRVEEVvgMGRMPHGTGQRRDAEIVEAALRAAD-AWHLVERSYLALSGGERQRVHLARVLaQLWPgeegSTL 160
Cdd:COG4619 81 QEPAL-WGGTVRDN--LPFPFQLRERKFDRERALELLERLGlPPDILDKPVERLSGGERQRLALIRAL-LLQP----DVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 939342971 161 LLDEPTSMLDPLHQHTTLEAVRRF-ADCGAAVLVILHDLNLAARYCDRILLLEQGR 215
Cdd:COG4619 153 LLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
23-255 |
2.89e-41 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 141.61 E-value: 2.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 23 QLPPGQVVGVLGPNGAGKSSLLSVLCGeLAPDRGRVTLQGRPLADWAGQERARRLAVLPQVSSLGFSFRVEEVVGMGRMP 102
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFAMPVFQYLTLHQPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 103 HG-TGQRRDA-EIVEAALRAADawhLVERSYLALSGGERQRVHLARVLAQLWP--GEEGSTLLLDEPTSMLDPLHQHTTL 178
Cdd:PRK03695 97 KTrTEAVASAlNEVAEALGLDD---KLGRSVNQLSGGEWQRVRLAAVVLQVWPdiNPAGQLLLLDEPMNSLDVAQQAALD 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 939342971 179 EAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPEAALTPAALKAVYGIDvlVQAHPERGHPLIITR 255
Cdd:PRK03695 174 RLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVFGVN--FRRLDVEGHPMLIST 248
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
12-226 |
1.29e-40 |
|
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: 146.83 E-value: 1.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 12 GSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAVLPQVSSLgFSFR 91
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYL-FAGT 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 92 VEEVVGMGRmPHGTgqrrDAEIvEAALRAADAWHLVER-----------SYLALSGGERQRVHLARVLAQlwpgeEGSTL 160
Cdd:COG4988 427 IRENLRLGR-PDAS----DEEL-EAALEAAGLDEFVAAlpdgldtplgeGGRGLSGGQAQRLALARALLR-----DAPLL 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 939342971 161 LLDEPTSMLDPLHQHTTLEAVRRFADcGAAVLVILHDLNLAARyCDRILLLEQGRCHAFATPEAAL 226
Cdd:COG4988 496 LLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELL 559
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-215 |
1.89e-40 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 137.13 E-value: 1.89e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLRRGSN--EVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAV 79
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 80 LPQVSSLgFSFRVEEVVgmgrmphgtgqrrdaeiveaalraadawhlversylaLSGGERQRVHLARVLAQlwpgeEGST 159
Cdd:cd03228 81 VPQDPFL-FSGTIRENI-------------------------------------LSGGQRQRIAIARALLR-----DPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 939342971 160 LLLDEPTSMLDPLHQHTTLEAVRRFAdCGAAVLVILHDLNLaARYCDRILLLEQGR 215
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALA-KGKTVIVIAHRLST-IRDADRIIVLDDGR 171
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-223 |
2.70e-40 |
|
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: 138.47 E-value: 2.70e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 4 VEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCG-----ELAPDRGRVTLQGRPLADWAGQ--ERARR 76
Cdd:cd03260 3 LRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDIYDLDVDvlELRRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 77 LAVLPQVSSLgFSFRVEEVVGMGRMPHGTGQRRD-AEIVEAALRAADAWHLVER--SYLALSGGERQRVHLARVLAQlwp 153
Cdd:cd03260 83 VGMVFQKPNP-FPGSIYDNVAYGLRLHGIKLKEElDERVEEALRKAALWDEVKDrlHALGLSGGQQQRLCLARALAN--- 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 154 geEGSTLLLDEPTSMLDPLHQHTTLEAVRRFADcGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPE 223
Cdd:cd03260 159 --EPEVLLLDEPTSALDPISTAKIEELIAELKK-EYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTE 225
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-235 |
5.05e-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: 5.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARR-LAV 79
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLgIAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 80 LPQVSSLGFSFRVEEVVGMGRMPHGTG------------QRRDAEIVEAALRAADAWHLVERSYL---ALSGGERQRVHL 144
Cdd:COG0411 84 TFQNPRLFPELTVLENVLVAAHARLGRgllaallrlpraRREEREARERAEELLERVGLADRADEpagNLSYGQQRRLEI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 145 ARVLAQlwpgeEGSTLLLDEPTSMLDPLHQHTTLEAVRRFADC-GAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPE 223
Cdd:COG0411 164 ARALAT-----EPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPA 238
|
250
....*....|..
gi 939342971 224 AALTPAALKAVY 235
Cdd:COG0411 239 EVRADPRVIEAY 250
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-215 |
9.01e-40 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 137.25 E-value: 9.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGL----YLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQ---ER 73
Cdd:cd03257 1 LLEVKNLsvsfPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRlrkIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 74 ARRLAVLPQ--VSSLGFSFRVEEVVGMGRMPHGTGqRRDAEIVEAALRAADAWHLVER---SY-LALSGGERQRVHLARV 147
Cdd:cd03257 81 RKEIQMVFQdpMSSLNPRMTIGEQIAEPLRIHGKL-SKKEARKEAVLLLLVGVGLPEEvlnRYpHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 939342971 148 LAQlwpgeEGSTLLLDEPTSMLDPLHQHTTLEAVRRFAD-CGAAVLVILHDLNLAARYCDRILLLEQGR 215
Cdd:cd03257 160 LAL-----NPKLLIADEPTSALDVSVQAQILDLLKKLQEeLGLTLLFITHDLGVVAKIADRVAVMYAGK 223
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-252 |
3.75e-39 |
|
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: 141.96 E-value: 3.75e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGL--YLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPD---RGRVTLQGRPLADWAGQERAR 75
Cdd:COG1123 4 LLEVRDLsvRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 76 RLAVLPQ--VSSLgFSFRVEEVVGMGRMPHGTGQRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQlwp 153
Cdd:COG1123 84 RIGMVFQdpMTQL-NPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL--- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 154 geEGSTLLLDEPTSMLDPLHQHTTLEAVRRF-ADCGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPEAALT-PAAL 231
Cdd:COG1123 160 --DPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAaPQAL 237
|
250 260
....*....|....*....|....
gi 939342971 232 KAVYGID---VLVQAHPERGHPLI 252
Cdd:COG1123 238 AAVPRLGaarGRAAPAAAAAEPLL 261
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-214 |
3.94e-39 |
|
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: 135.08 E-value: 3.94e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 3 HVEGLYLR-RGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWagqERARRLAVLP 81
Cdd:cd03226 1 RIENISFSyKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK---ERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 82 Q-VSSLGFSFRVEEVVGMGRMPHGtgqrRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQlwpgeEGSTL 160
Cdd:cd03226 78 QdVDYQLFTDSVREELLLGLKELD----AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLS-----GKDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 939342971 161 LLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQG 214
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-227 |
5.37e-39 |
|
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: 135.49 E-value: 5.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERA---RRL 77
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelrRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 78 AVLPQVSSLgF-SFRVEEVVGMG-RMpHGTGQRRDA-EIVEAALRA---ADAWHLversYLA-LSGGERQRVHLARVLA- 149
Cdd:COG1127 85 GMLFQGGAL-FdSLTVFENVAFPlRE-HTDLSEAEIrELVLEKLELvglPGAADK----MPSeLSGGMRKRVALARALAl 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 150 --QLwpgeegstLLLDEPTSMLDPLhqhttleAVRRFADC--------GAAVLVILHDLNLAARYCDRILLLEQGRCHAF 219
Cdd:COG1127 159 dpEI--------LLYDEPTAGLDPI-------TSAVIDELirelrdelGLTSVVVTHDLDSAFAIADRVAVLADGKIIAE 223
|
....*...
gi 939342971 220 ATPEAALT 227
Cdd:COG1127 224 GTPEELLA 231
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-235 |
7.54e-39 |
|
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: 135.39 E-value: 7.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLRRGSN-EVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQE-RA--RRL 77
Cdd:cd03256 1 IEVENLSKTYPNGkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlRQlrRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 78 AVLPQVSSLGFSFRVEEVVGMGRMPH-----GTGQRRDAEIVEAALRAADAWHLVERSYL---ALSGGERQRVHLARVLA 149
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRLGRrstwrSLFGLFPKEEKQRALAALERVGLLDKAYQradQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 150 QlwpgeEGSTLLLDEPTSMLDPLHQHTTLEAVRRFA-DCGAAVLVILHDLNLAARYCDRILLLEQGRChAFATPEAALTP 228
Cdd:cd03256 161 Q-----QPKLILADEPVASLDPASSRQVMDLLKRINrEEGITVIVSLHQVDLAREYADRIVGLKDGRI-VFDGPPAELTD 234
|
....*..
gi 939342971 229 AALKAVY 235
Cdd:cd03256 235 EVLDEIY 241
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-242 |
8.38e-38 |
|
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: 132.90 E-value: 8.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRG-RVTLQGRPLADWAGQERARRLAV 79
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 80 lpqVSS-LGFSFR----VEEVV------GMGRMPHGTgqRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVL 148
Cdd:COG1119 83 ---VSPaLQLRFPrdetVLDVVlsgffdSIGLYREPT--DEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 149 A---QLwpgeegstLLLDEPTSMLDPLHQHTTLEAVRRFADCGA-AVLVILHDLNLAARYCDRILLLEQGRCHAFATPEA 224
Cdd:COG1119 158 VkdpEL--------LILDEPTAGLDLGARELLLALLDKLAAEGApTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEE 229
|
250
....*....|....*...
gi 939342971 225 ALTPAALKAVYGIDVLVQ 242
Cdd:COG1119 230 VLTSENLSEAFGLPVEVE 247
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-210 |
9.26e-38 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 130.82 E-value: 9.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 12 GSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTlqgrpladwagQERARRLAVLPQVSSLGFSF- 90
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR-----------RAGGARVAYVPQRSEVPDSLp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 91 -RVEEVVGMGRMPHGTGQRR----DAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQlwpgeEGSTLLLDEP 165
Cdd:NF040873 72 lTVRDLVAMGRWARRGLWRRltrdDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQ-----EADLLLLDEP 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 939342971 166 TSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILL 210
Cdd:NF040873 147 TTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-215 |
1.09e-37 |
|
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: 131.46 E-value: 1.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLRRGSN----EVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQE----R 73
Cdd:cd03255 1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKElaafR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 74 ARRLAVLPQVSSLGFSFRVEEVVGMGRMPHGTGQRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQlwp 153
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAN--- 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 939342971 154 geEGSTLLLDEPTSMLDPLHQHTTLEAVRRFADC-GAAVLVILHDLNLaARYCDRILLLEQGR 215
Cdd:cd03255 158 --DPKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPEL-AEYADRIIELRDGK 217
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-167 |
2.01e-37 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 128.92 E-value: 2.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 17 LHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAVLPQVSSLGFSFRVEEVV 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 939342971 97 GMGRMPHGTGQRRDAEIVEAALRAADAWHL----VERSYLALSGGERQRVHLARVLAqlwpgEEGSTLLLDEPTS 167
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLadrpVGERPGTLSGGQRQRVAIARALL-----TKPKLLLLDEPTA 150
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-227 |
2.26e-37 |
|
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: 131.08 E-value: 2.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 4 VEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQER---ARRLAVL 80
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrlRRRMGML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 81 PQVSSLGFSFRVEEVVGM-----GRMPHGTGQRRDAEIVEAA-LRAAdawhlvERSYLA-LSGGERQRVHLARVLAqLWP 153
Cdd:cd03261 83 FQSGALFDSLTVFENVAFplrehTRLSEEEIREIVLEKLEAVgLRGA------EDLYPAeLSGGMKKRVALARALA-LDP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 939342971 154 geegSTLLLDEPTSMLDPLHQHTTLEAVRRFADC-GAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPEAALT 227
Cdd:cd03261 156 ----ELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-237 |
8.15e-37 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 129.87 E-value: 8.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLRRGsNEVLHdIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERArrLAVL 80
Cdd:COG3840 1 MLRLDDLTYRYG-DFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERP--VSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 81 PQVSSLGFSFRVEEVVGMGRMPHGTGQRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQLWPgeegsTL 160
Cdd:COG3840 77 FQENNLFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRP-----IL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 161 LLDEPTSMLDPLHQHTTLEAVRRFAD-CGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPEAAL---TPAALKAVYG 236
Cdd:COG3840 152 LLDEPFSALDPALRQEMLDLVDELCReRGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLdgePPPALAAYLG 231
|
.
gi 939342971 237 I 237
Cdd:COG3840 232 I 232
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-215 |
1.00e-36 |
|
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: 128.79 E-value: 1.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQEraRRLAVLP 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER--RNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 82 QVSSLGFSFRVEEVVG----MGRMPHGTGQRRdaeiVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQlwpgeEG 157
Cdd:cd03259 79 QDYALFPHLTVAENIAfglkLRGVPKAEIRAR----VRELLELVGLEGLLNRYPHELSGGQQQRVALARALAR-----EP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 939342971 158 STLLLDEPTSMLDPLHQHTTLEAVRR-FADCGAAVLVILHDLNLAARYCDRILLLEQGR 215
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELREELKElQRELGITTIYVTHDQEEALALADRIAVMNEGR 208
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
12-215 |
1.25e-36 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 136.06 E-value: 1.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 12 GSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAVLPQVSSLgFSFR 91
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFL-FSGT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 92 VEEVVGMGRmPHGTgqrrDAEIVEAAlRAADAWHLVER------SYLA-----LSGGERQRVHLARVL---AQLwpgeeg 157
Cdd:COG1132 430 IRENIRYGR-PDAT----DEEVEEAA-KAAQAHEFIEAlpdgydTVVGergvnLSGGQRQRIAIARALlkdPPI------ 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 939342971 158 stLLLDEPTSMLDPLHQHTTLEAVRRFADcGAAVLVILHDLNlAARYCDRILLLEQGR 215
Cdd:COG1132 498 --LILDEATSALDTETEALIQEALERLMK-GRTTIVIAHRLS-TIRNADRILVLDDGR 551
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-218 |
2.57e-35 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 125.54 E-value: 2.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGL--YLRRGSNEV--LHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERA-- 74
Cdd:COG1136 4 LLELRNLtkSYGTGEGEVtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELArl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 75 RRlavlpqvSSLGF---------SFRVEEVVGMGRMPHGTGQRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLA 145
Cdd:COG1136 84 RR-------RHIGFvfqffnllpELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 939342971 146 RVLAQlwpgeEGSTLLLDEPTSMLDPLHQHTTLEAVRRFA-DCGAAVLVILHDLNLAArYCDRILLLEQGRCHA 218
Cdd:COG1136 157 RALVN-----RPKLILADEPTGNLDSKTGEEVLELLRELNrELGTTIVMVTHDPELAA-RADRVIRLRDGRIVS 224
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-235 |
8.46e-35 |
|
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: 124.71 E-value: 8.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARR-LAV 79
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 80 LPQVSSLGFSFRVEEVVGMGRMPhgtgqRRDAEIVEAALRAADAW--HLVERSY-LA--LSGGERQRVHLARVLAQlwpg 154
Cdd:COG0410 83 VPEGRRIFPSLTVEENLLLGAYA-----RRDRAEVRADLERVYELfpRLKERRRqRAgtLSGGEQQMLAIGRALMS---- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 155 eEGSTLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPEAALTPAALKAV 234
Cdd:COG0410 154 -RPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEVREA 232
|
.
gi 939342971 235 Y 235
Cdd:COG0410 233 Y 233
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-226 |
8.75e-35 |
|
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: 130.66 E-value: 8.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLRR--GSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAV 79
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 80 LPQVSSLgFSFRVEEVVGMGRmPHGTgqrrDAEiVEAALRAADAWHLVERSY-----------LALSGGERQRVHLARVL 148
Cdd:COG4987 414 VPQRPHL-FDTTLRENLRLAR-PDAT----DEE-LWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLALARAL 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 939342971 149 AQlwpgeEGSTLLLDEPTSMLDPLHQHTTLEAVRRFADcGAAVLVILHDLNLAARyCDRILLLEQGRCHAFATPEAAL 226
Cdd:COG4987 487 LR-----DAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEELL 557
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-215 |
9.72e-35 |
|
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: 124.08 E-value: 9.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARR-LAVL 80
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 81 PQVSSLGFSFRVEE--VVGMGRMPHGTGQRRDAEIVEAALRaadawhLVER-SYLA--LSGGERQRVHLARVLAQlwpge 155
Cdd:cd03224 81 PEGRRIFPELTVEEnlLLGAYARRRAKRKARLERVYELFPR------LKERrKQLAgtLSGGEQQMLAIARALMS----- 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 156 EGSTLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGR 215
Cdd:cd03224 150 RPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-236 |
2.13e-34 |
|
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: 123.95 E-value: 2.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLRRGSN-EVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQER---ARR 76
Cdd:TIGR02315 1 MLEVENLSKVYPNGkQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLrklRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 77 LAVLPQVSSLGFSFRVEEVVGMGRM------PHGTGQRRDAEIVEAaLRAADAWHLVERSYL---ALSGGERQRVHLARV 147
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHGRLgykptwRSLLGRFSEEDKERA-LSALERVGLADKAYQradQLSGGQQQRVAIARA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 148 LAQlwpgeEGSTLLLDEPTSMLDPLHQHTTLEAVRRFA-DCGAAVLVILHDLNLAARYCDRILLLEQGRChAFATPEAAL 226
Cdd:TIGR02315 160 LAQ-----QPDLILADEPIASLDPKTSKQVMDYLKRINkEDGITVIINLHQVDLAKKYADRIVGLKAGEI-VFDGAPSEL 233
|
250
....*....|
gi 939342971 227 TPAALKAVYG 236
Cdd:TIGR02315 234 DDEVLRHIYG 243
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-215 |
2.69e-34 |
|
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: 130.34 E-value: 2.69e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLR--RGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAV 79
Cdd:COG2274 474 IELENVSFRypGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 80 LPQVSSLgFSFRVEEVVGMGRmPHGTgqrrDAEIVEAAlRAADAWHLVER------SYLA-----LSGGERQRVHLARVL 148
Cdd:COG2274 554 VLQDVFL-FSGTIRENITLGD-PDAT----DEEIIEAA-RLAGLHDFIEAlpmgydTVVGeggsnLSGGQRQRLAIARAL 626
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 939342971 149 AQlwpgeEGSTLLLDEPTSMLDPLHQHTTLEAVRRFAdCGAAVLVILHDLNLaARYCDRILLLEQGR 215
Cdd:COG2274 627 LR-----NPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLST-IRLADRIIVLDKGR 686
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-215 |
1.18e-33 |
|
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: 120.66 E-value: 1.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADwAGQERARRLAVL 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 81 PQVSSLGFSFRVEEVVGMGRMPHGTgqRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVL---AQLWpgeeg 157
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALYGL--RADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLlspAPLW----- 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 939342971 158 stlLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAAryCDRILLLEQGR 215
Cdd:COG4133 154 ---LLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELA--AARVLDLGDFK 206
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-215 |
1.49e-33 |
|
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: 119.60 E-value: 1.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERA--RRLAV 79
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPlrRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 80 LPQVSSLGFSFRVEEVVGMGrmphgtgqrrdaeiveaalraadawhlversylaLSGGERQRVHLARVLAQlwpgeEGST 159
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAM-----DPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 939342971 160 LLLDEPTSMLDPLHQHTTLEAVRR-FADCGAAVLVILHDLNLAARYCDRILLLEQGR 215
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSlQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-226 |
2.71e-32 |
|
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: 123.70 E-value: 2.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLR--RGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAV 79
Cdd:COG4618 331 LSVENLTVVppGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 80 LPQVSSLgFSFRVEEVVGmgRMPHGTgqrrDAEIVEAAlRAADAWHLVER---SY--------LALSGGERQRVHLARVL 148
Cdd:COG4618 411 LPQDVEL-FDGTIAENIA--RFGDAD----PEKVVAAA-KLAGVHEMILRlpdGYdtrigeggARLSGGQRQRIGLARAL 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 939342971 149 AQlWPgeegSTLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARyCDRILLLEQGRCHAFATPEAAL 226
Cdd:COG4618 483 YG-DP----RLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAA-VDKLLVLRDGRVQAFGPRDEVL 554
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-215 |
3.89e-32 |
|
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: 117.00 E-value: 3.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQerarRLAVLP 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARN----RIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 82 QVSSLGFSFRVEEVV-------GMGRmphgtgqrrdaeivEAALRAADAW-------HLVERSYLALSGGERQRVHLARV 147
Cdd:cd03269 77 EERGLYPKMKVIDQLvylaqlkGLKK--------------EEARRRIDEWlerlelsEYANKRVEELSKGNQQKVQFIAA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 939342971 148 LAQlwpgeEGSTLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGR 215
Cdd:cd03269 143 VIH-----DPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-215 |
7.40e-32 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 122.10 E-value: 7.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 4 VEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGrplaDWagqerarRLAVLPQV 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK----GL-------RIGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 84 SSLGFSFRVEEVVGMGRMPHGTGQRRDAEI----------------VEAALRAADAWHL-----------------VERS 130
Cdd:COG0488 70 PPLDDDLTVLDTVLDGDAELRALEAELEELeaklaepdedlerlaeLQEEFEALGGWEAearaeeilsglgfpeedLDRP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 131 YLALSGGERQRVHLARVLAQlwpgeEGSTLLLDEPTSMLDplhqhttLEAV-------RRFAdcgAAVLVILHDlnlaaR 203
Cdd:COG0488 150 VSELSGGWRRRVALARALLS-----EPDLLLLDEPTNHLD-------LESIewleeflKNYP---GTVLVVSHD-----R 209
|
250
....*....|....*..
gi 939342971 204 Y-----CDRILLLEQGR 215
Cdd:COG0488 210 YfldrvATRILELDRGK 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
10-217 |
1.09e-31 |
|
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: 116.03 E-value: 1.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 10 RRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLadwagQERARRLAVLPQVSSLgFS 89
Cdd:cd03293 13 GGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV-----TGPGPDRGYVFQQDAL-LP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 90 FR-VEEVVGMGRMPHGTGQRRDAEIVEAALRAAdawHL--VERSYLA-LSGGERQRVHLARVLAQlwpgeEGSTLLLDEP 165
Cdd:cd03293 87 WLtVLDNVALGLELQGVPKAEARERAEELLELV---GLsgFENAYPHqLSGGMRQRVALARALAV-----DPDVLLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 939342971 166 TSMLDP-----LHQHtTLEAVRRFadcGAAVLVILHDLNLAARYCDRILLLEQGRCH 217
Cdd:cd03293 159 FSALDAltreqLQEE-LLDIWRET---GKTVLLVTHDIDEAVFLADRVVVLSARPGR 211
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-211 |
1.12e-31 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 117.11 E-value: 1.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLR----RGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLAdwagqERARR 76
Cdd:COG1116 7 ALELRGVSKRfptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT-----GPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 77 LAVLPQVSSLgFSFR-VEEVVGMGRMPHGTGQRRDAEIVEAALR------AADAW-HlversylALSGGERQRVHLARVL 148
Cdd:COG1116 82 RGVVFQEPAL-LPWLtVLDNVALGLELRGVPKAERRERARELLElvglagFEDAYpH-------QLSGGMRQRVAIARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 939342971 149 AQlwpgeEGSTLLLDEPTSMLDP-----LHQhttlEAVRRFADCGAAVLVILHDLNLAARYCDRILLL 211
Cdd:COG1116 154 AN-----DPEVLLMDEPFGALDAltrerLQD----ELLRLWQETGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-215 |
1.49e-31 |
|
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: 114.24 E-value: 1.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLRRGSNE--VLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAV 79
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 80 LPQVSSLgFSfrveevvgmgrmphGTgqrrDAEIVeaalraadawhlversylaLSGGERQRVHLARVLAQlwpgeEGST 159
Cdd:cd03246 81 LPQDDEL-FS--------------GS----IAENI-------------------LSGGQRQRLGLARALYG-----NPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 939342971 160 LLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARyCDRILLLEQGR 215
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLAS-ADRILVLEDGR 172
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
2-235 |
3.94e-31 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 115.06 E-value: 3.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARR-LAVL 80
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLgIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 81 PQVSSLgfsFR---VEE--VVGMGRMPHGTGQRRDAEIvEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQlwpge 155
Cdd:TIGR04406 82 PQEASI---FRkltVEEniMAVLEIRKDLDRAEREERL-EALLEEFQISHLRDNKAMSLSGGERRRVEIARALAT----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 156 EGSTLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPEAALTPAALKAVY 235
Cdd:TIGR04406 153 NPKFILLDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVRRVY 232
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
17-251 |
5.37e-31 |
|
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: 115.63 E-value: 5.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 17 LHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLadWAGQERARRlAVLPQVsslGFSFR----- 91
Cdd:TIGR04521 21 LDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDI--TAKKKKKLK-DLRKKV---GLVFQfpehq 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 92 -----VEEVVGMGrmPHGTGQRRDaeivEAALRAADAWHLV-------ERSYLALSGGERQRVHLARVLAQlwpgeEGST 159
Cdd:TIGR04521 95 lfeetVYKDIAFG--PKNLGLSEE----EAEERVKEALELVgldeeylERSPFELSGGQMRRVAIAGVLAM-----EPEV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 160 LLLDEPTSMLDPLHQHTTLEAVRRFAD-CGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPEAALT-PAALKAvYGI 237
Cdd:TIGR04521 164 LILDEPTAGLDPKGRKEILDLFKRLHKeKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSdVDELEK-IGL 242
|
250
....*....|....*....
gi 939342971 238 DV-----LVQAHPERGHPL 251
Cdd:TIGR04521 243 DVpeiteLARKLKEKGLPV 261
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-215 |
5.90e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 115.98 E-value: 5.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLadwaGQERARRLAVL 80
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL----DPEDRRRIGYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 81 PQVSSLGFSFRVEEVV-------GMGRmphgtgqrrdaeivEAALRAADAW-----------HLVErsylALSGGERQRV 142
Cdd:COG4152 77 PEERGLYPKMKVGEQLvylarlkGLSK--------------AEAKRRADEWlerlglgdranKKVE----ELSKGNQQKV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 143 HLArvlaqlwpgeegSTLL-------LDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGR 215
Cdd:COG4152 139 QLI------------AALLhdpelliLDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGR 206
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
11-211 |
6.32e-31 |
|
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: 119.70 E-value: 6.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 11 RGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAVLPQVSSLgFSF 90
Cdd:TIGR02857 332 PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFL-FAG 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 91 RVEEVVGMGRmPHGTgqrrDAEIVEaALRAADAWHLVE-----------RSYLALSGGERQRVHLARVLAQLWPgeegsT 159
Cdd:TIGR02857 411 TIAENIRLAR-PDAS----DAEIRE-ALERAGLDEFVAalpqgldtpigEGGAGLSGGQAQRLALARAFLRDAP-----L 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 939342971 160 LLLDEPTSMLDPLHQHTTLEAVRRFADcGAAVLVILHDLNLAARyCDRILLL 211
Cdd:TIGR02857 480 LLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-235 |
8.90e-31 |
|
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: 114.18 E-value: 8.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARR-LAVL 80
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 81 PQVSSLgfsFR---VEEVVGMGRMPHGTGQRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQlwpgeEG 157
Cdd:cd03218 81 PQEASI---FRkltVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALAT-----NP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 939342971 158 STLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPEAALTPAALKAVY 235
Cdd:cd03218 153 KFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKVY 230
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-223 |
1.57e-30 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 114.73 E-value: 1.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLRRGSNE--VLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAV 79
Cdd:PRK13635 6 IRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 80 LPQVSSLGF-SFRVEEVVGMG----RMPHGTGQRRdaeiVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQlwpg 154
Cdd:PRK13635 86 VFQNPDNQFvGATVQDDVAFGleniGVPREEMVER----VDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLAL---- 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 155 eEGSTLLLDEPTSMLDPLHQHTTLEAVRRFAD-CGAAVLVILHDLNLAARyCDRILLLEQGRCHAFATPE 223
Cdd:PRK13635 158 -QPDIIILDEATSMLDPRGRREVLETVRQLKEqKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPE 225
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
15-201 |
3.71e-30 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 111.36 E-value: 3.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 15 EVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLA-DWAGQERARRLA--VLPQVSSLGFSFR 91
Cdd:TIGR01166 6 EVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDySRKGLLERRQRVglVFQDPDDQLFAAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 92 VEEVVGMGRMPHGTGQRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQlwpgeEGSTLLLDEPTSMLDP 171
Cdd:TIGR01166 86 VDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAM-----RPDVLLLDEPTAGLDP 160
|
170 180 190
....*....|....*....|....*....|
gi 939342971 172 LHQHTTLEAVRRFADCGAAVLVILHDLNLA 201
Cdd:TIGR01166 161 AGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-216 |
4.77e-30 |
|
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: 110.21 E-value: 4.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLAdWAGQERARRLAVlp 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS-FASPRDARRAGI-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 82 qvsslgfsfrveevvgmgRMPHgtgQrrdaeiveaalraadawhlversylaLSGGERQRVHLARVLAQlwpgeEGSTLL 161
Cdd:cd03216 78 ------------------AMVY---Q--------------------------LSVGERQMVEIARALAR-----NARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 939342971 162 LDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGRC 216
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-233 |
1.30e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 112.14 E-value: 1.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 4 VEGLYLR-RGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQE-RARRLAVLP 81
Cdd:PRK13647 7 VEDLHFRyKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvRSKVGLVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 82 QVSSLGFSFRVEEVVGMGRMPHGTGQRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQlwpgeEGSTLL 161
Cdd:PRK13647 87 DPDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAM-----DPDVIV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 939342971 162 LDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPEAALTPAALKA 233
Cdd:PRK13647 162 LDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIVEQ 233
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-215 |
3.42e-29 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 109.76 E-value: 3.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLR-RGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERA---RR 76
Cdd:COG2884 1 MIRFENVSKRyPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPylrRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 77 LAVLPQvsslgfSFR------VEEVVGMGRMPHGTGQRRDAEIVEAALRaadawhLV-----ERSY-LALSGGERQRVHL 144
Cdd:COG2884 81 IGVVFQ------DFRllpdrtVYENVALPLRVTGKSRKEIRRRVREVLD------LVglsdkAKALpHELSGGEQQRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 939342971 145 ARVLA---QLwpgeegstLLLDEPTSMLDPlhqHTTLEAVR---RFADCGAAVLVILHDLNLAARYCDRILLLEQGR 215
Cdd:COG2884 149 ARALVnrpEL--------LLADEPTGNLDP---ETSWEIMElleEINRRGTTVLIATHDLELVDRMPKRVLELEDGR 214
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-172 |
4.66e-29 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 109.73 E-value: 4.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARR-LAV 79
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 80 LPQVSSLgfsFR---VE-------EVVGMGRmphgtGQRRdaEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLA 149
Cdd:COG1137 83 LPQEASI---FRkltVEdnilavlELRKLSK-----KERE--ERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALA 152
|
170 180
....*....|....*....|...
gi 939342971 150 QlwpgeEGSTLLLDEPTSMLDPL 172
Cdd:COG1137 153 T-----NPKFILLDEPFAGVDPI 170
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-215 |
5.23e-29 |
|
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: 108.82 E-value: 5.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLRRGSNEVLHDIHLQLPPGqVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADwAGQERARRLAVLP 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 82 QVSSLGFSFRVEEVVG-MGRMpHGTGQRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQlwpgeEGSTL 160
Cdd:cd03264 79 QEFGVYPNFTVREFLDyIAWL-KGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVG-----DPSIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 939342971 161 LLDEPTSMLDPLHQHttleAVRR-FADCGAAVLVIL--HDLNLAARYCDRILLLEQGR 215
Cdd:cd03264 153 IVDEPTAGLDPEERI----RFRNlLSELGEDRIVILstHIVEDVESLCNQVAVLNKGK 206
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-225 |
9.29e-29 |
|
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: 108.68 E-value: 9.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLRRGSNE----VLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARR 76
Cdd:COG4181 8 IIELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 77 LAvlpqvSSLGFSFR----------VEEVVgmgrMPHGTGQRRDAEivEAALRAADAWHLVERS--YLA-LSGGERQRVH 143
Cdd:COG4181 88 RA-----RHVGFVFQsfqllptltaLENVM----LPLELAGRRDAR--ARARALLERVGLGHRLdhYPAqLSGGEQQRVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 144 LARVLAQlwpgeEGSTLLLDEPTSMLDplhQHT------TLEAVRRfaDCGAAVLVILHDLNLAARyCDRILLLEQGRCH 217
Cdd:COG4181 157 LARAFAT-----EPAILFADEPTGNLD---AATgeqiidLLFELNR--ERGTTLVLVTHDPALAAR-CDRVLRLRAGRLV 225
|
....*...
gi 939342971 218 AFATPEAA 225
Cdd:COG4181 226 EDTAATAA 233
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-224 |
9.94e-29 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 111.39 E-value: 9.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRplaDWAGQE--RARRLAV 79
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGR---DLFTNLppRERRVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 80 LPQVSSLgfsFR---VEEVV--GMGRMPHGTGQRRdaEIVEAALRAADAWHLVERsYLA-LSGGERQRVHLARVLAQlwp 153
Cdd:COG1118 80 VFQHYAL---FPhmtVAENIafGLRVRPPSKAEIR--ARVEELLELVQLEGLADR-YPSqLSGGQRQRVALARALAV--- 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 939342971 154 geEGSTLLLDEPTSMLDPlHQHTTLEAV--RRFADCGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPEA 224
Cdd:COG1118 151 --EPEVLLLDEPFGALDA-KVRKELRRWlrRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDE 220
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
19-215 |
4.05e-28 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 106.42 E-value: 4.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 19 DIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGrplADWAGQERARR-LAVLPQVSSLGFSFRVEEVVG 97
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING---VDVTAAPPADRpVSMLFQENNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 98 MGRMPHGTGQRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQLWPgeegsTLLLDEPTSMLDPLHQHTT 177
Cdd:cd03298 93 LGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKP-----VLLLDEPFAALDPALRAEM 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 939342971 178 LEAVRRF-ADCGAAVLVILHDLNLAARYCDRILLLEQGR 215
Cdd:cd03298 168 LDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGR 206
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
22-237 |
5.44e-28 |
|
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: 106.47 E-value: 5.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 22 LQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPladwaGQERARRLAVLPQVSSLGFSF--RVEEVVGMG 99
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGAS-----PGKGWRHIGYVPQRHEFAWDFpiSVAHTVMSG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 100 RMPHGTGQRR----DAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQlwpgeEGSTLLLDEPTSMLDPLHQH 175
Cdd:TIGR03771 76 RTGHIGWLRRpcvaDFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALAT-----RPSVLLLDEPFTGLDMPTQE 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 939342971 176 TTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLeQGRCHAFATPEAALTPAALKAVYGI 237
Cdd:TIGR03771 151 LLTELFIELAGAGTAILMTTHDLAQAMATCDRVVLL-NGRVIADGTPQQLQDPAPWMTTFGV 211
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-223 |
6.70e-28 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 106.30 E-value: 6.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 4 VEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERaRRLAVLPQV 83
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVR-RRIGIVFQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 84 SSL-----GFsfrvEEVVGMGRMpHGTGQRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQlwpgeEGS 158
Cdd:cd03265 82 LSVddeltGW----ENLYIHARL-YGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVH-----RPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 939342971 159 TLLLDEPTSMLDPLHQHTTLEAVRRF-ADCGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPE 223
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPE 217
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-219 |
8.89e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 110.92 E-value: 8.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLqGRPLadwagqerarRLAVL 80
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------KIGYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 81 PQvsslgfsfrveevvgmgrmpHGTGQRRDAEIVEAALRAADAWHLVE-RSYLA---------------LSGGERQRVHL 144
Cdd:COG0488 384 DQ--------------------HQEELDPDKTVLDELRDGAPGGTEQEvRGYLGrflfsgddafkpvgvLSGGEKARLAL 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 939342971 145 ARVLAQlwpgeEGSTLLLDEPTSMLDPlhqhTTLEAV----RRFAdcGaAVLVILHDLNLAARYCDRILLLEQGRCHAF 219
Cdd:COG0488 444 AKLLLS-----PPNVLLLDEPTNHLDI----ETLEALeealDDFP--G-TVLLVSHDRYFLDRVATRILEFEDGGVREY 510
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-223 |
1.22e-27 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 108.26 E-value: 1.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQEraRRLAVL 80
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK--RNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 81 PQVSSLgFSFR-VEEVVGMG-RMphgtgQRRDAEivEAALRAADAWHLVERSYLA------LSGGERQRVHLARVLA--- 149
Cdd:COG3842 83 FQDYAL-FPHLtVAENVAFGlRM-----RGVPKA--EIRARVAELLELVGLEGLAdryphqLSGGQQQRVALARALApep 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 939342971 150 QLwpgeegstLLLDEPTSMLDP-LHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPE 223
Cdd:COG3842 155 RV--------LLLDEPLSALDAkLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPE 221
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-218 |
1.73e-27 |
|
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: 105.14 E-value: 1.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLR----RGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADwAGQERARR 76
Cdd:cd03266 1 MITADALTKRfrdvKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 77 LAVLPQVSSLGFSFRVEEVVG-MGRMpHGTGQRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQlwpge 155
Cdd:cd03266 80 LGFVSDSTGLYDRLTARENLEyFAGL-YGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVH----- 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 939342971 156 EGSTLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGRCHA 218
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVY 216
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
12-240 |
1.84e-27 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. 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. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 107.09 E-value: 1.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 12 GSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERaRRLAVLPQVSSL--GFS 89
Cdd:TIGR01188 4 GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVR-RSIGIVPQYASVdeDLT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 90 FRvEEVVGMGR---MPHGTGQRRDAEIVEAAlraaDAWHLVERSYLALSGGERQRVHLARVLAQlwpgeEGSTLLLDEPT 166
Cdd:TIGR01188 83 GR-ENLEMMGRlygLPKDEAEERAEELLELF----ELGEAADRPVGTYSGGMRRRLDIAASLIH-----QPDVLFLDEPT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 939342971 167 SMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPEaaltpaALKAVYGIDVL 240
Cdd:TIGR01188 153 TGLDPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPE------ELKRRLGKDTL 220
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
16-215 |
6.02e-27 |
|
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: 103.84 E-value: 6.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 16 VLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAVLPQVSSLgFSFRVEEV 95
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDTFL-FSGTIMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 96 VGMGRmphgtgQRRDAEIVEAALRAADAWHLVERS---YLA--------LSGGERQRVHLARVLAQlwpgeEGSTLLLDE 164
Cdd:cd03254 97 IRLGR------PNATDEEVIEAAKEAGAHDFIMKLpngYDTvlgenggnLSQGERQLLAIARAMLR-----DPKILILDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 939342971 165 PTSMLDPLHQHTTLEAVRRFADcGAAVLVILHDLNlAARYCDRILLLEQGR 215
Cdd:cd03254 166 ATSNIDTETEKLIQEALEKLMK-GRTSIIIAHRLS-TIKNADKILVLDDGK 214
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-223 |
6.53e-27 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 103.96 E-value: 6.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 4 VEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERarrlavlpqv 83
Cdd:cd03296 5 VRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER---------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 84 sSLGFSFR---------VEEVVGMG-RMPHGTGQRRDAEIVEaalRAADAWHLVERSYLA------LSGGERQRVHLARV 147
Cdd:cd03296 75 -NVGFVFQhyalfrhmtVFDNVAFGlRVKPRSERPPEAEIRA---KVHELLKLVQLDWLAdrypaqLSGGQRQRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 939342971 148 LAQlwpgeEGSTLLLDEPTSMLDPLHQHTTLEAVRRFAD-CGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPE 223
Cdd:cd03296 151 LAV-----EPKVLLLDEPFGALDAKVRKELRRWLRRLHDeLHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPD 222
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
17-215 |
7.08e-27 |
|
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: 103.14 E-value: 7.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 17 LHDIHLQLP---PGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQ----ERARRLAVLPQVSSLGFS 89
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKinlpPQQRKIGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 90 FRVEEVVGMGRMPHGTGQRRDAeiVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQlwpgeEGSTLLLDEPTSML 169
Cdd:cd03297 90 LNVRENLAFGLKRKRNREDRIS--VDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAA-----QPELLLLDEPFSAL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 939342971 170 D-PLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGR 215
Cdd:cd03297 163 DrALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGR 209
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
16-223 |
1.33e-26 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 104.05 E-value: 1.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 16 VLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLAD----WagqERARRLAVLPQ------VSS 85
Cdd:TIGR04520 17 ALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDeenlW---EIRKKVGMVFQnpdnqfVGA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 86 LgfsfrVEEVVGMG----RMPHGTGQRRdaeiVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQlwpgeEGSTLL 161
Cdd:TIGR04520 94 T-----VEDDVAFGlenlGVPREEMRKR----VDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAM-----RPDIII 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 939342971 162 LDEPTSMLDPLHQHTTLEAVRRF-ADCGAAVLVILHDLNLAARyCDRILLLEQGRCHAFATPE 223
Cdd:TIGR04520 160 LDEATSMLDPKGRKEVLETIRKLnKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPR 221
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-224 |
1.57e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 104.50 E-value: 1.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERArRLAVLP 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQ-RVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 82 QVSSLGFSFRV-EEVVGMGR---MPHGTGQRRDAEIVEAALRAADAwhlvERSYLALSGGERQRVHLARVLAQlwpgeEG 157
Cdd:PRK13537 87 QFDNLDPDFTVrENLLVFGRyfgLSAAAARALVPPLLEFAKLENKA----DAKVGELSGGMKRRLTLARALVN-----DP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 939342971 158 STLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPEA 224
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHA 224
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
12-224 |
4.06e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 104.14 E-value: 4.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 12 GSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERArRLAVLPQVSSLGFSFR 91
Cdd:PRK13536 52 GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARA-RIGVVPQFDNLDLEFT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 92 VEE-VVGMGRMpHGTGQRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQlwpgeEGSTLLLDEPTSMLD 170
Cdd:PRK13536 131 VREnLLVFGRY-FGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALIN-----DPQLLILDEPTTGLD 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 939342971 171 PLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPEA 224
Cdd:PRK13536 205 PHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHA 258
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
17-215 |
5.33e-26 |
|
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: 100.95 E-value: 5.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 17 LHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERA---RRLAVLPQVSSLGFSFRVE 93
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPylrRKIGVVFQDFRLLPDRNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 94 EVVGMGRMPHGTGQRRDAEIVEAALRAADAWHlVERSYLA-LSGGERQRVHLARVLAQlwpgeEGSTLLLDEPTSMLDPL 172
Cdd:cd03292 97 ENVAFALEVTGVPPREIRKRVPAALELVGLSH-KHRALPAeLSGGEQQRVAIARAIVN-----SPTILIADEPTGNLDPD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 939342971 173 HQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGR 215
Cdd:cd03292 171 TTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGK 213
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-223 |
5.61e-26 |
|
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: 101.64 E-value: 5.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYlRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQEraRRLAVLP 81
Cdd:cd03299 1 LKVENLS-KDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK--RDISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 82 QVSSLGFSFRVEEVVGMG-RMPHGTGQRRDAEIVEAAlRAADAWHLVERSYLALSGGERQRVHLARVLAQlwpgeEGSTL 160
Cdd:cd03299 78 QNYALFPHMTVYKNIAYGlKKRKVDKKEIERKVLEIA-EMLGIDHLLNRKPETLSGGEQQRVAIARALVV-----NPKIL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 939342971 161 LLDEPTSMLDPLHQHTTLEAVRRFAD-CGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPE 223
Cdd:cd03299 152 LLDEPFSALDVRTKEKLREELKKIRKeFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPE 215
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
14-215 |
6.15e-26 |
|
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: 101.13 E-value: 6.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 14 NEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAVLPQVSSLgFSFRVE 93
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQDVTL-FYGTLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 94 EVVGMGrMPHGTgqrrDAEIVEAALRA-----------ADAWHLVERSYlALSGGERQRVHLARVLAQlwpgeEGSTLLL 162
Cdd:cd03245 96 DNITLG-APLAD----DERILRAAELAgvtdfvnkhpnGLDLQIGERGR-GLSGGQRQAVALARALLN-----DPPILLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 939342971 163 DEPTSMLDPLHQHTTLEAVRRFAdCGAAVLVILHDLNLAArYCDRILLLEQGR 215
Cdd:cd03245 165 DEPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRPSLLD-LVDRIIVMDSGR 215
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
16-215 |
1.03e-25 |
|
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: 99.31 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 16 VLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADwAGQERARRLAVLPQVSSLgFSFRVEEV 95
Cdd:cd03247 17 VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSD-LEKALSSLISVLNQRPYL-FDTTLRNN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 96 VGmgrmphgtgqRRdaeiveaalraadawhlversylaLSGGERQRVHLARVLAQlwpgeEGSTLLLDEPTSMLDPLHQH 175
Cdd:cd03247 95 LG----------RR------------------------FSGGERQRLALARILLQ-----DAPIVLLDEPTVGLDPITER 135
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 939342971 176 TTLEAVRRFADcGAAVLVILHDLnLAARYCDRILLLEQGR 215
Cdd:cd03247 136 QLLSLIFEVLK-DKTLIWITHHL-TGIEHMDKILFLENGK 173
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-254 |
1.54e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 101.24 E-value: 1.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLadwagqERARR--LA 78
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL------DYSKRglLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 79 VLPQVSSLG-------FSFRVEEVVGMGRMPHGTGQRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQl 151
Cdd:PRK13638 75 LRQQVATVFqdpeqqiFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVL- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 152 wpgeEGSTLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPEAALTPAAL 231
Cdd:PRK13638 154 ----QARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEA 229
|
250 260
....*....|....*....|....*
gi 939342971 232 KAVYGIDV--LVQAHPERGHPLIIT 254
Cdd:PRK13638 230 MEQAGLTQpwLVKLHTQLGLPLCKT 254
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-223 |
1.87e-25 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 100.07 E-value: 1.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRlavl 80
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKLR---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 81 pqvSSLGFSF---------RVEE--------VVGMGRmphgtgqrrdAEIVEAALRAADAWHLVER--SYLA-LSGGERQ 140
Cdd:COG1126 77 ---RKVGMVFqqfnlfphlTVLEnvtlapikVKKMSK----------AEAEERAMELLERVGLADKadAYPAqLSGGQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 141 RVHLARVLAQlwpgeEGSTLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGRCHAFA 220
Cdd:COG1126 144 RVAIARALAM-----EPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEG 218
|
...
gi 939342971 221 TPE 223
Cdd:COG1126 219 PPE 221
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
16-235 |
3.08e-25 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 99.58 E-value: 3.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 16 VLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARR-LAVLPQVSSLGFSFRV-E 93
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgIGYLPQEASIFRRLSVyD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 94 EVVGMGRMPHGTGQRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQlwpgeEGSTLLLDEPTSMLDPLH 173
Cdd:PRK10895 98 NLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAA-----NPKFILLDEPFAGVDPIS 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 939342971 174 QHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPEAALTPAALKAVY 235
Cdd:PRK10895 173 VIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVY 234
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-215 |
3.41e-25 |
|
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: 99.19 E-value: 3.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGL----YLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAG---QER 73
Cdd:cd03258 1 MIELKNVskvfGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGkelRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 74 ARRLAVLPQVSSLGFSFRVEEVVGMGRMPHGTGQRRDAEIVEAALraadawHLV-----ERSYLA-LSGGERQRVHLARV 147
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELL------ELVgledkADAYPAqLSGGQKQRVGIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 939342971 148 LAQlwpgeEGSTLLLDEPTSMLDPLHQHTTLEAVRRF-ADCGAAVLVILHDLNLAARYCDRILLLEQGR 215
Cdd:cd03258 155 LAN-----NPKVLLCDEATSALDPETTQSILALLRDInRELGLTIVLITHEMEVVKRICDRVAVMEKGE 218
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
11-235 |
5.30e-25 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 99.96 E-value: 5.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 11 RGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADwagQERARRLAVLPQVSSLGFSF 90
Cdd:PRK15056 17 RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ---ALQKNLVAYVPQSEEVDWSF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 91 RV--EEVVGMGRMPHGTGQRR----DAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQlwpgeEGSTLLLDE 164
Cdd:PRK15056 94 PVlvEDVVMMGRYGHMGWLRRakkrDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQ-----QGQVILLDE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 939342971 165 PTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLeQGRCHAFATPEAALTPAALKAVY 235
Cdd:PRK15056 169 PFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMV-KGTVLASGPTETTFTAENLELAF 238
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
17-215 |
7.18e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 102.41 E-value: 7.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 17 LHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLaDWAGQERARRLAV--LPQVSSLGFSFRVEE 94
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV-RIRSPRDAIALGIgmVHQHFMLVPNLTVAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 95 VVGMGRMPHGTGQRRDAEIVEAALRAADAWHL-------VERsylaLSGGERQRVHLARVLAQlwpgeeGSTLL-LDEPT 166
Cdd:COG3845 100 NIVLGLEPTKGGRLDRKAARARIRELSERYGLdvdpdakVED----LSVGEQQRVEILKALYR------GARILiLDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 939342971 167 SMLDPlhQHTT--LEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGR 215
Cdd:COG3845 170 AVLTP--QEADelFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGK 218
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
10-226 |
8.64e-25 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 98.62 E-value: 8.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 10 RRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRpladwagqerarrlavlpqVSSLgfs 89
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR-------------------VSAL--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 90 frVEevVGMGRMPHGTG------------------QRRDAEIVE-AALRaaDAWHLVERSYlalSGGERQRVHLArVLAQ 150
Cdd:COG1134 93 --LE--LGAGFHPELTGreniylngrllglsrkeiDEKFDEIVEfAELG--DFIDQPVKTY---SSGMRARLAFA-VATA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 939342971 151 LwpgeEGSTLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPEAAL 226
Cdd:COG1134 163 V----DPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVI 234
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
11-216 |
9.97e-25 |
|
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: 97.24 E-value: 9.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 11 RGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAP--DRGRVTLQGRPLADwagQERARRLAVLPQvsslgf 88
Cdd:cd03213 19 KSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDK---RSFRKIIGYVPQ------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 89 sfrvEEVVgmgrmpHGTGQRRDAEIVEAALRAadawhlversylaLSGGERQRVHLARVLAQlwpgeEGSTLLLDEPTSM 168
Cdd:cd03213 90 ----DDIL------HPTLTVRETLMFAAKLRG-------------LSGGERKRVSIALELVS-----NPSLLFLDEPTSG 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 939342971 169 LDPLHQHTTLEAVRRFADCGAAVLVILHDL-NLAARYCDRILLLEQGRC 216
Cdd:cd03213 142 LDSSSALQVMSLLRRLADTGRTIICSIHQPsSEIFELFDKLLLLSQGRV 190
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-215 |
1.24e-24 |
|
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: 97.89 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEG------LYLRRGSN-EVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTL--QGRP--LADWA 69
Cdd:COG4778 4 LLEVENlsktftLHLQGGKRlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWvdLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 70 GQE--RARR---------LAVLPQVSSLgfsfrveEVVGMGRMPHGTgqrrDAEivEAALRAADA----------WHLve 128
Cdd:COG4778 84 PREilALRRrtigyvsqfLRVIPRVSAL-------DVVAEPLLERGV----DRE--EARARARELlarlnlperlWDL-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 129 rSYLALSGGERQRVHLARVLAQLWPgeegsTLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRI 208
Cdd:COG4778 149 -PPATFSGGEQQRVNIARGFIADPP-----LLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRV 222
|
....*..
gi 939342971 209 LLLEQGR 215
Cdd:COG4778 223 VDVTPFS 229
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-222 |
1.64e-24 |
|
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: 97.19 E-value: 1.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLR--RGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERaRRLAV 79
Cdd:cd03263 1 LQIRNLTKTykKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAAR-QSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 80 LPQVSSLGFSFRVEE-VVGMGRMpHGTGQRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAqlwpGeEGS 158
Cdd:cd03263 80 CPQFDALFDELTVREhLRFYARL-KGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALI----G-GPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 939342971 159 TLLLDEPTSMLDPLHQH---TTLEAVRRfadcGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATP 222
Cdd:cd03263 154 VLLLDEPTSGLDPASRRaiwDLILEVRK----GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSP 216
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
8-223 |
1.75e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 98.72 E-value: 1.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 8 YLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAVLPQVSSLG 87
Cdd:PRK13652 11 YSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPDDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 88 -FSFRVEEVVGMGRMPHGTGQRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQlwpgeEGSTLLLDEPT 166
Cdd:PRK13652 91 iFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAM-----EPQVLVLDEPT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 939342971 167 SMLDPLHQHTTLEAVRRFADC-GAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPE 223
Cdd:PRK13652 166 AGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVE 223
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
15-215 |
2.20e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 98.38 E-value: 2.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 15 EVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLaDWAgqerarRLAVLPQVSSLG------- 87
Cdd:PRK13636 20 HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYS------RKGLMKLRESVGmvfqdpd 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 88 ---FSFRVEEVVGMGRMPHGTGQRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQlwpgeEGSTLLLDE 164
Cdd:PRK13636 93 nqlFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVM-----EPKVLVLDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 939342971 165 PTSMLDPLHQHTTLEAVRRFA-DCGAAVLVILHDLNLAARYCDRILLLEQGR 215
Cdd:PRK13636 168 PTAGLDPMGVSEIMKLLVEMQkELGLTIIIATHDIDIVPLYCDNVFVMKEGR 219
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
15-215 |
2.31e-24 |
|
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: 97.40 E-value: 2.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 15 EVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGrpLADWAGQER-ARRLAV-----------LPQ 82
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG--LVPWKRRKKfLRRIGVvfgqktqlwwdLPV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 83 VSSLGFSFRVEevvgmgRMPHGTGQRRDAEIVEaalrAADAWHLVERSYLALSGGERQRVHLARVLaqLWpgeEGSTLLL 162
Cdd:cd03267 113 IDSFYLLAAIY------DLPPARFKKRLDELSE----LLDLEELLDTPVRQLSLGQRMRAEIAAAL--LH---EPEILFL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 939342971 163 DEPTSMLDPLHQhttlEAVRRF-----ADCGAAVLVILHDLNLAARYCDRILLLEQGR 215
Cdd:cd03267 178 DEPTIGLDVVAQ----ENIRNFlkeynRERGTTVLLTSHYMKDIEALARRVLVIDKGR 231
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-208 |
2.94e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 100.86 E-value: 2.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPL-------ADWAG--- 70
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVrfrsprdAQAAGiai 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 71 --QErarrLAVLPQVSslgfsfrVEEVVGMGRMPHGTGQRRDAEIVEAALRAADAWHL-------VERsylaLSGGERQR 141
Cdd:COG1129 84 ihQE----LNLVPNLS-------VAENIFLGREPRRGGLIDWRAMRRRARELLARLGLdidpdtpVGD----LSVAQQQL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 939342971 142 VHLARVLAQlwpgeEGSTLLLDEPTSMLDP-----LhqhttLEAVRRFADCGAAVLVILHDLNLAARYCDRI 208
Cdd:COG1129 149 VEIARALSR-----DARVLILDEPTASLTEreverL-----FRIIRRLKAQGVAIIYISHRLDEVFEIADRV 210
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-215 |
3.45e-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: 94.05 E-value: 3.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPladwagqerarRLAVLP 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV-----------KIGYFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 82 QvsslgfsfrveevvgmgrmphgtgqrrdaeiveaalraadawhlversylaLSGGERQRVHLARVLAqlwpgEEGSTLL 161
Cdd:cd03221 70 Q---------------------------------------------------LSGGEKMRLALAKLLL-----ENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 939342971 162 LDEPTSMLDPLHQHTTLEAVRRFADcgaAVLVILHDLNLAARYCDRILLLEQGR 215
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKEYPG---TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
12-198 |
5.99e-24 |
|
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: 100.13 E-value: 5.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 12 GSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAVLPQVSSLgFSFR 91
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHL-FDTT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 92 VEEVVGMGRmPHGTgqrrDAEIVEAALRAADAWHLVERSY----------LALSGGERQRVHLARVLAQLWPgeegsTLL 161
Cdd:TIGR02868 425 VRENLRLAR-PDAT----DEELWAALERVGLADWLRALPDgldtvlgeggARLSGGERQRLALARALLADAP-----ILL 494
|
170 180 190
....*....|....*....|....*....|....*..
gi 939342971 162 LDEPTSMLDPLHQHTTLEAVRRfADCGAAVLVILHDL 198
Cdd:TIGR02868 495 LDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-215 |
8.01e-24 |
|
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: 95.29 E-value: 8.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADwagqeRARRLAVLP 81
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-----DKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 82 QvsSLGFSFR---------VEEVVGMGrmPHGTGQRRDAEIVEAALRAADAWHLVER--SYLA-LSGGERQRVHLARVLA 149
Cdd:cd03262 76 Q--KVGMVFQqfnlfphltVLENITLA--PIKVKGMSKAEAEERALELLEKVGLADKadAYPAqLSGGQQQRVAIARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 939342971 150 QlwpgeEGSTLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGR 215
Cdd:cd03262 152 M-----NPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-214 |
9.50e-24 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 95.92 E-value: 9.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADwAGQERarrlAVL 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-PGAER----GVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 81 PQVSSLGFSFRVEEVVGMGRMPHGTGQRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQlwpgeEGSTL 160
Cdd:PRK11248 76 FQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAA-----NPQLL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 939342971 161 LLDEPTSMLDPL--HQHTTLeAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQG 214
Cdd:PRK11248 151 LLDEPFGALDAFtrEQMQTL-LLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
10-227 |
9.58e-24 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 95.54 E-value: 9.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 10 RRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLA---------VL 80
Cdd:PRK09493 10 HFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEagmvfqqfyLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 81 PQVSSLgfsfrveEVVGMG-RMPHGTGqRRDAEIVEAALRAADAwhLVERS--YLA-LSGGERQRVHLARVLAqLWPgee 156
Cdd:PRK09493 90 PHLTAL-------ENVMFGpLRVRGAS-KEEAEKQARELLAKVG--LAERAhhYPSeLSGGQQQRVAIARALA-VKP--- 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 939342971 157 gSTLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPEAALT 227
Cdd:PRK09493 156 -KLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIK 225
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-171 |
1.87e-23 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 95.10 E-value: 1.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCG--ELAPD---RGRVTLQGRPLADwagqerarr 76
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRmnDLIPGarvEGEILLDGEDIYD--------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 77 lavlPQVSslgfsfrVEEV---VGM------------------G-RMpHGTGQRRD-AEIVEAALRAADAWHLV----ER 129
Cdd:COG1117 83 ----PDVD-------VVELrrrVGMvfqkpnpfpksiydnvayGlRL-HGIKSKSElDEIVEESLRKAALWDEVkdrlKK 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 939342971 130 SYLALSGGERQRVHLARVLAQlwpgeEGSTLLLDEPTSMLDP 171
Cdd:COG1117 151 SALGLSGGQQQRLCIARALAV-----EPEVLLMDEPTSALDP 187
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-249 |
2.29e-23 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 96.71 E-value: 2.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEgLYLRRGSNEVlhDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQ-----ERaR 75
Cdd:COG4148 2 MLEVD-FRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGiflppHR-R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 76 RLAVLPQVSSLgFS-FRVEEVV--GMGRMPHGTGQRRDAEIVEA-ALRaadawHLVERSYLALSGGERQRVHLARVLA-- 149
Cdd:COG4148 78 RIGYVFQEARL-FPhLSVRGNLlyGRKRAPRAERRISFDEVVELlGIG-----HLLDRRPATLSGGERQRVAIGRALLss 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 150 -QLwpgeegstLLLDEPTSMLD--------PLhqhttLEAVRRFADCgaAVLVILHDLNLAARYCDRILLLEQGRCHAFA 220
Cdd:COG4148 152 pRL--------LLMDEPLAALDlarkaeilPY-----LERLRDELDI--PILYVSHSLDEVARLADHVVLLEQGRVVASG 216
|
250 260 270
....*....|....*....|....*....|....*.
gi 939342971 221 TPEAALTPAALKAVYG-------IDVLVQAHPERGH 249
Cdd:COG4148 217 PLAEVLSRPDLLPLAGgeeagsvLEATVAAHDPDYG 252
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
5-215 |
2.64e-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: 94.48 E-value: 2.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 5 EGLYLRRGSNE--VLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAVLPQ 82
Cdd:cd03252 4 EHVRFRYKPDGpvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 83 VSSLgFSFRVEEVVGMGRmphgTGQRRDaEIVEAAlRAADAWHLV------------ERSyLALSGGERQRVHLARVLAQ 150
Cdd:cd03252 84 ENVL-FNRSIRDNIALAD----PGMSME-RVIEAA-KLAGAHDFIselpegydtivgEQG-AGLSGGQRQRIAIARALIH 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 939342971 151 lwpgeEGSTLLLDEPTSMLDPLHQHTTLEAVRRFADcGAAVLVILHDLNlAARYCDRILLLEQGR 215
Cdd:cd03252 156 -----NPRILIFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLS-TVKNADRIIVMEKGR 213
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
13-215 |
3.43e-23 |
|
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: 94.22 E-value: 3.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 13 SNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAVLPQVSSLgFSFRV 92
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQDTVL-FNDTI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 93 EEVVGMGRmPHGTgqrrDAEIVEAALRAA---------DAWHLV--ERSyLALSGGERQRVHLARVLAQlwpgeEGSTLL 161
Cdd:cd03253 92 GYNIRYGR-PDAT----DEEVIEAAKAAQihdkimrfpDGYDTIvgERG-LKLSGGEKQRVAIARAILK-----NPPILL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 939342971 162 LDEPTSMLDPLHQHTTLEAVRRFADcGAAVLVILHDLNLAARyCDRILLLEQGR 215
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLSTIVN-ADKIIVLKDGR 212
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
17-232 |
3.63e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 95.05 E-value: 3.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 17 LHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAVL----PQVSSLGFSfrV 92
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGIvfqnPETQFVGRT--V 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 93 EEVVGMGRM-----PHGTGQRRDAEIVEAALRAADawhlvERSYLALSGGERQRVHLARVLAQlwpgeEGSTLLLDEPTS 167
Cdd:PRK13644 96 EEDLAFGPEnlclpPIEIRKRVDRALAEIGLEKYR-----HRSPKTLSGGQGQCVALAGILTM-----EPECLIFDEVTS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 939342971 168 MLDPLHQHTTLEAVRRFADCGAAVLVILHDLNlAARYCDRILLLEQGRCHAFATPEAALTPAALK 232
Cdd:PRK13644 166 MLDPDSGIAVLERIKKLHEKGKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLSDVSLQ 229
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-197 |
4.43e-23 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 94.54 E-value: 4.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLR----RGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADwAGQERA-- 74
Cdd:COG4525 3 MLTVRHVSVRypggGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGADRGvv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 75 -RRLAVLPQVS-----SLGFSFRveevvGMGRMphgtgQRRdaEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVL 148
Cdd:COG4525 82 fQKDALLPWLNvldnvAFGLRLR-----GVPKA-----ERR--ARAEELLALVGLADFARRRIWQLSGGMRQRVGIARAL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 939342971 149 AQlwpgeEGSTLLLDEPTSMLDPLHQHTTLEAVRR-FADCGAAVLVILHD 197
Cdd:COG4525 150 AA-----DPRFLLMDEPFGALDALTREQMQELLLDvWQRTGKGVFLITHS 194
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
15-223 |
4.62e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 94.76 E-value: 4.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 15 EVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLA-DWAGQERARRLA--VLPQVSSLGFSFR 91
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKyDKKSLLEVRKTVgiVFQNPDDQLFAPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 92 VEEVVGMGRMPHGTGQRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQlwpgeEGSTLLLDEPTSMLDP 171
Cdd:PRK13639 96 VEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAM-----KPEIIVLDEPTSGLDP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 939342971 172 LHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPE 223
Cdd:PRK13639 171 MGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPK 222
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-215 |
4.69e-23 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 94.36 E-value: 4.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADwaGQERARrlaVLP 81
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE--AREDTR---LMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 82 QVSSLGFSFRVEEVVGMGRmphgTGQRRDaeiveAALRAADAWHLVERSY---LALSGGERQRVHLARVLAQLwPGeegs 158
Cdd:PRK11247 88 QDARLLPWKKVIDNVGLGL----KGQWRD-----AALQALAAVGLADRANewpAALSGGQKQRVALARALIHR-PG---- 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 939342971 159 TLLLDEPTSMLDPLhqhTTLEA----VRRFADCGAAVLVILHDLNLAARYCDRILLLEQGR 215
Cdd:PRK11247 154 LLLLDEPLGALDAL---TRIEMqdliESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
10-229 |
5.88e-23 |
|
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: 93.52 E-value: 5.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 10 RRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAVLPQVSSLGFS 89
Cdd:cd03295 10 YGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQQIGLFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 90 FRVEEVVGMgrMPHGTG---QRRDAEIVEA-ALRAADAWHLVERSYLALSGGERQRVHLARVLAQlwpgeEGSTLLLDEP 165
Cdd:cd03295 90 MTVEENIAL--VPKLLKwpkEKIRERADELlALVGLDPAEFADRYPHELSGGQQQRVGVARALAA-----DPPLLLMDEP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 939342971 166 TSMLDPLHQHTTLEAVRRF-ADCGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPEAALT-PA 229
Cdd:cd03295 163 FGALDPITRDQLQEEFKRLqQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRsPA 228
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
6-215 |
7.62e-23 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 93.98 E-value: 7.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 6 GLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPL-----ADWAGQERARRLAVL 80
Cdd:PRK10419 17 GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLaklnrAQRKAFRRDIQMVFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 81 PQVSSLGFSFRVEEVVGMgRMPHGTG------QRRDAEIVEAA-LRAADAWHLVERsylaLSGGERQRVHLARVLAQlwp 153
Cdd:PRK10419 97 DSISAVNPRKTVREIIRE-PLRHLLSldkaerLARASEMLRAVdLDDSVLDKRPPQ----LSGGQLQRVCLARALAV--- 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 939342971 154 geEGSTLLLDEPTSMLDPLHQHTTLEAVRRF-ADCGAAVLVILHDLNLAARYCDRILLLEQGR 215
Cdd:PRK10419 169 --EPKLLILDEAVSNLDLVLQAGVIRLLKKLqQQFGTACLFITHDLRLVERFCQRVMVMDNGQ 229
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-215 |
9.96e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 93.61 E-value: 9.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLR--RGS-NE--VLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERAR 75
Cdd:COG1101 1 MLELKNLSKTfnPGTvNEkrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 76 RLAVLPQVSSLGFSFR--VEE--VVGMGRmphgtGQRRDAEIveaALRAADAWHLVERsyLA----------------LS 135
Cdd:COG1101 81 YIGRVFQDPMMGTAPSmtIEEnlALAYRR-----GKRRGLRR---GLTKKRRELFREL--LAtlglglenrldtkvglLS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 136 GGERQRVHLarVLAQLWPGEegsTLLLDEPTSMLDP----LHQHTTLEAVRRFadcGAAVLVILHDLNLAARYCDRILLL 211
Cdd:COG1101 151 GGQRQALSL--LMATLTKPK---LLLLDEHTAALDPktaaLVLELTEKIVEEN---NLTTLMVTHNMEQALDYGNRLIMM 222
|
....
gi 939342971 212 EQGR 215
Cdd:COG1101 223 HEGR 226
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
12-223 |
1.10e-22 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 92.77 E-value: 1.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 12 GSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQG------RPLADWAGQERARRLAVLPQVSS 85
Cdd:COG4161 13 GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRLLRQKVGMVFQQYN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 86 LGFSFRVEE--------VVGMGRmphgTGQRRDAEIVEAALRAADawhLVERSYLALSGGERQRVHLARVLAQlwpgeEG 157
Cdd:COG4161 93 LWPHLTVMEnlieapckVLGLSK----EQAREKAMKLLARLRLTD---KADRFPLHLSGGQQQRVAIARALMM-----EP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 939342971 158 STLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGR------CHAFATPE 223
Cdd:COG4161 161 QVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRiieqgdASHFTQPQ 232
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-215 |
1.13e-22 |
|
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: 91.89 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAgqERARRLAVLp 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI--EALRRIGAL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 82 qVSSLGFsfrVEEVVGMGRMP-HGTGQRRDAEIVEAALRA---ADAWHLVERSYlalSGGERQRVHLARVLAQlwpgeEG 157
Cdd:cd03268 78 -IEAPGF---YPNLTARENLRlLARLLGIRKKRIDEVLDVvglKDSAKKKVKGF---SLGMKQRLGIALALLG-----NP 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 939342971 158 STLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGR 215
Cdd:cd03268 146 DLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGK 203
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-223 |
1.19e-22 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 94.75 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAgqERARRLAVL 80
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLP--PKDRNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 81 PQvsS------------LGFSFRveevvgMGRMPhgtgqrrDAEIVEAALRAADAW---HLVERSYLALSGGERQRVHLA 145
Cdd:COG3839 81 FQ--SyalyphmtvyenIAFPLK------LRKVP-------KAEIDRRVREAAELLgleDLLDRKPKQLSGGQRQRVALG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 146 RVLAQlwpgeEGSTLLLDEPTSMLDP-LHQHTTLEAVRRFADCGAAVLVILHD----LNLAarycDRILLLEQGRCHAFA 220
Cdd:COG3839 146 RALVR-----EPKVFLLDEPLSNLDAkLRVEMRAEIKRLHRRLGTTTIYVTHDqveaMTLA----DRIAVMNDGRIQQVG 216
|
...
gi 939342971 221 TPE 223
Cdd:COG3839 217 TPE 219
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
15-215 |
1.45e-22 |
|
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: 96.32 E-value: 1.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 15 EVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAVLPQVSSLgFSFRVEE 94
Cdd:TIGR02203 346 PALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVL-FNDTIAN 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 95 VVGMGRMphgtGQRRDAEIvEAALRAADAWHLVERSYLA-----------LSGGERQRVHLARVLAQLWPgeegsTLLLD 163
Cdd:TIGR02203 425 NIAYGRT----EQADRAEI-ERALAAAYAQDFVDKLPLGldtpigengvlLSGGQRQRLAIARALLKDAP-----ILILD 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 939342971 164 EPTSMLD---PLHQHTTLEAVRRfadcGAAVLVILHDLNlAARYCDRILLLEQGR 215
Cdd:TIGR02203 495 EATSALDnesERLVQAALERLMQ----GRTTLVIAHRLS-TIEKADRIVVMDDGR 544
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-215 |
2.02e-22 |
|
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: 91.76 E-value: 2.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGL---------YLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQE 72
Cdd:cd03248 6 DHLKGIvkfqnvtfaYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 73 RARRLAVLPQVSSLgFSFRVEEvvgmgRMPHGTGQRRDAEIVEAALR--AADAWHLVERSYLA--------LSGGERQRV 142
Cdd:cd03248 86 LHSKVSLVGQEPVL-FARSLQD-----NIAYGLQSCSFECVKEAAQKahAHSFISELASGYDTevgekgsqLSGGQKQRV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 939342971 143 HLARVLAQlwpgeEGSTLLLDEPTSMLDPLHQHTTLEAVRRFADcGAAVLVILHDLNLAARyCDRILLLEQGR 215
Cdd:cd03248 160 AIARALIR-----NPQVLILDEATSALDAESEQQVQQALYDWPE-RRTVLVIAHRLSTVER-ADQILVLDGGR 225
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
13-203 |
2.22e-22 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 91.80 E-value: 2.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 13 SNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERA----RRLAVLPQVSSLGF 88
Cdd:PRK11629 21 QTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAelrnQKLGFIYQFHHLLP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 89 SFRVEEVVGmgrMPHGTGQRRDAEIVEAALRAADAWHLVERSY---LALSGGERQRVHLARVLAQlwpgeEGSTLLLDEP 165
Cdd:PRK11629 101 DFTALENVA---MPLLIGKKKPAEINSRALEMLAAVGLEHRANhrpSELSGGERQRVAIARALVN-----NPRLVLADEP 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 939342971 166 TSMLDPLHQHTTLEAVRRF-ADCGAAVLVILHDLNLAAR 203
Cdd:PRK11629 173 TGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKR 211
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-215 |
2.38e-22 |
|
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: 91.16 E-value: 2.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQEraRRLAVLP 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 82 QVSSLGFSFRVEEVVGMGRMPHGTGQRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQlwpgeEGSTLL 161
Cdd:cd03301 79 QNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVR-----EPKVFL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 939342971 162 LDEPTSMLDP-LHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGR 215
Cdd:cd03301 154 MDEPLSNLDAkLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQ 208
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-209 |
2.89e-22 |
|
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: 93.19 E-value: 2.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGL----YLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAP---DRGRVTLQGRPLADWAGQE- 72
Cdd:COG0444 1 LLEVRNLkvyfPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 73 ---RARRLAVLPQ--VSSLGFSFRVEEVVGMGRMPHGTGQRRDA-EIVEAALRA---ADAWHLVERSYLALSGGERQRVH 143
Cdd:COG0444 81 rkiRGREIQMIFQdpMTSLNPVMTVGDQIAEPLRIHGGLSKAEArERAIELLERvglPDPERRLDRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 144 LARVLA---QLwpgeegstLLLDEPTSMLDPLHQHTTLEAVRRF-ADCGAAVLVILHDLNLAARYCDRIL 209
Cdd:COG0444 161 IARALAlepKL--------LIADEPTTALDVTIQAQILNLLKDLqRELGLAILFITHDLGVVAEIADRVA 222
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-223 |
3.86e-22 |
|
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: 91.14 E-value: 3.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERA-----RR 76
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPvntvfQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 77 LAVLPQVSslgfsfrVEEVVGMG-RMphgtgQRRDAEIVEAalRAADAWHLVERSYLA------LSGGERQRVHLARVLA 149
Cdd:cd03300 81 YALFPHLT-------VFENIAFGlRL-----KKLPKAEIKE--RVAEALDLVQLEGYAnrkpsqLSGGQQQRVAIARALV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 939342971 150 QlwpgeEGSTLLLDEPTSMLD-PLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPE 223
Cdd:cd03300 147 N-----EPKVLLLDEPLGALDlKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPE 216
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
14-215 |
6.30e-22 |
|
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: 90.75 E-value: 6.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 14 NEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAVLPQVSSLgFSFRVE 93
Cdd:cd03251 15 PPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVSQDVFL-FNDTVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 94 EVVGMGRmphgtgqrRDA--EIVEAALRAADAWHLVERS---Y--------LALSGGERQRVHLARVLAQLWPgeegsTL 160
Cdd:cd03251 94 ENIAYGR--------PGAtrEEVEEAARAANAHEFIMELpegYdtvigergVKLSGGQRQRIAIARALLKDPP-----IL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 939342971 161 LLDEPTSMLDPLHQHTTLEAVRRFADcGAAVLVILHDLNlAARYCDRILLLEQGR 215
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMK-NRTTFVIAHRLS-TIENADRIVVLEDGK 213
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
12-215 |
1.00e-21 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 90.46 E-value: 1.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 12 GSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQG------RPLADWAGQERARRLAVLPQVSS 85
Cdd:PRK11124 13 GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRELRRNVGMVFQQYN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 86 LGFSFRVEE--------VVGMGRmphgTGQRRDAEIVEAALRAADawhLVERSYLALSGGERQRVHLARVLAQlwpgeEG 157
Cdd:PRK11124 93 LWPHLTVQQnlieapcrVLGLSK----DQALARAEKLLERLRLKP---YADRFPLHLSGGQQQRVAIARALMM-----EP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 939342971 158 STLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGR 215
Cdd:PRK11124 161 QVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGH 218
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-211 |
1.77e-21 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 89.39 E-value: 1.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAVL 80
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 81 PQVSSLgFSfrvEEVVGMGRMPHGT-GQRRDAEIVEAAL-RAADAWHLVERSYLALSGGERQRVHLARVLaQLWPgeegS 158
Cdd:PRK10247 87 AQTPTL-FG---DTVYDNLIFPWQIrNQQPDPAIFLDDLeRFALPDTILTKNIAELSGGEKQRISLIRNL-QFMP----K 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 939342971 159 TLLLDEPTSMLDPLHQHTTLEAVRRFA-DCGAAVLVILHDLNlAARYCDRILLL 211
Cdd:PRK10247 158 VLLLDEITSALDESNKHNVNEIIHRYVrEQNIAVLWVTHDKD-EINHADKVITL 210
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
19-224 |
1.94e-21 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 91.71 E-value: 1.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 19 DIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADwAGQ------ERaRRLAVLPQVSSL--GFSF 90
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFD-SRKgiflppEK-RRIGYVFQEARLfpHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 91 RVEEVVGMGRMPHGTGQRRDAEIVEaaLRAADawHLVERSYLALSGGERQRVHLAR-VLAQlwpgeeGSTLLLDEPTSML 169
Cdd:TIGR02142 93 RGNLRYGMKRARPSERRISFERVIE--LLGIG--HLLGRLPGRLSGGEKQRVAIGRaLLSS------PRLLLMDEPLAAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 939342971 170 DPLHQHTTLEAVRRFAD-CGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPEA 224
Cdd:TIGR02142 163 DDPRKYEILPYLERLHAeFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAE 218
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-215 |
2.01e-21 |
|
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: 88.68 E-value: 2.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLRRGSNE-----VLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGrpladwagqerarR 76
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 77 LAVLPQVSSLgfsfrveevvgmgrmPHGT-------GQRRDAEIVEAALRAA------------DAWHLVERSyLALSGG 137
Cdd:cd03250 68 IAYVSQEPWI---------------QNGTirenilfGKPFDEERYEKVIKACalepdleilpdgDLTEIGEKG-INLSGG 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 138 ERQRVHLARVLAQlwpgeEGSTLLLDEPTSMLDPlhqHTtleAVRRFADC-------GAAVLVILHDLNLaARYCDRILL 210
Cdd:cd03250 132 QKQRISLARAVYS-----DADIYLLDDPLSAVDA---HV---GRHIFENCilglllnNKTRILVTHQLQL-LPHADQIVV 199
|
....*
gi 939342971 211 LEQGR 215
Cdd:cd03250 200 LDNGR 204
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
21-239 |
2.84e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 88.87 E-value: 2.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 21 HLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGrplADWAGQERARR-LAVLPQVSSLGFSFRVEEVVGMG 99
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG---QDHTTTPPSRRpVSMLFQENNLFSHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 100 RMPhgtGQRRDAE---IVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQLWPgeegsTLLLDEPTSMLDPLHQHT 176
Cdd:PRK10771 96 LNP---GLKLNAAqreKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQP-----ILLLDEPFSALDPALRQE 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 177 TLEAVRRFadCGAAVLVIL---HDLNLAARYCDRILLLEQGRCHaFATPEAAL----TPAAlkAVYGIDV 239
Cdd:PRK10771 168 MLTLVSQV--CQERQLTLLmvsHSLEDAARIAPRSLVVADGRIA-WDGPTDELlsgkASAS--ALLGIKS 232
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-219 |
5.55e-21 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 88.92 E-value: 5.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDR---GRVTLQGRPLadwagqERARRL 77
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagSHIELLGRTV------QREGRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 78 A--VLPQVSSLGFSFR----------VEEVV--GMGRMPHGT------GQRRDAEIVEAALRAADAwHLVERSYLALSGG 137
Cdd:PRK09984 78 ArdIRKSRANTGYIFQqfnlvnrlsvLENVLigALGSTPFWRtcfswfTREQKQRALQALTRVGMV-HFAHQRVSTLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 138 ERQRVHLARVLAQlwpgeEGSTLLLDEPTSMLDPLHQHTTLEAVRRFADC-GAAVLVILHDLNLAARYCDRILLLEQGrc 216
Cdd:PRK09984 157 QQQRVAIARALMQ-----QAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQG-- 229
|
...
gi 939342971 217 HAF 219
Cdd:PRK09984 230 HVF 232
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
10-222 |
5.92e-21 |
|
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: 87.93 E-value: 5.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 10 RRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAVLPQVSSLgFS 89
Cdd:cd03244 13 RPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQDPVL-FS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 90 frveevvgmgrmphGT--------GQRRDAEIVEaALRAADAW-----------HLVERSYLALSGGERQRVHLARVLAQ 150
Cdd:cd03244 92 --------------GTirsnldpfGEYSDEELWQ-ALERVGLKefveslpggldTVVEEGGENLSVGQRQLLCLARALLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 939342971 151 lwpgeEGSTLLLDEPTSMLDPLHQHTTLEAVR-RFADCgaAVLVILHDLNLAARYcDRILLLEQGRCHAFATP 222
Cdd:cd03244 157 -----KSKILVLDEATASVDPETDALIQKTIReAFKDC--TVLTIAHRLDTIIDS-DRILVLDKGRVVEFDSP 221
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
12-224 |
8.86e-21 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 87.86 E-value: 8.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 12 GSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTlqgrpladwagQERARRLAVLPQVSSLGFSFR 91
Cdd:PRK09544 15 GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-----------RNGKLRIGYVPQKLYLDTTLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 92 VeEVVGMGRMPHGTgqrRDAEIVeAALRAADAWHLVERSYLALSGGERQRVHLARVLAQlwpgeEGSTLLLDEPTSMLDP 171
Cdd:PRK09544 84 L-TVNRFLRLRPGT---KKEDIL-PALKRVQAGHLIDAPMQKLSGGETQRVLLARALLN-----RPQLLVLDEPTQGVDV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 939342971 172 LHQ---HTTLEAVRRFADCgaAVLVILHDLNLAARYCDRILLLEQGRCHAfATPEA 224
Cdd:PRK09544 154 NGQvalYDLIDQLRRELDC--AVLMVSHDLHLVMAKTDEVLCLNHHICCS-GTPEV 206
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-239 |
9.23e-21 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 89.37 E-value: 9.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGL----YLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQE--RA 74
Cdd:COG1135 1 MIELENLsktfPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElrAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 75 RR-LAVLPQVSSLgFSFR-----VE---EVVGMGRmphgtgqrrdAEIVEaalRAADAWHLV-----ERSYLA-LSGGER 139
Cdd:COG1135 81 RRkIGMIFQHFNL-LSSRtvaenVAlplEIAGVPK----------AEIRK---RVAELLELVglsdkADAYPSqLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 140 QRVHLARVLAQlwpgeEGSTLLLDEPTSMLDPlhqHTT------LEAVRRfaDCGAAVLVILHDLNLAARYCDRILLLEQ 213
Cdd:COG1135 147 QRVGIARALAN-----NPKVLLCDEATSALDP---ETTrsildlLKDINR--ELGLTIVLITHEMDVVRRICDRVAVLEN 216
|
250 260 270
....*....|....*....|....*....|...
gi 939342971 214 GRC-------HAFATPEAALTPAALKAVYGIDV 239
Cdd:COG1135 217 GRIveqgpvlDVFANPQSELTRRFLPTVLNDEL 249
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-215 |
1.17e-20 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 87.88 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTL------QGRPLADWAGQERA 74
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidTARSLSQQKGLIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 75 RRLAVlpqvsslGFSFRveevvGMGRMPHGT-------------GQRRDAEIVEA-ALRAADAWHLVERSY-LALSGGER 139
Cdd:PRK11264 83 LRQHV-------GFVFQ-----NFNLFPHRTvleniiegpvivkGEPKEEATARArELLAKVGLAGKETSYpRRLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 939342971 140 QRVHLARVLAQlwpgeEGSTLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGR 215
Cdd:PRK11264 151 QRVAIARALAM-----RPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGR 221
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
17-223 |
2.11e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 87.77 E-value: 2.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 17 LHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLadwAGQERARRLAVLPQVSSLGFSF------ 90
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVI---TAGKKNKKLKPLRKKVGIVFQFpehqlf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 91 --RVEEVVGMGRMPHGTGQRrdaeivEAALRAADAWHLV-------ERSYLALSGGERQRVHLARVLAQlwpgeEGSTLL 161
Cdd:PRK13634 100 eeTVEKDICFGPMNFGVSEE------DAKQKAREMIELVglpeellARSPFELSGGQMRRVAIAGVLAM-----EPEVLV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 939342971 162 LDEPTSMLDPLHQHTTLEAVRRF-ADCGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPE 223
Cdd:PRK13634 169 LDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPR 231
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-215 |
2.81e-20 |
|
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: 86.17 E-value: 2.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 16 VLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPD---RGRVTLQGRPLADwagQERARRLAVLPQVSSLGFSFRV 92
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKP---DQFQKCVAYVRQDDILLPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 93 EEVV---GMGRMP-HGTGQRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQLwPGeegsTLLLDEPTSM 168
Cdd:cd03234 99 RETLtytAILRLPrKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWD-PK----VLILDEPTSG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 939342971 169 LDPLHQHTTLEAVRRFADCGAAVLVILH----DLnlaARYCDRILLLEQGR 215
Cdd:cd03234 174 LDSFTALNLVSTLSQLARRNRIVILTIHqprsDL---FRLFDRILLLSSGE 221
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-235 |
3.56e-20 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 86.09 E-value: 3.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARR-LAV 79
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREaVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 80 LPQVSSLGFSFRVEEVVGMGRM--PHGTGQRRDAEIVEAALRaadawhLVERSYL---ALSGGERQRVHLARVLAQlwpg 154
Cdd:PRK11614 85 VPEGRRVFSRMTVEENLAMGGFfaERDQFQERIKWVYELFPR------LHERRIQragTMSGGEQQMLAIGRALMS---- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 155 eEGSTLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPEAALTPAALKAV 234
Cdd:PRK11614 155 -QPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSA 233
|
.
gi 939342971 235 Y 235
Cdd:PRK11614 234 Y 234
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-223 |
4.33e-20 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 86.39 E-value: 4.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSvlCGEL--APDRGRVTLQGRPLAdWAGQERARRLA 78
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLR--CINLleTPDSGEIRVGGEEIR-LKPDRDGELVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 79 VLP-QV----SSLGFSFR---------VEEVVGMGRMpHGTGQRRdAEIVEAALraadawHLVERSYLA---------LS 135
Cdd:COG4598 85 ADRrQLqrirTRLGMVFQsfnlwshmtVLENVIEAPV-HVLGRPK-AEAIERAE------ALLAKVGLAdkrdaypahLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 136 GGERQRVHLARVLAQlwpgeEGSTLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGR 215
Cdd:COG4598 157 GGQQQRAAIARALAM-----EPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGR 231
|
....*...
gi 939342971 216 CHAFATPE 223
Cdd:COG4598 232 IEEQGPPA 239
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
15-215 |
5.10e-20 |
|
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: 88.72 E-value: 5.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 15 EVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAgQERARR-LAVLPQVSSLgFSFRVE 93
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVT-QASLRAaIGIVPQDTVL-FNDTIA 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 94 EVVGMGRmPHGTgqrrDAEIVEAAlRAA----------DAWH-LV-ERSyLALSGGERQRVHLARVLAQLWPgeegsTLL 161
Cdd:COG5265 450 YNIAYGR-PDAS----EEEVEAAA-RAAqihdfieslpDGYDtRVgERG-LKLSGGEKQRVAIARTLLKNPP-----ILI 517
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 162 LDEPTSMLDplhQHT------TLEAVRRfadcGAAVLVILHDLNLAARyCDRILLLEQGR 215
Cdd:COG5265 518 FDEATSALD---SRTeraiqaALREVAR----GRTTLVIAHRLSTIVD-ADEILVLEAGR 569
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
16-215 |
6.82e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 88.34 E-value: 6.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 16 VLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAVLPQVSSLgFSFRVEEV 95
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHL-FSATLRDN 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 96 VGMGRmPHGTgqrrDAEIVEAALRaadawhlVERSYLA----------------LSGGERQRVHLARVLAQLWPgeegsT 159
Cdd:PRK11160 434 LLLAA-PNAS----DEALIEVLQQ-------VGLEKLLeddkglnawlgeggrqLSGGEQRRLGIARALLHDAP-----L 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 939342971 160 LLLDEPTSMLDPLHQHTTLEAVRRFAdCGAAVLVILHDLNLAARYcDRILLLEQGR 215
Cdd:PRK11160 497 LLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITHRLTGLEQF-DRICVMDNGQ 550
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
9-238 |
6.85e-20 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 88.20 E-value: 6.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 9 LRRGSNEV--LHDIHLQLPPGQVVGVLGPNGAGKSSL-LSVLcgELAPDRGRVTLQGRPLADWAGQE-RARRLAVlpQV- 83
Cdd:COG4172 292 FRRTVGHVkaVDGVSLTLRRGETLGLVGESGSGKSTLgLALL--RLIPSEGEIRFDGQDLDGLSRRAlRPLRRRM--QVv 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 84 -----SSLGFSFRVEEVVGMG---RMPHGTGQRRDAEIVEA----ALRAADAW---HlversylALSGGERQRVHLARVL 148
Cdd:COG4172 368 fqdpfGSLSPRMTVGQIIAEGlrvHGPGLSAAERRARVAEAleevGLDPAARHrypH-------EFSGGQRQRIAIARAL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 149 AqLWPgeegSTLLLDEPTSMLDPLHQHTTLEAVRRF-ADCGAAVLVILHDLNLAARYCDRILLL------EQGRCHA-FA 220
Cdd:COG4172 441 I-LEP----KLLVLDEPTSALDVSVQAQILDLLRDLqREHGLAYLFISHDLAVVRALAHRVMVMkdgkvvEQGPTEQvFD 515
|
250
....*....|....*...
gi 939342971 221 TPEAALTPAALKAVYGID 238
Cdd:COG4172 516 APQHPYTRALLAAAPLLE 533
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-215 |
1.01e-19 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 85.36 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGR-----PLADWAGQERaR 75
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAER-R 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 76 RLA-----VLPQVSSLGFSFRVEEVVGMGRMPHGTGQRRDAEIVEAALRaadaWhlVERSYLAL----------SGGERQ 140
Cdd:PRK11701 85 RLLrtewgFVHQHPRDGLRMQVSAGGNIGERLMAVGARHYGDIRATAGD----W--LERVEIDAariddlpttfSGGMQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 939342971 141 RVHLARVLAQlwpgeEGSTLLLDEPTSMLDPLHQHTTLEAVRRF-ADCGAAVLVILHDLNLAARYCDRILLLEQGR 215
Cdd:PRK11701 159 RLQIARNLVT-----HPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-215 |
1.35e-19 |
|
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: 83.73 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCG--ELAPDRGRVTLQGRPLADWAGQERARRlav 79
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGEDITDLPPEERARL--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 80 lpqvsSLGFSFrveevvgmgRMPhgtgqrrdAEI----VEAALRAADAwhlversylALSGGERQRVHLARVLAQlwpge 155
Cdd:cd03217 78 -----GIFLAF---------QYP--------PEIpgvkNADFLRYVNE---------GFSGGEKKRNEILQLLLL----- 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 939342971 156 EGSTLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAArYC--DRILLLEQGR 215
Cdd:cd03217 122 EPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLD-YIkpDRVHVLYDGR 182
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
17-229 |
1.41e-19 |
|
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: 85.00 E-value: 1.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 17 LHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQE----RARRL-------AVLPQVSS 85
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelRRKKIsmvfqsfALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 86 L---GFSFrveEVVGMGRmphgtgQRRDAeiveaalRAADAWHLV-----ERSYL-ALSGGERQRVHLARVLAQlwpgeE 156
Cdd:cd03294 120 LenvAFGL---EVQGVPR------AEREE-------RAAEALELVglegwEHKYPdELSGGMQQRVGLARALAV-----D 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 939342971 157 GSTLLLDEPTSMLDPL----HQHTTLEAVRRFadcGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPEAALT-PA 229
Cdd:cd03294 179 PDILLMDEAFSALDPLirreMQDELLRLQAEL---QKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTnPA 253
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
3-215 |
2.32e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 87.08 E-value: 2.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 3 HVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAVLPQ 82
Cdd:TIGR00958 483 DVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQ 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 83 VSSLgFSFRVEEVVGMGRmphgtgQRRDAEIVEAALRAADAWHLV---ERSYLA--------LSGGERQRVHLARVLAQl 151
Cdd:TIGR00958 563 EPVL-FSGSVRENIAYGL------TDTPDEEIMAAAKAANAHDFImefPNGYDTevgekgsqLSGGQKQRIAIARALVR- 634
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 939342971 152 wpgeEGSTLLLDEPTSMLDPLHQHtTLEAVRRFADcgAAVLVILHDLNLAARyCDRILLLEQGR 215
Cdd:TIGR00958 635 ----KPRVLILDEATSALDAECEQ-LLQESRSRAS--RTVLLIAHRLSTVER-ADQILVLKKGS 690
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-222 |
2.62e-19 |
|
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: 83.23 E-value: 2.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLRRGSN--EVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAV 79
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 80 LPQVSSLgFSfrveevvgmgrmphGT--------GQRRDAEIVEaALRaadawhlVERSYLALSGGERQRVHLARVLAQl 151
Cdd:cd03369 87 IPQDPTL-FS--------------GTirsnldpfDEYSDEEIYG-ALR-------VSEGGLNLSQGQRQLLCLARALLK- 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 939342971 152 wpgeEGSTLLLDEPTSMLDPLHQHTTLEAVRR-FADcgAAVLVILHDLNLAARyCDRILLLEQGRCHAFATP 222
Cdd:cd03369 143 ----RPRVLVLDEATASIDYATDALIQKTIREeFTN--STILTIAHRLRTIID-YDKILVMDAGEVKEYDHP 207
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
10-226 |
4.28e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 86.25 E-value: 4.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 10 RRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPD---RGRVTLQGRPLADWagqERARRLAVLPQVSSL 86
Cdd:TIGR00955 34 ERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAK---EMRAISAYVQQDDLF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 87 GFSFRVEE---VVGMGRMPHGTGQRRDAEIVEAALRA---ADAWHLV---ERSYLALSGGERQRVHLArvlaqlwpgEEG 157
Cdd:TIGR00955 111 IPTLTVREhlmFQAHLRMPRRVTKKEKRERVDEVLQAlglRKCANTRigvPGRVKGLSGGERKRLAFA---------SEL 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 939342971 158 ST----LLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNlAARYC--DRILLLEQGRCHAFATPEAAL 226
Cdd:TIGR00955 182 LTdpplLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPS-SELFElfDKIILMAEGRVAYLGSPDQAV 255
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
12-215 |
4.70e-19 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 85.78 E-value: 4.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 12 GSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAVLPQVSSLgFSFR 91
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGL-FNRS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 92 VEEVVGMGRmPHGTgqrrDAEIVEAALRAAdAWHLVERSYL-----------ALSGGERQRVHLARVLAQLWPgeegsTL 160
Cdd:PRK13657 425 IEDNIRVGR-PDAT----DEEMRAAAERAQ-AHDFIERKPDgydtvvgergrQLSGGERQRLAIARALLKDPP-----IL 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 939342971 161 LLDEPTSMLDPlhqhTTLEAVRRFADC---GAAVLVILHDLNlAARYCDRILLLEQGR 215
Cdd:PRK13657 494 ILDEATSALDV----ETEAKVKAALDElmkGRTTFIIAHRLS-TVRNADRILVFDNGR 546
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-212 |
4.97e-19 |
|
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: 85.76 E-value: 4.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERarrlavlp 81
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSR-------- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 82 qvSSLGFSFRVEEVV--GMGRMPHGTgqrrdaeiVEAALRA---------ADAWHLVErsylALSGGERQRVHLARVLAQ 150
Cdd:TIGR03719 395 --DALDPNKTVWEEIsgGLDIIKLGK--------REIPSRAyvgrfnfkgSDQQKKVG----QLSGGERNRVHLAKTLKS 460
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 939342971 151 lwpgeEGSTLLLDEPTSMLDPlhqhTTL----EAVRRFADCgaaVLVILHDLNLAARYCDRILLLE 212
Cdd:TIGR03719 461 -----GGNVLLLDEPTNDLDV----ETLraleEALLNFAGC---AVVISHDRWFLDRIATHILAFE 514
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
13-215 |
6.31e-19 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 85.53 E-value: 6.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 13 SNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAVLPQVSSLgFSFRV 92
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFL-FSDTV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 93 EEVVGMGRmPHGTGQR-----RDAEIVEAALRAADAW--HLVERSYLaLSGGERQRVHLARVLAQlwpgeEGSTLLLDEP 165
Cdd:PRK10789 406 ANNIALGR-PDATQQEiehvaRLASVHDDILRLPQGYdtEVGERGVM-LSGGQKQRISIARALLL-----NAEILILDDA 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 939342971 166 TSMLDPLHQHTTLEAVRRFADcGAAVLVILHDLNlAARYCDRILLLEQGR 215
Cdd:PRK10789 479 LSAVDGRTEHQILHNLRQWGE-GRTVIISAHRLS-ALTEASEILVMQHGH 526
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-207 |
6.91e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 82.90 E-value: 6.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVL--CGELAPD---RGRVTLQGR----PLADWAgQ 71
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHniysPRTDTV-D 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 72 ERARRLAVLPQVSSLGFSFrVEEVVGMGRMPHGTGQRRDAEIVEAALRAADAWHLVE----RSYLALSGGERQRVHLARV 147
Cdd:PRK14239 84 LRKEIGMVFQQPNPFPMSI-YENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVKdrlhDSALGLSGGQQQRVCIARV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 148 LAQlwpgeEGSTLLLDEPTSMLDPLHQHTTLEAVRRFADcGAAVLVILHDLNLAARYCDR 207
Cdd:PRK14239 163 LAT-----SPKIILLDEPTSALDPISAGKIEETLLGLKD-DYTMLLVTRSMQQASRISDR 216
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-215 |
6.96e-19 |
|
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: 81.32 E-value: 6.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLRRgsneVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRlavl 80
Cdd:cd03215 4 VLEVRGLSVKG----AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRA---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 81 pqvsslgfsfrveevvGMGRMPhgtGQRRDAEIVeaaLRAADAWHLVERSYLalSGGERQRVHLARVLAQlwpgeEGSTL 160
Cdd:cd03215 76 ----------------GIAYVP---EDRKREGLV---LDLSVAENIALSSLL--SGGNQQKVVLARWLAR-----DPRVL 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 939342971 161 LLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGR 215
Cdd:cd03215 127 ILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
6-219 |
1.11e-18 |
|
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: 81.81 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 6 GLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGR---PLA-------DWAGQERAR 75
Cdd:cd03220 27 GRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRvssLLGlgggfnpELTGRENIY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 76 RLAVLpqvssLGFSfrVEEVvgmgrmphgtgQRRDAEIVE-AALraADAWHLVERSYlalSGGerQRVHLARVLAQLWPG 154
Cdd:cd03220 107 LNGRL-----LGLS--RKEI-----------DEKIDEIIEfSEL--GDFIDLPVKTY---SSG--MKARLAFAIATALEP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 939342971 155 EegsTLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGRCHAF 219
Cdd:cd03220 162 D---ILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-212 |
1.15e-18 |
|
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: 84.84 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLRRGsnevlhdihlqlppgQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVtlqgrpladwagqERARRLAVLP 81
Cdd:COG1245 356 LEVEGGEIREG---------------EVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-------------DEDLKISYKP 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 82 QVSSLGFSFRVEEVVGMGRMPHGTGQRRDAEIVEA-ALRaadawHLVERSYLALSGGERQRVHLARVLAQlwpgeEGSTL 160
Cdd:COG1245 408 QYISPDYDGTVEEFLRSANTDDFGSSYYKTEIIKPlGLE-----KLLDKNVKDLSGGELQRVAIAACLSR-----DADLY 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 939342971 161 LLDEPTSMLDPLHQHTTLEAVRRFADC-GAAVLVILHDLNLAARYCDRILLLE 212
Cdd:COG1245 478 LLDEPSAHLDVEQRLAVAKAIRRFAENrGKTAMVVDHDIYLIDYISDRLMVFE 530
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
12-229 |
1.42e-18 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes 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 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. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 83.75 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 12 GSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQE----RARRLAVLPQVSSLG 87
Cdd:TIGR01186 4 GGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVElrevRRKKIGMVFQQFALF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 88 FSFRVEEVVGMGRMPHGTGQRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQlwpgeEGSTLLLDEPTS 167
Cdd:TIGR01186 84 PHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAA-----EPDILLMDEAFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 939342971 168 MLDPLHQHTTLEAVRRFAD-CGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPEAAL-TPA 229
Cdd:TIGR01186 159 ALDPLIRDSMQDELKKLQAtLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILrNPA 222
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-227 |
1.92e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 81.96 E-value: 1.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLRRGSNE--VLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLAdwagQERARRLA 78
Cdd:PRK13632 7 MIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIS----KENLKEIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 79 vlpqvSSLGFSFR----------VEEVVGMG----RMPHgtgQRRDAEIVEAALRAADAWHLvERSYLALSGGERQRVHL 144
Cdd:PRK13632 83 -----KKIGIIFQnpdnqfigatVEDDIAFGlenkKVPP---KKMKDIIDDLAKKVGMEDYL-DKEPQNLSGGQKQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 145 ARVLAqLWPgeegSTLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLV-ILHDLNLAARyCDRILLLEQGRCHAFATPE 223
Cdd:PRK13632 154 ASVLA-LNP----EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLIsITHDMDEAIL-ADKVIVFSEGKLIAQGKPK 227
|
....
gi 939342971 224 AALT 227
Cdd:PRK13632 228 EILN 231
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
2-212 |
3.47e-18 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 83.32 E-value: 3.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLRRGsnevlhdihlqlppgQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVtlqgrpladwagqERARRLAVLP 81
Cdd:PRK13409 355 LEVEGGEIYEG---------------EVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV-------------DPELKISYKP 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 82 QVSSLGFSFRVEEVVGMGRMPHGTGQRRdAEIVEAaLRAADawhLVERSYLALSGGERQRVHLARVLAQlwpgeEGSTLL 161
Cdd:PRK13409 407 QYIKPDYDGTVEDLLRSITDDLGSSYYK-SEIIKP-LQLER---LLDKNVKDLSGGELQRVAIAACLSR-----DADLYL 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 939342971 162 LDEPTSMLDPLHQHTTLEAVRRFAD-CGAAVLVILHDLNLAARYCDRILLLE 212
Cdd:PRK13409 477 LDEPSAHLDVEQRLAVAKAIRRIAEeREATALVVDHDIYMIDYISDRLMVFE 528
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-224 |
4.00e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 81.17 E-value: 4.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQG---RPLADWAGQE------ 72
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtiNLVRDKDGQLkvadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 73 -----RARRLAVLPQVSSLGFSFRVEEVVgmgRMPHGTGQRRDAEIVEAALRAADAWHLVERSY----LALSGGERQRVH 143
Cdd:PRK10619 86 qlrllRTRLTMVFQHFNLWSHMTVLENVM---EAPIQVLGLSKQEARERAVKYLAKVGIDERAQgkypVHLSGGQQQRVS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 144 LARVLAQlwpgeEGSTLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPE 223
Cdd:PRK10619 163 IARALAM-----EPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPE 237
|
.
gi 939342971 224 A 224
Cdd:PRK10619 238 Q 238
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
16-227 |
4.10e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 83.63 E-value: 4.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 16 VLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAVLPQVSSLgFSfrveev 95
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVL-FS------ 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 96 vgmgrmphGT--------GQRRDAEIVEAALRAadawHL---VERSYLAL-----------SGGERQRVHLARVLAQlwp 153
Cdd:PLN03130 1327 --------GTvrfnldpfNEHNDADLWESLERA----HLkdvIRRNSLGLdaevseagenfSVGQRQLLSLARALLR--- 1391
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 939342971 154 geEGSTLLLDEPTSML----DPLHQHTTLEavrRFADCgaAVLVILHDLNLAARyCDRILLLEQGRCHAFATPEAALT 227
Cdd:PLN03130 1392 --RSKILVLDEATAAVdvrtDALIQKTIRE---EFKSC--TMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLS 1461
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-252 |
4.13e-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: 80.53 E-value: 4.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 27 GQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVtlqGRPLADwagqerarrLAVLPQVSSLGFSFRVEEVVGMGRMPHGTG 106
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI---EIELDT---------VSYKPQYIKADYEGTVRDLLSSITKDFYTH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 107 QRRDAEIVEAaLRAADawhLVERSYLALSGGERQRVHLARVLAQlwpgeEGSTLLLDEPTSMLDPLHQHTTLEAVRRFAD 186
Cdd:cd03237 93 PYFKTEIAKP-LQIEQ---ILDREVPELSGGELQRVAIAACLSK-----DADIYLLDEPSAYLDVEQRLMASKVIRRFAE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 939342971 187 -CGAAVLVILHDLNLAARYCDRILLLE-QGRCHAFATPEAALTPAALKAVYGIDVLVQAHPERGHPLI 252
Cdd:cd03237 164 nNEKTAFVVEHDIIMIDYLADRLIVFEgEPSVNGVANPPQSLRSGMNRFLKNLDITFRRDPETGRPRI 231
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
15-219 |
4.44e-18 |
|
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: 83.06 E-value: 4.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 15 EVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGelaPDRgrvtlqgrplaDWAGQERAR---RLAVLPQVSSLGFSFR 91
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG---VDK-----------DFNGEARPQpgiKVGYLPQEPQLDPTKT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 92 VEEVVGMGRMPHGTGQRRDAEI--------------------VEAALRAADAWHL---VERSYLAL------------SG 136
Cdd:TIGR03719 85 VRENVEEGVAEIKDALDRFNEIsakyaepdadfdklaaeqaeLQEIIDAADAWDLdsqLEIAMDALrcppwdadvtklSG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 137 GERQRVHLARVLAQlwpgeEGSTLLLDEPTSMLDP-----LHQHttleaVRRFAdcgAAVLVILHDlnlaaRY-----CD 206
Cdd:TIGR03719 165 GERRRVALCRLLLS-----KPDMLLLDEPTNHLDAesvawLERH-----LQEYP---GTVVAVTHD-----RYfldnvAG 226
|
250
....*....|...
gi 939342971 207 RILLLEQGRCHAF 219
Cdd:TIGR03719 227 WILELDRGRGIPW 239
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
24-198 |
5.26e-18 |
|
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: 82.91 E-value: 5.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 24 LP---PGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVtlqGRPlADW-------AG---QERARRLA------------ 78
Cdd:COG1245 93 LPvpkKGKVTGILGPNGIGKSTALKILSGELKPNLGDY---DEE-PSWdevlkrfRGtelQDYFKKLAngeikvahkpqy 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 79 --VLPQVsslgFSFRVEEVVGmgrmphGTGQRRDA-EIVEA-ALRaadawHLVERSYLALSGGERQRVHLARVLAQlwpg 154
Cdd:COG1245 169 vdLIPKV----FKGTVRELLE------KVDERGKLdELAEKlGLE-----NILDRDISELSGGELQRVAIAAALLR---- 229
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 939342971 155 eEGSTLLLDEPTSMLDpLHQHTTL-EAVRRFADCGAAVLVILHDL 198
Cdd:COG1245 230 -DADFYFFDEPSSYLD-IYQRLNVaRLIRELAEEGKYVLVVEHDL 272
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-215 |
5.52e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 82.97 E-value: 5.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 20 IHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELaPDRGRVTLQGRPLADWAGQERARRLAVLPQVSSLgFSFRVEEVVGMG 99
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQL-PHGTLRDNVLLG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 100 RmPHGTgqrrDAEIvEAALRAADAWHLVERSYL-----------ALSGGERQRVHLARVLAQlwpgeEGSTLLLDEPTSM 168
Cdd:PRK11174 447 N-PDAS----DEQL-QQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQ-----PCQLLLLDEPTAS 515
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 939342971 169 LDPLHQHTTLEAVRRfADCGAAVLVILHDLN-LAAryCDRILLLEQGR 215
Cdd:PRK11174 516 LDAHSEQLVMQALNA-ASRRQTTLMVTHQLEdLAQ--WDQIWVMQDGQ 560
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
7-227 |
5.72e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 83.10 E-value: 5.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 7 LYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAVLPQvSSL 86
Cdd:PLN03232 1242 LRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQ-SPV 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 87 GFS----FRVEEVvgmgrmphgtGQRRDAEIVEAALRAadawHL---VERSYLAL-----------SGGERQRVHLARVL 148
Cdd:PLN03232 1321 LFSgtvrFNIDPF----------SEHNDADLWEALERA----HIkdvIDRNPFGLdaevseggenfSVGQRQLLSLARAL 1386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 149 AQlwpgeEGSTLLLDEPTSML----DPLHQHTTLEavrRFADCgaAVLVILHDLNLAARyCDRILLLEQGRCHAFATPEA 224
Cdd:PLN03232 1387 LR-----RSKILVLDEATASVdvrtDSLIQRTIRE---EFKSC--TMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQE 1455
|
...
gi 939342971 225 ALT 227
Cdd:PLN03232 1456 LLS 1458
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
13-222 |
6.09e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 80.93 E-value: 6.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 13 SNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLqgrplADWAGQERARRLAVLPQVSSLGFSFRV 92
Cdd:PRK13643 18 ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-----GDIVVSSTSKQKEIKPVRKKVGVVFQF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 93 EEV----------VGMGRMPHGT----GQRRDAEIVEAALRAADAWhlvERSYLALSGGERQRVHLARVLAQlwpgeEGS 158
Cdd:PRK13643 93 PESqlfeetvlkdVAFGPQNFGIpkekAEKIAAEKLEMVGLADEFW---EKSPFELSGGQMRRVAIAGILAM-----EPE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 939342971 159 TLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATP 222
Cdd:PRK13643 165 VLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTP 228
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
3-217 |
9.51e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 79.15 E-value: 9.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 3 HVEGLYLrrGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERA---RRLAV 79
Cdd:PRK10908 6 HVSKAYL--GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPflrRQIGM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 80 LPQVSSLGFSFRVEEVVGMGRMPHGTGQRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQlwpgeEGST 159
Cdd:PRK10908 84 IFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVN-----KPAV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 939342971 160 LLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGRCH 217
Cdd:PRK10908 159 LLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-227 |
1.48e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 79.19 E-value: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVL--CGELAPD---RGRVTLQGRPLADWAGQERARR 76
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrLIELYPEarvSGEVYLDGQDIFKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 77 LAVLPQVSSLGFSFRVEEVVGMG-RMPHGTGQRRD-AEIVEAALRAADAWHLVERSYLA----LSGGERQRVHLARVLAQ 150
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALGlKLNRLVKSKKElQERVRWALEKAQLWDEVKDRLDApagkLSGGQQQRLCIARALAF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 151 lwpgeEGSTLLLDEPTSMLDPLHQhTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGRC-------HAFATPE 223
Cdd:PRK14247 164 -----QPEVLLADEPTANLDPENT-AKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIvewgptrEVFTNPR 237
|
....
gi 939342971 224 AALT 227
Cdd:PRK14247 238 HELT 241
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
17-223 |
1.49e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 79.41 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 17 LHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAVLPQ------VSSLgfsf 90
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQnpdnqfVGSI---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 91 rVEEVVGMGRMPHGTGQRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAqLWPgeegSTLLLDEPTSMLD 170
Cdd:PRK13648 101 -VKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLA-LNP----SVIILDEATSMLD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 939342971 171 PLHQHTTLEAVRRF-ADCGAAVLVILHDLNLAARyCDRILLLEQGRCHAFATPE 223
Cdd:PRK13648 175 PDARQNLLDLVRKVkSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPT 227
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
17-227 |
1.59e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 79.87 E-value: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 17 LHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAvlpQVSSLGFSF------ 90
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKKLR---KKVSLVFQFpeaqlf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 91 --RVEEVVGMGRMPHGTGqrrDAEIVEAALRaadaW--------HLVERSYLALSGGERQRVHLARVLAqlwpgEEGSTL 160
Cdd:PRK13641 100 enTVLKDVEFGPKNFGFS---EDEAKEKALK----WlkkvglseDLISKSPFELSGGQMRRVAIAGVMA-----YEPEIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 939342971 161 LLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPEAALT 227
Cdd:PRK13641 168 CLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFS 234
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-201 |
2.18e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 77.99 E-value: 2.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRL--- 77
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLghr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 78 -AVLPQVSslgfsfrVEEVVGMGRMPHGTGQRRdaeiVEAALRAADAWHLVERSYLALSGGERQRVHLARVLA---QLWp 153
Cdd:PRK13539 82 nAMKPALT-------VAENLEFWAAFLGGEELD----IAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVsnrPIW- 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 939342971 154 geegstlLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILH-DLNLA 201
Cdd:PRK13539 150 -------ILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATHiPLGLP 191
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-236 |
2.32e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 78.73 E-value: 2.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVL-----CGELAPDRGRVTLQGRPL--ADWAGQERA 74
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIysPDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 75 RRLAVLPQVSSLGFSFRVEEVVGMGRMPHGTGQRRDA--EIVEAALRAADAWHLVE---RSYLA-LSGGERQRVHLARVL 148
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKKEldERVEWALKKAALWDEVKdrlNDYPSnLSGGQRQRLVIARAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 149 AQlwpgeEGSTLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVIlHDLNLAARYCDRILLLEQGRC-------HAFAT 221
Cdd:PRK14267 165 AM-----KPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVT-HSPAQAARVSDYVAFLYLGKLievgptrKVFEN 238
|
250
....*....|....*
gi 939342971 222 PEAALTPAALKAVYG 236
Cdd:PRK14267 239 PEHELTEKYVTGALG 253
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
10-231 |
2.94e-17 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 79.76 E-value: 2.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 10 RRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERA-----RRLAVLPQVs 84
Cdd:PRK11432 15 RFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDicmvfQSYALFPHM- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 85 SLGfsfrveEVVGMGRMPHGTGQRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAqLWPgeegSTLLLDE 164
Cdd:PRK11432 94 SLG------ENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALI-LKP----KVLLFDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 939342971 165 PTSMLDPLHQHTTLEAVR----RFadcGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATP-EAALTPAAL 231
Cdd:PRK11432 163 PLSNLDANLRRSMREKIRelqqQF---NITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPqELYRQPASR 231
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
8-215 |
3.01e-17 |
|
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: 77.97 E-value: 3.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 8 YLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAVLPQVSSLg 87
Cdd:cd03249 10 YPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVL- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 88 FSFRVEEVVGMGRMPhgtgqrRDAEIVEAALRAADAwH------------LVERSYLALSGGERQRVHLARVLAQlwpge 155
Cdd:cd03249 89 FDGTIAENIRYGKPD------ATDEEVEEAAKKANI-HdfimslpdgydtLVGERGSQLSGGQKQRIAIARALLR----- 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 156 EGSTLLLDEPTSMLDPLHQHTTLEAVRRFADcGAAVLVILHDLNlAARYCDRILLLEQGR 215
Cdd:cd03249 157 NPKILLLDEATSALDAESEKLVQEALDRAMK-GRTTIVIAHRLS-TIRNADLIAVLQNGQ 214
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
19-223 |
3.14e-17 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 79.88 E-value: 3.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 19 DIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERArrLAVLPQVSSLGFSFRVEEVVGM 98
Cdd:PRK11607 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRP--INMMFQSYALFPHMTVEQNIAF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 99 G----RMPHGTGQRRDAEIVEAAlraadawHLVE---RSYLALSGGERQRVHLARVLAQlwpgeEGSTLLLDEPTSMLD- 170
Cdd:PRK11607 115 GlkqdKLPKAEIASRVNEMLGLV-------HMQEfakRKPHQLSGGQRQRVALARSLAK-----RPKLLLLDEPMGALDk 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 939342971 171 PLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPE 223
Cdd:PRK11607 183 KLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPE 235
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-216 |
4.47e-17 |
|
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: 80.11 E-value: 4.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLR----RGSNEVLHDIHLQLPPGQVVGVLGPNGAGKS----SLLSVLCGELAPDRGRVTLQGRPLADWAGQE 72
Cdd:COG4172 6 LLSVEDLSVAfgqgGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 73 ----RARRLAVLPQ--VSSLGFSFRVEEVVGMGRMPHGTGQRRDAE-----------IVEAALRAADAWHlversylALS 135
Cdd:COG4172 86 lrriRGNRIAMIFQepMTSLNPLHTIGKQIAEVLRLHRGLSGAAARaralellervgIPDPERRLDAYPH-------QLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 136 GGERQRVHLARVLAQlwpgeEGSTLLLDEPTSMLDPLHQHTTLEAVRRF-ADCGAAVLVILHDLNLAARYCDRILLLEQG 214
Cdd:COG4172 159 GGQRQRVMIAMALAN-----EPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLITHDLGVVRRFADRVAVMRQG 233
|
..
gi 939342971 215 RC 216
Cdd:COG4172 234 EI 235
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-236 |
5.27e-17 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 77.72 E-value: 5.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAVL 80
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 81 P-QVSSLGFSFRVEEVVGMGRMPH----------GTGQRRDAEivEAALRAADAW-------HLVERSYLALSGGERQRV 142
Cdd:PRK11300 85 TfQHVRLFREMTVIENLLVAQHQQlktglfsgllKTPAFRRAE--SEALDRAATWlervgllEHANRQAGNLAYGQQRRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 143 HLARVLAQlwpgeEGSTLLLDEPTSMLDPLHQHTTLEAVRRFAD-CGAAVLVILHDLNLAARYCDRILLLEQGRCHAFAT 221
Cdd:PRK11300 163 EIARCMVT-----QPEILMLDEPAAGLNPKETKELDELIAELRNeHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGT 237
|
250
....*....|....*.
gi 939342971 222 PEAALT-PAALKAVYG 236
Cdd:PRK11300 238 PEEIRNnPDVIKAYLG 253
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-227 |
5.74e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 77.78 E-value: 5.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLadWAGQErARRLAVL 80
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVL--YFGKD-IFQIDAI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 81 PQVSSLGFSFR---------VEEVVGMGRMPHGTGQRRD-AEIVEAALRAADAWHLVERSYLA----LSGGERQRVHLAR 146
Cdd:PRK14246 87 KLRKEVGMVFQqpnpfphlsIYDNIAYPLKSHGIKEKREiKKIVEECLRKVGLWKEVYDRLNSpasqLSGGQQQRLTIAR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 147 VLAqLWPgeegSTLLLDEPTSMLDPLHQHTTLEAVRRFADcGAAVLVILHDLNLAARYCDRILLLEQGRC-------HAF 219
Cdd:PRK14246 167 ALA-LKP----KVLLMDEPTSMIDIVNSQAIEKLITELKN-EIAIVIVSHNPQQVARVADYVAFLYNGELvewgssnEIF 240
|
....*...
gi 939342971 220 ATPEAALT 227
Cdd:PRK14246 241 TSPKNELT 248
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
10-198 |
5.78e-17 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 77.79 E-value: 5.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 10 RRGSNE-VLHdihlQLP---PGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVT-----------LQGRPLADWAGQ--E 72
Cdd:cd03236 9 RYGPNSfKLH----RLPvprEGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDdppdwdeildeFRGSELQNYFTKllE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 73 RARRLAVLPQVSSL---GFSFRVEEVVgmgRMPHGTGQRRdaEIVEA-ALRaadawHLVERSYLALSGGERQRVHLARVL 148
Cdd:cd03236 85 GDVKVIVKPQYVDLipkAVKGKVGELL---KKKDERGKLD--ELVDQlELR-----HVLDRNIDQLSGGELQRVAIAAAL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 939342971 149 AQlwpgeEGSTLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDL 198
Cdd:cd03236 155 AR-----DADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDL 199
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-239 |
5.91e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 78.21 E-value: 5.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGL---YLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRL 77
Cdd:PRK13642 4 ILEVENLvfkYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 78 AVLPQVSSLGF-SFRVEEVVGMGRMPHGTGQRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAqLWPgee 156
Cdd:PRK13642 84 GMVFQNPDNQFvGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIA-LRP--- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 157 gSTLLLDEPTSMLDPLHQHTTLEAVRRFAD-CGAAVLVILHDLNLAARyCDRILLLEQGRCHAFATPEAALTPAALKAVY 235
Cdd:PRK13642 160 -EIIILDESTSMLDPTGRQEIMRVIHEIKEkYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDMVEI 237
|
....
gi 939342971 236 GIDV 239
Cdd:PRK13642 238 GLDV 241
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
17-224 |
6.00e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 78.23 E-value: 6.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 17 LHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAVLPQVSSLGF-SFRVEEV 95
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQNPDNQFvGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 96 VGMGRMPHGTGQRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAqLWPgeegSTLLLDEPTSMLDP---L 172
Cdd:PRK13650 103 VAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVA-MRP----KIIILDEATSMLDPegrL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 939342971 173 HQHTTLEAVRRfaDCGAAVLVILHDLNLAArYCDRILLLEQGRCHAFATPEA 224
Cdd:PRK13650 178 ELIKTIKGIRD--DYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRE 226
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
12-223 |
7.74e-17 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 78.59 E-value: 7.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 12 GSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWagQERARRLAVLPQVSSLgfsFR 91
Cdd:PRK10851 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL--HARDRKVGFVFQHYAL---FR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 92 ---VEEVVGMGRMPHGTGQRRDAEI----VEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQlwpgeEGSTLLLDE 164
Cdd:PRK10851 88 hmtVFDNIAFGLTVLPRRERPNAAAikakVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAV-----EPQILLLDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 939342971 165 PTSMLDP------------LHQHTTLEAVrrfadcgaavlVILHDLNLAARYCDRILLLEQGRCHAFATPE 223
Cdd:PRK10851 163 PFGALDAqvrkelrrwlrqLHEELKFTSV-----------FVTHDQEEAMEVADRVVVMSQGNIEQAGTPD 222
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
16-239 |
9.41e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 77.53 E-value: 9.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 16 VLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPD---RGRVTLQGRPLAD---WAGQERARRLAVLPQVSSLGFS 89
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDdnpNSKITVDGITLTAktvWDIREKVGIVFQNPDNQFVGAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 90 frVEEVVGMGRMPHGTGQRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQlwpgeEGSTLLLDEPTSML 169
Cdd:PRK13640 102 --VGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAV-----EPKIIILDESTSML 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 939342971 170 DPLHQHTTLEAVRRFA-DCGAAVLVILHDLNLAArYCDRILLLEQGRCHAFATPEAALTPAALKAVYGIDV 239
Cdd:PRK13640 175 DPAGKEQILKLIRKLKkKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPVEIFSKVEMLKEIGLDI 244
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
19-197 |
1.30e-16 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 78.62 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 19 DIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRV----TLQgrpLAdWAGQERArrlavlpqvsSLGFSFRVEE 94
Cdd:PRK11819 342 DLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIkigeTVK---LA-YVDQSRD----------ALDPNKTVWE 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 95 VVGMGrmphgtgqrrdAEIVEAALRAADAwhlveRSYLA---------------LSGGERQRVHLARVLAQlwpgeEGST 159
Cdd:PRK11819 408 EISGG-----------LDIIKVGNREIPS-----RAYVGrfnfkggdqqkkvgvLSGGERNRLHLAKTLKQ-----GGNV 466
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 939342971 160 LLLDEPTSMLDPlhqhTTL----EAVRRFADCgaaVLVILHD 197
Cdd:PRK11819 467 LLLDEPTNDLDV----ETLraleEALLEFPGC---AVVISHD 501
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
9-227 |
1.61e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 78.59 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 9 LRR--GSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSL-LSVLcgELAPDRGRVTLQGRPLADWAGQER---ARRLAVLPQ 82
Cdd:PRK15134 292 LKRtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTTgLALL--RLINSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQ 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 83 --VSSLGFSFRVEEVVGMG---RMPHGTGQRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAqLWPgeeg 157
Cdd:PRK15134 370 dpNSSLNPRLNVLQIIEEGlrvHQPTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALI-LKP---- 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 939342971 158 STLLLDEPTSMLDPLHQHTTLEAVRRF-ADCGAAVLVILHDLNLAARYCDRILLL------EQGRC-HAFATPEAALT 227
Cdd:PRK15134 445 SLIILDEPTSSLDKTVQAQILALLKSLqQKHQLAYLFISHDLHVVRALCHQVIVLrqgevvEQGDCeRVFAAPQQEYT 522
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-215 |
2.15e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.14 E-value: 2.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLRRGSN-EVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADW-AGQERARRLAV 79
Cdd:COG3845 258 LEVENLSVRDDRGvPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLsPRERRRLGVAY 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 80 LPQ-----VSSLGFS---------FRVEEVVGMGRMPHGTGQRRDAEIVEA-ALRAADAWHLVErsylALSGGERQRVHL 144
Cdd:COG3845 338 IPEdrlgrGLVPDMSvaenlilgrYRRPPFSRGGFLDRKAIRAFAEELIEEfDVRTPGPDTPAR----SLSGGNQQKVIL 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 939342971 145 ARVLAQlwpgeEGSTLLLDEPTSMLDPlhqhTTLEAVRR----FADCGAAVLVILHDLNLAARYCDRILLLEQGR 215
Cdd:COG3845 414 ARELSR-----DPKLLIAAQPTRGLDV----GAIEFIHQrlleLRDAGAAVLLISEDLDEILALSDRIAVMYEGR 479
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-233 |
2.65e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 77.93 E-value: 2.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLRRGSNEVL-HDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGeLAPD-RGRVTlqgRPladwagqeRARRLA 78
Cdd:COG4178 362 ALALEDLTLRTPDGRPLlEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG-LWPYgSGRIA---RP--------AGARVL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 79 VLPQVSslgfsfrveevvgmgRMPHGT----------GQRRDAEIVEAALRAADAWHLVERsyLA--------LSGGERQ 140
Cdd:COG4178 430 FLPQRP---------------YLPLGTlreallypatAEAFSDAELREALEAVGLGHLAER--LDeeadwdqvLSLGEQQ 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 141 RVHLARVLAQLwPgeegSTLLLDEPTSMLDPLHQHTTLEAVRRfADCGAAVLVILHDLNLAArYCDRILLLEqgrchafA 220
Cdd:COG4178 493 RLAFARLLLHK-P----DWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGHRSTLAA-FHDRVLELT-------G 558
|
250
....*....|...
gi 939342971 221 TPEAALTPAALKA 233
Cdd:COG4178 559 DGSWQLLPAEAPA 571
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
2-201 |
3.14e-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: 74.84 E-value: 3.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGqERARRLAVLP 81
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD-SIARGLLYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 82 QVSSLGFSFRVEEVVGMGRMPHGTGQrrdaeiVEAALRAADAWHLVERSYLALSGGERQRVHLARVL---AQLWpgeegs 158
Cdd:cd03231 80 HAPGIKTTLSVLENLRFWHADHSDEQ------VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLlsgRPLW------ 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 939342971 159 tlLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILH-DLNLA 201
Cdd:cd03231 148 --ILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHqDLGLS 189
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-206 |
4.36e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 75.59 E-value: 4.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVL--CGELAPD---RGRVTLQGRPLadWAGQ----E 72
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLIPGfrvEGKVTFHGKNL--YAPDvdpvE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 73 RARRLAVLPQVSSlGFSFRVEEVVGMGRMPHGTGQRRDaEIVEAALRAADAWHLVE----RSYLALSGGERQRVHLARVL 148
Cdd:PRK14243 89 VRRRIGMVFQKPN-PFPKSIYDNIAYGARINGYKGDMD-ELVERSLRQAALWDEVKdklkQSGLSLSGGQQQRLCIARAI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 939342971 149 AQlwpgeEGSTLLLDEPTSMLDPLhqhTTL-------EAVRRFadcgaAVLVILHDLNLAARYCD 206
Cdd:PRK14243 167 AV-----QPEVILMDEPCSALDPI---STLrieelmhELKEQY-----TIIIVTHNMQQAARVSD 218
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
15-217 |
5.08e-16 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 77.08 E-value: 5.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 15 EVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQgrpladwAGQerarRLAVLPQVSSLGFSFRVEE 94
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPA-------PGI----KVGYLPQEPQLDPEKTVRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 95 VVGMGrmphgTGQRRDA-----EI--------------------VEAALRAADAWHL---VERSYLAL------------ 134
Cdd:PRK11819 90 NVEEG-----VAEVKAAldrfnEIyaayaepdadfdalaaeqgeLQEIIDAADAWDLdsqLEIAMDALrcppwdakvtkl 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 135 SGGERQRVHLARVLAqlwpgEEGSTLLLDEPTSMLDP-----LHQHttleaVRRFAdcgAAVLVILHDlnlaaRY----- 204
Cdd:PRK11819 165 SGGERRRVALCRLLL-----EKPDMLLLDEPTNHLDAesvawLEQF-----LHDYP---GTVVAVTHD-----RYfldnv 226
|
250
....*....|...
gi 939342971 205 CDRILLLEQGRCH 217
Cdd:PRK11819 227 AGWILELDRGRGI 239
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
24-198 |
6.04e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 76.77 E-value: 6.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 24 LP---PGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQgrplADW-------AG---QERARRLA------------ 78
Cdd:PRK13409 93 LPipkEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEE----PSWdevlkrfRGtelQNYFKKLYngeikvvhkpqy 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 79 --VLPQVsslgFSFRVEEVVgmgrmpHGTGQRRDA-EIVEA-ALRaadawHLVERSYLALSGGERQRVHLARVLAQlwpg 154
Cdd:PRK13409 169 vdLIPKV----FKGKVRELL------KKVDERGKLdEVVERlGLE-----NILDRDISELSGGELQRVAIAAALLR---- 229
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 939342971 155 eEGSTLLLDEPTSMLDPLHQHTTLEAVRRFADcGAAVLVILHDL 198
Cdd:PRK13409 230 -DADFYFFDEPTSYLDIRQRLNVARLIRELAE-GKYVLVVEHDL 271
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-236 |
6.32e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 75.13 E-value: 6.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 16 VLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLC---GELAPDR--GRVTLQGRPLADWAG-QERARRLAVLPQVSSlGFS 89
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNrmnDKVSGYRysGDVLLGGRSIFNYRDvLEFRRRVGMLFQRPN-PFP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 90 FRVEEVVGMGRMPHGTGQRRDAE-IVEAALRAADAWHLVER----SYLALSGGERQRVHLARVLAQlwpgeEGSTLLLDE 164
Cdd:PRK14271 115 MSIMDNVLAGVRAHKLVPRKEFRgVAQARLTEVGLWDAVKDrlsdSPFRLSGGQQQLLCLARTLAV-----NPEVLLLDE 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 939342971 165 PTSMLDPLHQHTTLEAVRRFADcGAAVLVILHDLNLAARYCDRILLLEQGRC-------HAFATPEAALTPAALKAVYG 236
Cdd:PRK14271 190 PTSALDPTTTEKIEEFIRSLAD-RLTVIIVTHNLAQAARISDRAALFFDGRLveegpteQLFSSPKHAETARYVAGLSG 267
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
13-215 |
8.03e-16 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 76.47 E-value: 8.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 13 SNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAVLPQVSSLgFSFRV 92
Cdd:TIGR01192 347 SSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGL-FNRSI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 93 EEVVGMGRMphgtgQRRDAEIVEAALRAADAWHLVERS--YLA--------LSGGERQRVHLARVLAQLWPgeegsTLLL 162
Cdd:TIGR01192 426 RENIRLGRE-----GATDEEVYEAAKAAAAHDFILKRSngYDTlvgergnrLSGGERQRLAIARAILKNAP-----ILVL 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 939342971 163 DEPTSMLDPlhqhTTLEAVRRFADC---GAAVLVILHDLNlAARYCDRILLLEQGR 215
Cdd:TIGR01192 496 DEATSALDV----ETEARVKNAIDAlrkNRTTFIIAHRLS-TVRNADLVLFLDQGR 546
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
16-239 |
1.04e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 74.74 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 16 VLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLAD----WAGQERARRLAVLPQ---VSSLgf 88
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDeenlWDIRNKAGMVFQNPDnqiVATI-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 89 sfrVEEVVGMGRMPHGTGQRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAqLWPgeegSTLLLDEPTSM 168
Cdd:PRK13633 103 ---VEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILA-MRP----ECIIFDEPTAM 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 939342971 169 LDPLHQHTTLEAVRRFAD-CGAAVLVILHDLNLAARyCDRILLLEQGRCHAFATPEAALTPAALKAVYGIDV 239
Cdd:PRK13633 175 LDPSGRREVVNTIKELNKkYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKEVEMMKKIGLDV 245
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-227 |
1.07e-15 |
|
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: 76.02 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGeLAPD---RGRVTLQGRPL--ADWAGQERA- 74
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHgtwDGEIYWSGSPLkaSNIRDTERAg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 75 -----RRLAVLPQVSSLGFSFRVEEVVGMGRMPHGTGQRRDAEIVEAALRAADAwhLVERSYLALSGGERQRVHLARVLa 149
Cdd:TIGR02633 80 iviihQELTLVPELSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDAD--NVTRPVGDYGGGQQQLVEIAKAL- 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 939342971 150 qlwpGEEGSTLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGRcHAFATPEAALT 227
Cdd:TIGR02633 157 ----NKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ-HVATKDMSTMS 229
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-214 |
2.77e-15 |
|
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: 72.50 E-value: 2.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 17 LHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADwAGQERA---RRLAVLPQVSSL-GFSFRV 92
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE-PGPDRMvvfQNYSLLPWLTVReNIALAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 93 EEVvgmgrMPH-GTGQRRdaEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAqLWPgeegSTLLLDEPTSMLDP 171
Cdd:TIGR01184 80 DRV-----LPDlSKSERR--AIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALS-IRP----KVLLLDEPFGALDA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 939342971 172 LHQHTTLEAVRRFA-DCGAAVLVILHDLNLAARYCDRILLLEQG 214
Cdd:TIGR01184 148 LTRGNLQEELMQIWeEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
17-222 |
3.47e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 73.16 E-value: 3.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 17 LHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADwagqERARRLAVLPQVsslGFSFR----- 91
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD----KKVKLSDIRKKV---GLVFQypeyq 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 92 -----VEEVVGMGRMPHGTGQRRDAEIVEAALRAA--DAWHLVERSYLALSGGERQRVHLARVLAQlwpgeEGSTLLLDE 164
Cdd:PRK13637 96 lfeetIEKDIAFGPINLGLSEEEIENRVKRAMNIVglDYEDYKDKSPFELSGGQKRRVAIAGVVAM-----EPKILILDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 939342971 165 PTSMLDPLHQHTTLEAVRRFAD-CGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATP 222
Cdd:PRK13637 171 PTAGLDPKGRDEILNKIKELHKeYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
12-252 |
4.17e-15 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 73.68 E-value: 4.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 12 GSNEV--LHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQE--RARRlavlpqvsSLG 87
Cdd:PRK11153 14 GGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrKARR--------QIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 88 FSFR---------VEEVVGM----GRMPHGTGQRRDAEIVEaalraadawhLVERSYLA------LSGGERQRVHLARVL 148
Cdd:PRK11153 86 MIFQhfnllssrtVFDNVALplelAGTPKAEIKARVTELLE----------LVGLSDKAdrypaqLSGGQKQRVAIARAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 149 AQlwpgeEGSTLLLDEPTSMLDPLHQHTTLEAVRRF-ADCGAAVLVILHDLNLAARYCDRILLLEQGRC-------HAFA 220
Cdd:PRK11153 156 AS-----NPKVLLCDEATSALDPATTRSILELLKDInRELGLTIVLITHEMDVVKRICDRVAVIDAGRLveqgtvsEVFS 230
|
250 260 270
....*....|....*....|....*....|....*....
gi 939342971 221 TPEAALTPAALKAVYGID----VLVQAHPER---GHPLI 252
Cdd:PRK11153 231 HPKHPLTREFIQSTLHLDlpedYLARLQAEPttgSGPLL 269
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
12-231 |
4.89e-15 |
|
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: 74.56 E-value: 4.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 12 GSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCgELAPDRGRVTLQGRPLADWAGQERARRLAVLPQ-VSSLGFSF 90
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDGVSWNSVTLQTWRKAFGVIPQkVFIFSGTF 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 91 RveevvgMGRMPHgtGQRRDAEI----VEAALRAADA-------WHLVERSYLaLSGGERQRVHLAR-VLAQlwpgeeGS 158
Cdd:TIGR01271 1309 R------KNLDPY--EQWSDEEIwkvaEEVGLKSVIEqfpdkldFVLVDGGYV-LSNGHKQLMCLARsILSK------AK 1373
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 939342971 159 TLLLDEPTSMLDPLhqhtTLEAVRR-----FADCgaavLVILHDLNLAARY-CDRILLLEQGRCHAFATPEAALTPAAL 231
Cdd:TIGR01271 1374 ILLLDEPSAHLDPV----TLQIIRKtlkqsFSNC----TVILSEHRVEALLeCQQFLVIEGSSVKQYDSIQKLLNETSL 1444
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
2-215 |
5.36e-15 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 72.02 E-value: 5.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCG--ELAPDRGRVTLQGRPLADWAGQERARRlav 79
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSILLDGEDILELSPDERARA--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 80 lpqvsSLGFSF----RVEEVVGMGRMPHGTGQRRDAEI-VEAALRAADAW--------HLVERsYLA--LSGGERQRVHL 144
Cdd:COG0396 78 -----GIFLAFqypvEIPGVSVSNFLRTALNARRGEELsAREFLKLLKEKmkelgldeDFLDR-YVNegFSGGEKKRNEI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 145 ARVLAQlwpgeEGSTLLLDEPTSMLDplhqhttLEAVR-------RFADCGAAVLVILHD---LNLAAryCDRILLLEQG 214
Cdd:COG0396 152 LQMLLL-----EPKLAILDETDSGLD-------IDALRivaegvnKLRSPDRGILIITHYqriLDYIK--PDFVHVLVDG 217
|
.
gi 939342971 215 R 215
Cdd:COG0396 218 R 218
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-170 |
6.52e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 70.99 E-value: 6.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADwAGQERARRLA-- 78
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRR-QRDEYHQDLLyl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 79 --------VLPQVSSLGFSFRVEEVVgmgrmphgtgqrrDAEIVEAALRAADawhLVERSYLA---LSGGERQRVHLARV 147
Cdd:PRK13538 80 ghqpgiktELTALENLRFYQRLHGPG-------------DDEALWEALAQVG---LAGFEDVPvrqLSAGQQRRVALARL 143
|
170 180
....*....|....*....|....*.
gi 939342971 148 L---AQLWpgeegstlLLDEPTSMLD 170
Cdd:PRK13538 144 WltrAPLW--------ILDEPFTAID 161
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
19-230 |
6.55e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 73.53 E-value: 6.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 19 DIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQE----RARRLAVLPQVSSLGFSFRVEE 94
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevRRKKIAMVFQSFALMPHMTVLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 95 VVGMGRMPHGTGQRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQlwpgeEGSTLLLDEPTSMLDPL-H 173
Cdd:PRK10070 126 NTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAI-----NPDILLMDEAFSALDPLiR 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 939342971 174 QHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPEAALTPAA 230
Cdd:PRK10070 201 TEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPA 257
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-223 |
7.27e-15 |
|
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: 73.68 E-value: 7.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCG--ELAPDRGRVTLQ----------------GR 63
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYHvalcekcgyverpskvGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 64 P--------------LADWAGQERA---RRLAVLPQVSslgFSFRVEEVV---GMGRMPHGTGQRRDAeiVEAALRAADA 123
Cdd:TIGR03269 81 PcpvcggtlepeevdFWNLSDKLRRrirKRIAIMLQRT---FALYGDDTVldnVLEALEEIGYEGKEA--VGRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 124 WHLVER-SYLA--LSGGERQRVHLARVLAQlwpgeEGSTLLLDEPTSMLDPLHQHTTLEAVRRFA-DCGAAVLVILHDLN 199
Cdd:TIGR03269 156 VQLSHRiTHIArdLSGGEKQRVVLARQLAK-----EPFLFLADEPTGTLDPQTAKLVHNALEEAVkASGISMVLTSHWPE 230
|
250 260
....*....|....*....|....
gi 939342971 200 LAARYCDRILLLEQGRCHAFATPE 223
Cdd:TIGR03269 231 VIEDLSDKAIWLENGEIKEEGTPD 254
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
15-215 |
1.76e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 71.66 E-value: 1.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 15 EVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGR-PladwagQERARRLA-----VLPQVSSLGF 88
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYvP------FKRRKEFArrigvVFGQRSQLWW 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 89 ------SFRVEEVvgMGRMPHGTGQRRDAEIVEaALRAADawhLVERSYLALSGGERQRVHLARVLaqLW-PgeegSTLL 161
Cdd:COG4586 110 dlpaidSFRLLKA--IYRIPDAEYKKRLDELVE-LLDLGE---LLDTPVRQLSLGQRMRCELAAAL--LHrP----KILF 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 939342971 162 LDEPTSMLDPLHQhttlEAVRRF-----ADCGAAVLVILHDLNLAARYCDRILLLEQGR 215
Cdd:COG4586 178 LDEPTIGLDVVSK----EAIREFlkeynRERGTTILLTSHDMDDIEALCDRVIVIDHGR 232
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
11-226 |
1.77e-14 |
|
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: 72.53 E-value: 1.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 11 RGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLqgRPLADWA--------GQERARR-LAVLP 81
Cdd:TIGR03269 294 RGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNV--RVGDEWVdmtkpgpdGRGRAKRyIGILH 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 82 QVSSLgFSFR-----VEEVVGMgRMPHGTGQRRDAEIVEAA-LRAADAWHLVERSYLALSGGERQRVHLARVLAQlwpge 155
Cdd:TIGR03269 372 QEYDL-YPHRtvldnLTEAIGL-ELPDELARMKAVITLKMVgFDEEKAEEILDKYPDELSEGERHRVALAQVLIK----- 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 939342971 156 EGSTLLLDEPTSMLDPLHQHTTLEAVRRF-ADCGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPEAAL 226
Cdd:TIGR03269 445 EPRIVILDEPTGTMDPITKVDVTHSILKArEEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
16-215 |
1.96e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 71.27 E-value: 1.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 16 VLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQgrpLADWAGQERA--------------------- 74
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWI---FKDEKNKKKTkekekvleklviqktrfkkik 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 75 ------RRLAVLPQVSSLG-FSFRVEEVVGMGRMPHGTGQRrdaeivEAALRAADAWHLV-------ERSYLALSGGERQ 140
Cdd:PRK13651 99 kikeirRRVGVVFQFAEYQlFEQTIEKDIIFGPVSMGVSKE------EAKKRAAKYIELVgldesylQRSPFELSGGQKR 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 939342971 141 RVHLARVLAQlwpgeEGSTLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGR 215
Cdd:PRK13651 173 RVALAGILAM-----EPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGK 242
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-215 |
2.05e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 71.97 E-value: 2.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLylrrGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPL-----ADW--AG--- 70
Cdd:COG1129 256 VLEVEGL----SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVrirspRDAirAGiay 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 71 --QERARR-------------LAVLPQVSSLGFSFRVEEvvgmgrmphgtgqRRDAE--IVEAALRAADAWHLVErsylA 133
Cdd:COG1129 332 vpEDRKGEglvldlsirenitLASLDRLSRGGLLDRRRE-------------RALAEeyIKRLRIKTPSPEQPVG----N 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 134 LSGGERQRVHLARVLAQlwpgeEGSTLLLDEPTSMLDP-----LHQhttleAVRRFADCGAAVLVILHDLNLAARYCDRI 208
Cdd:COG1129 395 LSGGNQQKVVLAKWLAT-----DPKVLILDEPTRGIDVgakaeIYR-----LIRELAAEGKAVIVISSELPELLGLSDRI 464
|
....*..
gi 939342971 209 LLLEQGR 215
Cdd:COG1129 465 LVMREGR 471
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
6-231 |
2.12e-14 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 71.90 E-value: 2.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 6 GLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERA-----RRLAVL 80
Cdd:PRK09452 19 GISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHvntvfQSYALF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 81 PQVSslgfsfrVEEVVGMG-RMphgtgQRR-DAEI---VEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQlwpge 155
Cdd:PRK09452 99 PHMT-------VFENVAFGlRM-----QKTpAAEItprVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVN----- 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 939342971 156 EGSTLLLDEPTSMLD-PLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATP-EAALTPAAL 231
Cdd:PRK09452 162 KPKVLLLDESLSALDyKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPrEIYEEPKNL 239
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
15-230 |
2.24e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 72.01 E-value: 2.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 15 EVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADwAGQERARRLAV--LPQVSSLGFSFRV 92
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCAR-LTPAKAHQLGIylVPQEPLLFPNLSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 93 EEVVGMGrMPhgtGQRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQlwpgeEGSTLLLDEPTSMLDPL 172
Cdd:PRK15439 104 KENILFG-LP---KRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMR-----DSRILILDEPTASLTPA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 939342971 173 HQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQG------RCHAFATPE--AALTPAA 230
Cdd:PRK15439 175 ETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGtialsgKTADLSTDDiiQAITPAA 240
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-172 |
2.80e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 70.45 E-value: 2.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLcGELAPDRGRVTLQGRplADWAGQE--------- 72
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGR--VEFFNQNiyerrvnln 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 73 RARRLAVLPQVSSLGFSFRVEEVVGMGRMPHGTGQRRDAE-IVEAALRAADAW----HLVERSYLALSGGERQRVHLARV 147
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLEIDdIVESALKDADLWdeikHKIHKSALDLSGGQQQRLCIARA 164
|
170 180
....*....|....*....|....*
gi 939342971 148 LAQlwpgeEGSTLLLDEPTSMLDPL 172
Cdd:PRK14258 165 LAV-----KPKVLLMDEPCFGLDPI 184
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
17-215 |
3.63e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 71.48 E-value: 3.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 17 LHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPL-------ADWAG-----QErarrLAVLPQVS 84
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfasttaALAAGvaiiyQE----LHLVPEMT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 85 slgfsfrVEEVVGMGRMPHGTGQRRDAEIVEAALRAADawHLVER-------SYLALsgGERQRVHLARVLAQlwpgeEG 157
Cdd:PRK11288 96 -------VAENLYLGQLPHKGGIVNRRLLNYEAREQLE--HLGVDidpdtplKYLSI--GQRQMVEIAKALAR-----NA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 158 STLLLDEPTSMLDplHQHTT--LEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGR 215
Cdd:PRK11288 160 RVIAFDEPTSSLS--AREIEqlFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGR 217
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
17-227 |
3.88e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.50 E-value: 3.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 17 LHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGeLAPD---RGRVTLQGRPLA-------DWAG-----QErarrLAVLP 81
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFEGEELQasnirdtERAGiaiihQE----LALVK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 82 QVSSLGFSFRVEEVVGMGRMPHGTGQRRDAEI-------VEAALRAADawhlversylaLSGGERQRVHLARVLAQlwpg 154
Cdd:PRK13549 96 ELSVLENIFLGNEITPGGIMDYDAMYLRAQKLlaqlkldINPATPVGN-----------LGLGQQQLVEIAKALNK---- 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 939342971 155 eEGSTLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGRcHAFATPEAALT 227
Cdd:PRK13549 161 -QARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR-HIGTRPAAGMT 231
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-172 |
6.13e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 70.92 E-value: 6.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 3 HVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQER-ARRLAVLP 81
Cdd:NF033858 3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAvCPRIAYMP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 82 QvsSLG----FSFRVEEVVG-MGRM-PHGTGQRRdAEIvEAALRAADAWHLVERSYLALSGGERQRVHLARVL---AQLw 152
Cdd:NF033858 83 Q--GLGknlyPTLSVFENLDfFGRLfGQDAAERR-RRI-DELLRATGLAPFADRPAGKLSGGMKQKLGLCCALihdPDL- 157
|
170 180
....*....|....*....|
gi 939342971 153 pgeegstLLLDEPTSMLDPL 172
Cdd:NF033858 158 -------LILDEPTTGVDPL 170
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
2-215 |
7.19e-14 |
|
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: 68.83 E-value: 7.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGElaPD----RGRVTLQGRPLADWAGQERARR- 76
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGH--PSyevtSGTILFKGQDLLELEPDERARAg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 77 --LAV-----LPQVSSLGFsfrVEEVVGMGRMPHGTGQRRDAE---IVEAALRAADawhlVERSYL------ALSGGERQ 140
Cdd:TIGR01978 79 lfLAFqypeeIPGVSNLEF---LRSALNARRSARGEEPLDLLDfekLLKEKLALLD----MDEEFLnrsvneGFSGGEKK 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 939342971 141 RVHLARvLAQLWPgeegSTLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLaARYC--DRILLLEQGR 215
Cdd:TIGR01978 152 RNEILQ-MALLEP----KLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHYQRL-LNYIkpDYVHVLLDGR 222
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-213 |
8.52e-14 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 70.58 E-value: 8.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQER-ARRLAV 79
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETpALPQPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 80 LPQVSSLGFSFRVEEvvgmgRMPHGTGQRRDAE---IVEAALRAADAWHL-----------------VERSYLALSGGER 139
Cdd:PRK10636 81 LEYVIDGDREYRQLE-----AQLHDANERNDGHaiaTIHGKLDAIDAWTIrsraasllhglgfsneqLERPVSDFSGGWR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 939342971 140 QRVHLARVLAQlwpgeEGSTLLLDEPTSMLDplhqhttLEAV----RRFADCGAAVLVILHDLNLAARYCDRILLLEQ 213
Cdd:PRK10636 156 MRLNLAQALIC-----RSDLLLLDEPTNHLD-------LDAViwleKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQ 221
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
28-222 |
1.60e-13 |
|
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: 70.04 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 28 QVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERaRRLAVLPQVSSLGFSFRVEEVVGMGRMPHGTGQ 107
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVR-QSLGMCPQHNILFHHLTVAEHILFYAQLKGRSW 1035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 108 RRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQlwpgeEGSTLLLDEPTSMLDPLHQHTTLEAVRRFADc 187
Cdd:TIGR01257 1036 EEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVG-----DAKVVVLDEPTSGVDPYSRRSIWDLLLKYRS- 1109
|
170 180 190
....*....|....*....|....*....|....*
gi 939342971 188 GAAVLVILHDLNLAARYCDRILLLEQGRCHAFATP 222
Cdd:TIGR01257 1110 GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
19-219 |
1.84e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 68.75 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 19 DIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQ-----ERaRRLAVLPQVSSLGFSFRVE 93
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGiclppEK-RRIGYVFQDARLFPHYKVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 94 evvgmGRMPHGTGQRRDAE---IVEaaLRAADawHLVERSYLALSGGERQRVHLARVLAQlwpgeEGSTLLLDEPTSMLD 170
Cdd:PRK11144 95 -----GNLRYGMAKSMVAQfdkIVA--LLGIE--PLLDRYPGSLSGGEKQRVAIGRALLT-----APELLLMDEPLASLD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 939342971 171 PLHQHTTLEAVRRFA-DCGAAVLVILHDLNLAARYCDRILLLEQGRCHAF 219
Cdd:PRK11144 161 LPRKRELLPYLERLArEINIPILYVSHSLDEILRLADRVVVLEQGKVKAF 210
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
11-214 |
4.40e-13 |
|
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: 65.73 E-value: 4.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 11 RGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCG--ELAPDRGRVTLQGRPLadwaGQERARRLAVLPQVSSLGF 88
Cdd:cd03232 17 GGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPL----DKNFQRSTGYVEQQDVHSP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 89 SFRVeevvgmgrmphgtgqrRDAEIVEAALRaadawhlversylALSGGERQRVHLARVLAQLwPgeegSTLLLDEPTSM 168
Cdd:cd03232 93 NLTV----------------REALRFSALLR-------------GLSVEQRKRLTIGVELAAK-P----SILFLDEPTSG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 939342971 169 LDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAA-RYCDRILLLEQG 214
Cdd:cd03232 139 LDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIfEKFDRLLLLKRG 185
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
17-215 |
5.63e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 67.08 E-value: 5.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 17 LHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLAdwaGQERARRLAVLPQVSSLGFSF------ 90
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLIT---STSKNKDIKQIRKKVGLVFQFpesqlf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 91 --RVEEVVGMGRMPHGTGQRrdaeivEAALRAADAWHLV-------ERSYLALSGGERQRVHLARVLAQlwpgeEGSTLL 161
Cdd:PRK13649 100 eeTVLKDVAFGPQNFGVSQE------EAEALAREKLALVgiseslfEKNPFELSGGQMRRVAIAGILAM-----EPKILV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 939342971 162 LDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGR 215
Cdd:PRK13649 169 LDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGK 222
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
14-247 |
9.31e-13 |
|
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: 66.42 E-value: 9.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 14 NEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGrpladwagqerarRLAVLPQVSSLgfsfrve 93
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWI------- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 94 evvgmgrMPhGT-----------GQRRDAEIVEAALRAADAWHLVERSY-------LALSGGERQRVHLARVLAQlwpge 155
Cdd:cd03291 110 -------MP-GTikeniifgvsyDEYRYKSVVKACQLEEDITKFPEKDNtvlgeggITLSGGQRARISLARAVYK----- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 156 EGSTLLLDEPTSMLDPLHQHTTLEA-VRRFADCGAAVLVILHDLNLaaRYCDRILLLEQGRCHAFAT-PE-AALTPAALK 232
Cdd:cd03291 177 DADLYLLDSPFGYLDVFTEKEIFEScVCKLMANKTRILVTSKMEHL--KKADKILILHEGSSYFYGTfSElQSLRPDFSS 254
|
250
....*....|....*
gi 939342971 233 AVYGIDVLVQAHPER 247
Cdd:cd03291 255 KLMGYDTFDQFSAER 269
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
12-215 |
1.20e-12 |
|
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: 66.03 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 12 GSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDrGRVTLQGRPLADWAGQERARRLAVLPQ-VSSLGFSF 90
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGVIPQkVFIFSGTF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 91 RveevvgMGRMPHgtGQRRDAEIV----EAALRAADA-------WHLVERSYLaLSGGERQRVHLAR-VLAQlwpgeeGS 158
Cdd:cd03289 94 R------KNLDPY--GKWSDEEIWkvaeEVGLKSVIEqfpgqldFVLVDGGCV-LSHGHKQLMCLARsVLSK------AK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 939342971 159 TLLLDEPTSMLDPLhqhtTLEAVRR-----FADCgaAVLVILHDLNlAARYCDRILLLEQGR 215
Cdd:cd03289 159 ILLLDEPSAHLDPI----TYQVIRKtlkqaFADC--TVILSEHRIE-AMLECQRFLVIEENK 213
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
19-223 |
1.22e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 66.29 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 19 DIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPD---RGRVTLQGRPLADWAGQE----RARRLAVLPQ--VSSLGFS 89
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKElnklRAEQISMIFQdpMTSLNPY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 90 FRVEEVVGMGRMPH-GTGQrrdAEIVEAALRAADAWHLVE-RSYLAL-----SGGERQRVHLARVL---AQLwpgeegst 159
Cdd:PRK09473 114 MRVGEQLMEVLMLHkGMSK---AEAFEESVRMLDAVKMPEaRKRMKMyphefSGGMRQRVMIAMALlcrPKL-------- 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 939342971 160 LLLDEPTSMLDPLHQH---TTLEAVRRfaDCGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPE 223
Cdd:PRK09473 183 LIADEPTTALDVTVQAqimTLLNELKR--EFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNAR 247
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
12-220 |
1.24e-12 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 67.12 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 12 GSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTL-QGRPL------------ADWAGQERARRLA 78
Cdd:PRK10636 323 GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGIKLgyfaqhqleflrADESPLQHLARLA 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 79 vlPQVSSL-------GFSFRVEEVvgmgrmphgtgqrrdaeiVEAALRaadawhlversylaLSGGERQRVHLARVLAQl 151
Cdd:PRK10636 403 --PQELEQklrdylgGFGFQGDKV------------------TEETRR--------------FSGGEKARLVLALIVWQ- 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 939342971 152 wpgeEGSTLLLDEPTSMLDPLHQHTTLEAVRRFAdcgAAVLVILHDLNLAARYCDRILLLEQGRCHAFA 220
Cdd:PRK10636 448 ----RPNLLLLDEPTNHLDLDMRQALTEALIDFE---GALVVVSHDRHLLRSTTDDLYLVHDGKVEPFD 509
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
17-222 |
1.25e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 66.18 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 17 LHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLAdwAGQERARRLAVLPQVSSLGFSF------ 90
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIP--ANLKKIKEVKRLRKEIGLVFQFpeyqlf 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 91 --RVEEVVGMGRMPHGTGQRRDAEIVEAALRAAD-AWHLVERSYLALSGGERQRVHLARVLAQlwpgeEGSTLLLDEPTS 167
Cdd:PRK13645 105 qeTIEKDIAFGPVNLGENKQEAYKKVPELLKLVQlPEDYVKRSPFELSGGQKRRVALAGIIAM-----DGNTLVLDEPTG 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 939342971 168 MLDPLHQHTTLEAVRRF-ADCGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATP 222
Cdd:PRK13645 180 GLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSP 235
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
17-215 |
1.75e-12 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 66.58 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 17 LHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAVLPQVSSLgFSFRVEEVV 96
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHL-FNDTIANNI 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 97 GMGRmphgTGQRRDAEIVEAAlRAADAWHLVER-----------SYLALSGGERQRVHLARVLAQLWPgeegsTLLLDEP 165
Cdd:PRK11176 438 AYAR----TEQYSREQIEEAA-RMAYAMDFINKmdngldtvigeNGVLLSGGQRQRIAIARALLRDSP-----ILILDEA 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 939342971 166 TSMLDPLHQ---HTTLEAVRRfadcGAAVLVILHDLNLAARyCDRILLLEQGR 215
Cdd:PRK11176 508 TSALDTESEraiQAALDELQK----NRTSLVIAHRLSTIEK-ADEILVVEDGE 555
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
7-222 |
1.98e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 66.89 E-value: 1.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 7 LYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAVLPQVSSL 86
Cdd:TIGR00957 1292 LRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVL 1371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 87 gFSfrveevvGMGRM---PHgtGQRRDAEIveaalraadaWHLVERSYLA--------------------LSGGERQRVH 143
Cdd:TIGR00957 1372 -FS-------GSLRMnldPF--SQYSDEEV----------WWALELAHLKtfvsalpdkldhecaeggenLSVGQRQLVC 1431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 144 LARVLAQlwpgeEGSTLLLDEPTSMLDpLHQHTTLEAVRR--FADCgaAVLVILHDLNLAARYCdRILLLEQGRCHAFAT 221
Cdd:TIGR00957 1432 LARALLR-----KTKILVLDEATAAVD-LETDNLIQSTIRtqFEDC--TVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGA 1502
|
.
gi 939342971 222 P 222
Cdd:TIGR00957 1503 P 1503
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-221 |
2.75e-12 |
|
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: 66.47 E-value: 2.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 16 VLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGrpladwagqerarRLAVLPQVSSLgfsfrveev 95
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWI--------- 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 96 vgmgrMPhGT-----------GQRRDAEIVEAALRAADAWHLVERSY-------LALSGGERQRVHLARVLAQlwpgeEG 157
Cdd:TIGR01271 499 -----MP-GTikdniifglsyDEYRYTSVIKACQLEEDIALFPEKDKtvlgeggITLSGGQRARISLARAVYK-----DA 567
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 939342971 158 STLLLDEPTSMLDPLHQHTTLEA-VRRFADCGAAVLVI--LHDLNLAarycDRILLLEQGRCHAFAT 221
Cdd:TIGR01271 568 DLYLLDSPFTHLDVVTEKEIFEScLCKLMSNKTRILVTskLEHLKKA----DKILLLHEGVCYFYGT 630
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
15-215 |
3.13e-12 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 65.90 E-value: 3.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 15 EVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERA--RRlavlpqvSSLGFSFRV 92
Cdd:PRK10535 22 EVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAqlRR-------EHFGFIFQR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 93 EEVvgmgrMPHGTGQrRDAEI------VEAALRAADAWHLVERSYLA---------LSGGERQRVHLARVLAQlwpgeEG 157
Cdd:PRK10535 95 YHL-----LSHLTAA-QNVEVpavyagLERKQRLLRAQELLQRLGLEdrveyqpsqLSGGQQQRVSIARALMN-----GG 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 939342971 158 STLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARyCDRILLLEQGR 215
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGE 220
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
9-170 |
3.23e-12 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 65.14 E-value: 3.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 9 LRRGSNEV--LHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQE-RARRLAVlpQV-- 83
Cdd:COG4608 24 FGRTVGVVkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRElRPLRRRM--QMvf 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 84 ----SSLGFSFRVEEVVGMGRMPHG--TGQRRDAEIVEA----ALRAADAwhlvERSYLALSGGERQRVHLARVLAqLWP 153
Cdd:COG4608 102 qdpyASLNPRMTVGDIIAEPLRIHGlaSKAERRERVAELlelvGLRPEHA----DRYPHEFSGGQRQRIGIARALA-LNP 176
|
170
....*....|....*..
gi 939342971 154 geegSTLLLDEPTSMLD 170
Cdd:COG4608 177 ----KLIVCDEPVSALD 189
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1-171 |
5.15e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 63.33 E-value: 5.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADwagQERARRLAVL 80
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR---GDRSRFMAYL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 81 PQVSSLGFSFRVEEVVGMGRMPHGTGQRRDAEIVEAALRAADAWHLVERSylaLSGGERQRVHLARVL---AQLWpgeeg 157
Cdd:PRK13543 88 GHLPGLKADLSTLENLHFLCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQ---LSAGQKKRLALARLWlspAPLW----- 159
|
170
....*....|....
gi 939342971 158 stlLLDEPTSMLDP 171
Cdd:PRK13543 160 ---LLDEPYANLDL 170
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
11-170 |
6.95e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 64.97 E-value: 6.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 11 RGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGrpladwagqerarRLAVLPQVSSLGFSF 90
Cdd:TIGR00957 648 RDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAWIQNDS 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 91 RVEEVVgmgrMPHGTGQRRDAEIVEAA--------LRAADAWHLVERSyLALSGGERQRVHLARVLAQlwpgeEGSTLLL 162
Cdd:TIGR00957 715 LRENIL----FGKALNEKYYQQVLEACallpdleiLPSGDRTEIGEKG-VNLSGGQKQRVSLARAVYS-----NADIYLF 784
|
....*...
gi 939342971 163 DEPTSMLD 170
Cdd:TIGR00957 785 DDPLSAVD 792
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-222 |
8.97e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 63.72 E-value: 8.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYL---RRGSNE--VLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQ---------GRPLA 66
Cdd:PRK13631 21 ILRVKNLYCvfdEKQENElvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyigdkknNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 67 DWAGQERARRLAVLPQVSSLGFSF--------RVEEVVGMGrmPHGTGQRRDaeivEAALRAAdaWHLV---------ER 129
Cdd:PRK13631 101 TNPYSKKIKNFKELRRRVSMVFQFpeyqlfkdTIEKDIMFG--PVALGVKKS----EAKKLAK--FYLNkmglddsylER 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 130 SYLALSGGERQRVHLARVLAQlwpgeEGSTLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRIL 209
Cdd:PRK13631 173 SPFGLSGGQKRRVAIAGILAI-----QPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVI 247
|
250
....*....|...
gi 939342971 210 LLEQGRCHAFATP 222
Cdd:PRK13631 248 VMDKGKILKTGTP 260
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
6-172 |
9.07e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 62.67 E-value: 9.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 6 GLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGEL--APDRGRVTLQGRPLadwagqerARRLAVLPQV 83
Cdd:COG2401 35 GVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQF--------GREASLIDAI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 84 SSLGfsfrveevvgmgrmphgtgqrrDAEIVEAALRAA---DAWhLVERSYLALSGGERQRVHLARVLAqlwpgEEGSTL 160
Cdd:COG2401 107 GRKG----------------------DFKDAVELLNAVglsDAV-LWLRRFKELSTGQKFRFRLALLLA-----ERPKLL 158
|
170
....*....|..
gi 939342971 161 LLDEPTSMLDPL 172
Cdd:COG2401 159 VIDEFCSHLDRQ 170
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
7-215 |
9.38e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 64.30 E-value: 9.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 7 LYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARR-LAVLP---Q 82
Cdd:PRK15439 269 LTVEDLTGEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARgLVYLPedrQ 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 83 VSSL----GFSFRVEEVVgMGRMPHGTGQRRDAEIVEAALRA-----ADAwhlvERSYLALSGGERQRVHLARVLaqlwp 153
Cdd:PRK15439 349 SSGLyldaPLAWNVCALT-HNRRGFWIKPARENAVLERYRRAlnikfNHA----EQAARTLSGGNQQKVLIAKCL----- 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 939342971 154 geEGSTLLL--DEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGR 215
Cdd:PRK15439 419 --EASPQLLivDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGE 480
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
11-215 |
9.64e-12 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 64.35 E-value: 9.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 11 RGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAVLPQVSS-LGFS 89
Cdd:PRK10790 351 RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVvLADT 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 90 FRVEevVGMGRmphgtgqrrdaEIVEAALraadaWHLVERSYLA--------------------LSGGERQRVHLARVLA 149
Cdd:PRK10790 431 FLAN--VTLGR-----------DISEEQV-----WQALETVQLAelarslpdglytplgeqgnnLSVGQKQLLALARVLV 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 939342971 150 QLwPgeegSTLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVlVILHDLNLAARyCDRILLLEQGR 215
Cdd:PRK10790 493 QT-P----QILILDEATANIDSGTEQAIQQALAAVREHTTLV-VIAHRLSTIVE-ADTILVLHRGQ 551
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
17-209 |
1.06e-11 |
|
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: 61.57 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 17 LHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLcgeLAPDRGRVTLQGRPLADwagqerARRLAVLPQVSSLgfsfrVEevV 96
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG---LYASGKARLISFLPKFS------RNKLIFIDQLQFL-----ID--V 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 97 GMGRMPhgtgqrrdaeiveaalraadawhlVERSYLALSGGERQRVHLARVLAQlwpGEEGSTLLLDEPTSMLDPLHQHT 176
Cdd:cd03238 75 GLGYLT------------------------LGQKLSTLSGGELQRVKLASELFS---EPPGTLFILDEPSTGLHQQDINQ 127
|
170 180 190
....*....|....*....|....*....|...
gi 939342971 177 TLEAVRRFADCGAAVLVILHDLNLaARYCDRIL 209
Cdd:cd03238 128 LLEVIKGLIDLGNTVILIEHNLDV-LSSADWII 159
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
18-233 |
1.30e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 62.79 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 18 HDIHLQLPPGQVVGVLGPNGAGKS----SLLSVLCGELAPDRGRVTLQGRPLAdwAGQERARRLAVLPQVSSLGFSfrve 93
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVA--PCALRGRKIATIMQNPRSAFN---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 94 EVVGMGRMPHGTGQRRDAEIVEAALRAA-------DAWHLVERSYLALSGGERQRVHLArvLAQLwpgEEGSTLLLDEPT 166
Cdd:PRK10418 94 PLHTMHTHARETCLALGKPADDATLTAAleavgleNAARVLKLYPFEMSGGMLQRMMIA--LALL---CEAPFIIADEPT 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 939342971 167 SMLDPLHQHTTLEAVRRF-ADCGAAVLVILHDLNLAARYCDRILLLEQGRC-------HAFATPEAALTPAALKA 233
Cdd:PRK10418 169 TDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGRIveqgdveTLFNAPKHAVTRSLVSA 243
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
17-214 |
1.31e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 64.04 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 17 LHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARR-LAVLPQVSSLGFSFRVEEV 95
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGIIYQELSVIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 96 VGMGRMPhgTGQRRDAEIVEAALRAADAWHLVERSYLA---------LSGGERQRVHLARVLAQlwpgeEGSTLLLDEPT 166
Cdd:PRK09700 101 LYIGRHL--TKKVCGVNIIDWREMRVRAAMMLLRVGLKvdldekvanLSISHKQMLEIAKTLML-----DAKVIIMDEPT 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 939342971 167 SMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQG 214
Cdd:PRK09700 174 SSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
15-224 |
1.87e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 62.49 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 15 EVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERAR----RLAVLPQV-SSLGFS 89
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRpvrkRIGMVFQFpESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 90 FRVEEVVGMGrmPHGTGQrrdaEIVEAALRAAD-------AWHLVERSYLALSGGERQRVHLARVLAQlwpgeEGSTLLL 162
Cdd:PRK13646 101 DTVEREIIFG--PKNFKM----NLDEVKNYAHRllmdlgfSRDVMSQSPFQMSGGQMRKIAIVSILAM-----NPDIIVL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 939342971 163 DEPTSMLDPLHQHTTLEAVRRFA-DCGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPEA 224
Cdd:PRK13646 170 DEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKE 232
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
4-214 |
2.01e-11 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 61.58 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 4 VEGLYLRRGSN-EVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRV----TLQGRPLADWAGQERARRLA 78
Cdd:cd03290 3 VTNGYFSWGSGlATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRYSVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 79 VLPQVSSLgFSFRVEEVVGMGRmPHGTgQRRDAEIVEAALRA-------ADAWHLVERSyLALSGGERQRVHLARVLAQl 151
Cdd:cd03290 83 YAAQKPWL-LNATVEENITFGS-PFNK-QRYKAVTDACSLQPdidllpfGDQTEIGERG-INLSGGQRQRICVARALYQ- 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 939342971 152 wpgeEGSTLLLDEPTSMLD-PLHQHTTLEAVRRF-ADCGAAVLVILHDLNLAArYCDRILLLEQG 214
Cdd:cd03290 158 ----NTNIVFLDDPFSALDiHLSDHLMQEGILKFlQDDKRTLVLVTHKLQYLP-HADWIIAMKDG 217
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
27-212 |
2.05e-11 |
|
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: 61.05 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 27 GQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRpladwagqerarRLAVLPQvsslgfsfrveevvgmgrmphgtg 106
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGI------------TPVYKPQ------------------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 107 qrrdaeiveaalraadawhlversYLALSGGERQRVHLARVLaqlwpGEEGSTLLLDEPTSMLDPLHQHTTLEAVRRFAD 186
Cdd:cd03222 69 ------------------------YIDLSGGELQRVAIAAAL-----LRNATFYLFDEPSAYLDIEQRLNAARAIRRLSE 119
|
170 180
....*....|....*....|....*..
gi 939342971 187 CGA-AVLVILHDLNLAARYCDRILLLE 212
Cdd:cd03222 120 EGKkTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
27-233 |
2.30e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.01 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 27 GQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAVL-P---------QVSSlgfsfrVEEVV 96
Cdd:PRK11288 279 GEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMLcPedrkaegiiPVHS------VADNI 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 97 GMGRMPHgtgQRRDAEIVEAALRAADAWHLVER----------SYLALSGGERQRVHLARvlaqlWPGEEGSTLLLDEPT 166
Cdd:PRK11288 353 NISARRH---HLRAGCLINNRWEAENADRFIRSlniktpsreqLIMNLSGGNQQKAILGR-----WLSEDMKVILLDEPT 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 939342971 167 SMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGRC-----HAFATPEAALTPAALKA 233
Cdd:PRK11288 425 RGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIagelaREQATERQALSLALPRT 496
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-172 |
3.00e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 61.70 E-value: 3.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQ---ERARRL 77
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSrlyTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 78 AVLPQVSSLGFSFRVEEVVGM-----GRMPHGTGQRRDAEIVEA-ALRAADAWHLVErsylaLSGGERQRVHLARVLAQl 151
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVAYplrehTQLPAPLLHSTVMMKLEAvGLRGAAKLMPSE-----LSGGMARRAALARAIAL- 160
|
170 180
....*....|....*....|.
gi 939342971 152 wpgeEGSTLLLDEPTSMLDPL 172
Cdd:PRK11831 161 ----EPDLIMFDEPFVGQDPI 177
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
26-216 |
4.63e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 62.59 E-value: 4.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 26 PGQVVGVLGPNGAGKSSLLSVLCGELAPD--RGRVTLQGRPLAdwagQERARRLAVLPQVSSLGFSFRVEEV---VGMGR 100
Cdd:PLN03211 93 PGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPT----KQILKRTGFVTQDDILYPHLTVRETlvfCSLLR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 101 MPHGTGQR---RDAEIVEAALRAADAWH-LVERSYL-ALSGGERQRVHLARVLAqLWPgeegSTLLLDEPTSMLDPLHQH 175
Cdd:PLN03211 169 LPKSLTKQekiLVAESVISELGLTKCENtIIGNSFIrGISGGERKRVSIAHEML-INP----SLLILDEPTSGLDATAAY 243
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 939342971 176 TTLEAVRRFADCGAAVLVILHD-LNLAARYCDRILLLEQGRC 216
Cdd:PLN03211 244 RLVLTLGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGRC 285
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
14-233 |
5.96e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 62.03 E-value: 5.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 14 NEVLHDIHLQLPPGQVVGVLGPNGAGKS-SLLSVLcgELAPDRGRVTLQGRPLadWAGQE------------RARRLAVL 80
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSvTALSIL--RLLPSPPVVYPSGDIR--FHGESllhaseqtlrgvRGNKIAMI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 81 PQ--VSSLGFSFRVE----EVVGMGRmphgtGQRRDA---EIV---------EAALRAADAWHlversylALSGGERQRV 142
Cdd:PRK15134 98 FQepMVSLNPLHTLEkqlyEVLSLHR-----GMRREAargEILncldrvgirQAAKRLTDYPH-------QLSGGERQRV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 143 HLARVLAQlwpgeEGSTLLLDEPTSMLDPLHQHTTLEAVRRF-ADCGAAVLVILHDLNLAARYCDRILLLEQGRC----- 216
Cdd:PRK15134 166 MIAMALLT-----RPELLIADEPTTALDVSVQAQILQLLRELqQELNMGLLFITHNLSIVRKLADRVAVMQNGRCveqnr 240
|
250
....*....|....*....
gi 939342971 217 --HAFATPEAALTPAALKA 233
Cdd:PRK15134 241 aaTLFSAPTHPYTQKLLNS 259
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
17-214 |
8.59e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 61.68 E-value: 8.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 17 LHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAP-DRGRVTLQGrpladwagqerarRLAVLPQVSSLgFSFRVEEV 95
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPrSDASVVIRG-------------TVAYVPQVSWI-FNATVRDN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 96 VGMG---------RMPHGTGQRRDAEIveaaLRAADAWHLVERSyLALSGGERQRVHLARVLAQlwpgeEGSTLLLDEPT 166
Cdd:PLN03130 699 ILFGspfdperyeRAIDVTALQHDLDL----LPGGDLTEIGERG-VNISGGQKQRVSMARAVYS-----NSDVYIFDDPL 768
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 939342971 167 SMLDplhQHTtleAVRRFADC-------GAAVLVI--LHDLNlaarYCDRILLLEQG 214
Cdd:PLN03130 769 SALD---AHV---GRQVFDKCikdelrgKTRVLVTnqLHFLS----QVDRIILVHEG 815
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
22-204 |
1.30e-10 |
|
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: 58.53 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 22 LQLPPGQVVGVLGPNGAGKSSLLSVLCGELApdrGRVTLQGRPLADWAGQERARrlavlpqvSSLGFSFRVeevvgmgrm 101
Cdd:cd03227 16 VTFGEGSLTIITGPNGSGKSTILDAIGLALG---GAQSATRRRSGVKAGCIVAA--------VSAELIFTR--------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 102 phgtgqrrdaeiveaalraadawhlversyLALSGGERQRVHLARVLAqLWPGEEGSTLLLDEPTSMLDPLHQHTTLEAV 181
Cdd:cd03227 76 ------------------------------LQLSGGEKELSALALILA-LASLKPRPLYILDEIDRGLDPRDGQALAEAI 124
|
170 180
....*....|....*....|...
gi 939342971 182 RRFADCGAAVLVILHDLNLAARY 204
Cdd:cd03227 125 LEHLVKGAQVIVITHLPELAELA 147
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
16-215 |
1.37e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 59.41 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 16 VLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAvlpqvSSLGFSFR---- 91
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRA-----KHVGFVFQsfml 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 92 -----VEEVVGMGRMPHGTGQRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQlwpgeEGSTLLLDEPT 166
Cdd:PRK10584 100 iptlnALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNG-----RPDVLFADEPT 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 939342971 167 SMLDplhQHT------TLEAVRRfaDCGAAVLVILHDLNLAARyCDRILLLEQGR 215
Cdd:PRK10584 175 GNLD---RQTgdkiadLLFSLNR--EHGTTLILVTHDLQLAAR-CDRRLRLVNGQ 223
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
4-196 |
1.65e-10 |
|
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: 58.32 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 4 VEGLYLRRGSNEVL-HDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGeLAP-DRGRVtlqGRPladwagqeRARRLAVLP 81
Cdd:cd03223 3 LENLSLATPDGRVLlKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG-LWPwGSGRI---GMP--------EGEDLLFLP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 82 QVSslgfsfrveevvgmgRMPHGTgqrrdaeiveaaLRAADA--WHLVersylaLSGGERQRVHLARVLAQlwpgeEGST 159
Cdd:cd03223 71 QRP---------------YLPLGT------------LREQLIypWDDV------LSGGEQQRLAFARLLLH-----KPKF 112
|
170 180 190
....*....|....*....|....*....|....*..
gi 939342971 160 LLLDEPTSMLDPLHQHTTLEAVRRFadcGAAVLVILH 196
Cdd:cd03223 113 VFLDEATSALDEESEDRLYQLLKEL---GITVISVGH 146
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
13-214 |
2.47e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 60.37 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 13 SNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAP-DRGRVTLQGrpladwagqerarRLAVLPQVSSLgFSFR 91
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaETSSVVIRG-------------SVAYVPQVSWI-FNAT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 92 VEEVVGMGR--MPHGTGQRRDAEIVEAALR---AADAWHLVERSyLALSGGERQRVHLARVLAQlwpgeEGSTLLLDEPT 166
Cdd:PLN03232 695 VRENILFGSdfESERYWRAIDVTALQHDLDllpGRDLTEIGERG-VNISGGQKQRVSMARAVYS-----NSDIYIFDDPL 768
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 939342971 167 SMLDPLHQHTTLEAVRRFADCGAA-VLVI--LHDLNLAarycDRILLLEQG 214
Cdd:PLN03232 769 SALDAHVAHQVFDSCMKDELKGKTrVLVTnqLHFLPLM----DRIILVSEG 815
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
12-215 |
3.98e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 59.27 E-value: 3.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 12 GSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERA-----RRLAVLPQVSsl 86
Cdd:PRK11000 14 GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGvgmvfQSYALYPHLS-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 87 gfsfrVEEVVGMGRMPHGTGQRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQlwpgeEGSTLLLDEPT 166
Cdd:PRK11000 92 -----VAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVA-----EPSVFLLDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 939342971 167 SMLDP-LHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGR 215
Cdd:PRK11000 162 SNLDAaLRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGR 211
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-170 |
6.86e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 58.75 E-value: 6.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTlqgrpladWAgqERArRLAVLP 81
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK--------WS--ENA-NIGYYA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 82 QVSSLGFSfrvEEVVGMGRMPHGTGQRRDAEIVEAAL-R---AADAwhlVERSYLALSGGERQRVHLARVLAQlwpgeEG 157
Cdd:PRK15064 389 QDHAYDFE---NDLTLFDWMSQWRQEGDDEQAVRGTLgRllfSQDD---IKKSVKVLSGGEKGRMLFGKLMMQ-----KP 457
|
170
....*....|...
gi 939342971 158 STLLLDEPTSMLD 170
Cdd:PRK15064 458 NVLVMDEPTNHMD 470
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-215 |
1.02e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 57.82 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAG--KSSLLSVLCGelaPDRGRvtlqgRP--LADWAGQERARRL 77
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGR-----RPwrF*TWCANRRALRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 78 AV-----LPQVSSLGFSFRvEEVVGMGRMPHGTgqRRDAE-----------IVEAALRAADAWhlversylalSGGERQR 141
Cdd:NF000106 86 TIg*hrpVR*GRRESFSGR-ENLYMIGR*LDLS--RKDARaradellerfsLTEAAGRAAAKY----------SGGMRRR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 939342971 142 VHLARVLAQlwpgeEGSTLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGR 215
Cdd:NF000106 153 LDLAASMIG-----RPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGR 221
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
4-214 |
1.30e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 57.98 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 4 VEGLYLRRGSNE---VLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRpladwagqerarrlAVL 80
Cdd:PRK13545 24 LKDLFFRSKDGEyhyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS--------------AAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 81 PQVSSlGFSFR---VEEVVGMGRMpHGTGQRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLArVLAQLWPgeeg 157
Cdd:PRK13545 90 IAISS-GLNGQltgIENIELKGLM-MGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFA-ISVHINP---- 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 939342971 158 STLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQG 214
Cdd:PRK13545 163 DILVIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYG 219
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-74 |
2.60e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 55.95 E-value: 2.60e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 939342971 1 MLHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCG--ELAPDRGRVTLQGRPLADWAGQERA 74
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGKDLLELSPEDRA 76
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-76 |
3.03e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 55.80 E-value: 3.03e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 939342971 1 MLHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPD--RGRVTLQGRPLADWAGQERARR 76
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGESILDLEPEERAHL 84
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
26-214 |
5.89e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.78 E-value: 5.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 26 PGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLA-------DWAG-----QErarrLAVLPQVSslgfsfrVE 93
Cdd:PRK10762 29 PGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpkssQEAGigiihQE----LNLIPQLT-------IA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 94 EVVGMGRMPHGTGQRRD-AEIVEAA---LRAADAWHLVERSYLALSGGERQRVHLARVLAQlwpgeEGSTLLLDEPTSML 169
Cdd:PRK10762 98 ENIFLGREFVNRFGRIDwKKMYAEAdklLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSF-----ESKVIIMDEPTDAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 939342971 170 DPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQG 214
Cdd:PRK10762 173 TDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
15-216 |
2.04e-08 |
|
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: 53.04 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 15 EVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPD---RGRVTLQGRPLADWAgqERARRLAVlpqvsslgfsFR 91
Cdd:cd03233 21 PILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFA--EKYPGEII----------YV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 92 VEEVVgmgRMPHGTGQrrdaEIVEAALRA-ADAwhlversYL-ALSGGERQRVHLARVLAQlwpgeEGSTLLLDEPTSML 169
Cdd:cd03233 89 SEEDV---HFPTLTVR----ETLDFALRCkGNE-------FVrGISGGERKRVSIAEALVS-----RASVLCWDNSTRGL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 939342971 170 DPLHQHTTLEAVRRFADC-GAAVLVILHDLNLAARYC-DRILLLEQGRC 216
Cdd:cd03233 150 DSSTALEILKCIRTMADVlKTTTFVSLYQASDEIYDLfDKVLVLYEGRQ 198
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-200 |
2.48e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 52.64 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPL-ADWAGQEraRRLAV 79
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIkKDLCTYQ--KQLCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 80 LPQVSSLGFSFRVEEVVgMGRMPHGTGQRRDAEIVeaalRAADAWHLVERSYLALSGGERQRVHLARVL---AQLWpgee 156
Cdd:PRK13540 79 VGHRSGINPYLTLRENC-LYDIHFSPGAVGITELC----RLFSLEHLIDYPCGLLSSGQKRQVALLRLWmskAKLW---- 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 939342971 157 gstlLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILH-DLNL 200
Cdd:PRK13540 150 ----LLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHqDLPL 190
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
19-214 |
2.63e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.19 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 19 DIHLQlpPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVT---------LQGRPLADWAG----------QERARRLAV 79
Cdd:PRK11147 23 ELHIE--DNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIyeqdlivarLQQDPPRNVEGtvydfvaegiEEQAEYLKR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 80 LPQVSSLgfsfrveevvgMGRMPHGTGQRRDAEiVEAALRAADAWHLVER--------------SYLALSGGERQRVHLA 145
Cdd:PRK11147 101 YHDISHL-----------VETDPSEKNLNELAK-LQEQLDHHNLWQLENRinevlaqlgldpdaALSSLSGGWLRKAALG 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 146 RVLAQlwpgeEGSTLLLDEPTSMLDPlhqhTTLEAVRRF-ADCGAAVLVILHDLNLAARYCDRILLLEQG 214
Cdd:PRK11147 169 RALVS-----NPDVLLLDEPTNHLDI----ETIEWLEGFlKTFQGSIIFISHDRSFIRNMATRIVDLDRG 229
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
134-209 |
2.91e-08 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 53.00 E-value: 2.91e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 939342971 134 LSGGERQRVHLARVLAQlwpGEEGSTL-LLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLaARYCDRIL 209
Cdd:cd03271 170 LSGGEAQRIKLAKELSK---RSTGKTLyILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDV-IKCADWII 242
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
128-209 |
4.87e-08 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 53.68 E-value: 4.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 128 ERSYLALSGGERQRVHLARVL-AQLwpgeEGSTLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAArYCD 206
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHLgAEL----IGITYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMIS-LAD 545
|
...
gi 939342971 207 RIL 209
Cdd:PRK00635 546 RII 548
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-239 |
8.08e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 52.70 E-value: 8.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 2 LHVEGLylrrgSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQE--------- 72
Cdd:PRK10762 258 LKVDNL-----SGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglangivyi 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 73 ---RARRLAVlpqvssLGFSfrVEE---VVGMGRMPHGTGQRRDAEIVEAALRAADAWHL----VERSYLALSGGERQRV 142
Cdd:PRK10762 333 sedRKRDGLV------LGMS--VKEnmsLTALRYFSRAGGSLKHADEQQAVSDFIRLFNIktpsMEQAIGLLSGGNQQKV 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 143 HLARVLAQLwPgeegSTLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGR-CHAFAT 221
Cdd:PRK10762 405 AIARGLMTR-P----KVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRiSGEFTR 479
|
250 260
....*....|....*....|.
gi 939342971 222 PEA---ALTPAALKAVYGIDV 239
Cdd:PRK10762 480 EQAtqeKLMAAAVGKLNRVNQ 500
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-234 |
8.29e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 52.55 E-value: 8.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLR----RGSNEVLHDIHLQLPPGQVVGVLGPNGAGKS-------SLLSVLCGELAPDRGRVTLQGRPLADWA 69
Cdd:PRK10261 12 VLAVENLNIAfmqeQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalalmRLLEQAGGLVQCDKMLLRRRSRQVIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 70 GQE-------RARRLAVLPQ--VSSLGFSFRV-EEVVGMGRMPHGTGqrRDAEIVEAA-----LRAADAWHLVERSYLAL 134
Cdd:PRK10261 92 EQSaaqmrhvRGADMAMIFQepMTSLNPVFTVgEQIAESIRLHQGAS--REEAMVEAKrmldqVRIPEAQTILSRYPHQL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 135 SGGERQRVHLARVLAQlwpgeEGSTLLLDEPTSMLDPLHQHTTLEAVRRF-ADCGAAVLVILHDLNLAARYCDRILLLEQ 213
Cdd:PRK10261 170 SGGMRQRVMIAMALSC-----RPAVLIADEPTTALDVTIQAQILQLIKVLqKEMSMGVIFITHDMGVVAEIADRVLVMYQ 244
|
250 260
....*....|....*....|....*...
gi 939342971 214 GRC-------HAFATPEAALTPAALKAV 234
Cdd:PRK10261 245 GEAvetgsveQIFHAPQHPYTRALLAAV 272
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
134-198 |
1.39e-07 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 51.95 E-value: 1.39e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 939342971 134 LSGGERQRVHLARVLAQlwpGEEGSTL-LLDEPTSmldPLHQH---TTLEAVRRFADCGAAVLVILHDL 198
Cdd:COG0178 827 LSGGEAQRVKLASELSK---RSTGKTLyILDEPTT---GLHFHdirKLLEVLHRLVDKGNTVVVIEHNL 889
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-227 |
1.95e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 51.32 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 19 DIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLA------------DWAGQER-----------AR 75
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprspldavkkgmAYITESRrdngffpnfsiAQ 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 76 RLAVLPQVSSLGFSfrveevvGMGRMPHGTGQRRDAEIVEAALraADAWHLVERSYLALSGGERQRVHLARvlaqlWPGE 155
Cdd:PRK09700 361 NMAISRSLKDGGYK-------GAMGLFHEVDEQRTAENQRELL--ALKCHSVNQNITELSGGNQQKVLISK-----WLCC 426
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 939342971 156 EGSTLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPEAALT 227
Cdd:PRK09700 427 CPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMS 498
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
26-214 |
2.15e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.65 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 26 PGQVVGVLGPNGAGKSSLLSVLCGELapDRGRVT-----LQGRPLadwagQER-ARRLAV-------LPQVS---SLGFS 89
Cdd:TIGR00956 788 PGTLTALMGASGAGKTTLLNVLAERV--TTGVITggdrlVNGRPL-----DSSfQRSIGYvqqqdlhLPTSTvreSLRFS 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 90 FRVeevvgmgRMPHGTGQRRDAEIVEAALRA------ADAwhLVERSYLALSGGERQRVHLARVLAqlwpGEEGSTLLLD 163
Cdd:TIGR00956 861 AYL-------RQPKSVSKSEKMEYVEEVIKLlemesyADA--VVGVPGEGLNVEQRKRLTIGVELV----AKPKLLLFLD 927
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 939342971 164 EPTSMLDPLHQHTTLEAVRRFADCGAAVLVILH--DLNLAARYcDRILLLEQG 214
Cdd:TIGR00956 928 EPTSGLDSQTAWSICKLMRKLADHGQAILCTIHqpSAILFEEF-DRLLLLQKG 979
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
127-197 |
2.70e-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: 49.95 E-value: 2.70e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 939342971 127 VERSYLALSGGERQRVHLARvlaQLWPGEEGSTLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHD 197
Cdd:cd03270 131 LSRSAPTLSGGEAQRIRLAT---QIGSGLTGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHD 198
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
30-219 |
2.75e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.01 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 30 VGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPladwagqerarRLAVLPQVSSLGFSFRVEEVVGMGRMPHGtgqrr 109
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKV-----------RMAVFSQHHVDGLDLSSNPLLYMMRCFPG----- 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 110 daeIVEAALRA-----ADAWHLVERSYLALSGGERQRVHLARVLAQlwpgeEGSTLLLDEPTSMLDplhqhttLEAV--- 181
Cdd:PLN03073 602 ---VPEQKLRAhlgsfGVTGNLALQPMYTLSGGQKSRVAFAKITFK-----KPHILLLDEPSNHLD-------LDAVeal 666
|
170 180 190
....*....|....*....|....*....|....*....
gi 939342971 182 -RRFADCGAAVLVILHDLNLAARYCDRILLLEQGRCHAF 219
Cdd:PLN03073 667 iQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPF 705
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
13-196 |
3.78e-07 |
|
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: 50.52 E-value: 3.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 13 SNEVL-HDIHLQLPPGQVVGVLGPNGAGKSSLLSVLcGELAPDRGRVTLQGRPladwagqeraRRLAVLPQ--VSSLGfS 89
Cdd:TIGR00954 463 NGDVLiESLSFEVPSGNNLLICGPNGCGKSSLFRIL-GELWPVYGGRLTKPAK----------GKLFYVPQrpYMTLG-T 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 90 FRVEEVVGMGRMPHGTGQRRDAEIvEAALRAADAWHLVER--SYLA-------LSGGERQRVHLARVLAQlwpgeEGSTL 160
Cdd:TIGR00954 531 LRDQIIYPDSSEDMKRRGLSDKDL-EQILDNVQLTHILERegGWSAvqdwmdvLSGGEKQRIAMARLFYH-----KPQFA 604
|
170 180 190
....*....|....*....|....*....|....*.
gi 939342971 161 LLDEPTSMLDPLHQHTTLEAVRRFadcGAAVLVILH 196
Cdd:TIGR00954 605 ILDECTSAVSVDVEGYMYRLCREF---GITLFSVSH 637
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
27-197 |
4.95e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.33 E-value: 4.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 27 GQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERArrlAVLPQVSslgfsfrVEEVVGMGR---MPH 103
Cdd:PRK11147 345 GDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRA---ELDPEKT-------VMDNLAEGKqevMVN 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 104 GtgqrRDAEIVeaalraadawhlverSYL---------------ALSGGERQRVHLARVLaqLWPgeegSTLL-LDEPTS 167
Cdd:PRK11147 415 G----RPRHVL---------------GYLqdflfhpkramtpvkALSGGERNRLLLARLF--LKP----SNLLiLDEPTN 469
|
170 180 190
....*....|....*....|....*....|.
gi 939342971 168 MLDPlhqhTTLEAVRRF-ADCGAAVLVILHD 197
Cdd:PRK11147 470 DLDV----ETLELLEELlDSYQGTVLLVSHD 496
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
7-211 |
7.90e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.83 E-value: 7.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 7 LYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLS---VLCGE----------LAPDRGRVT--------LQGR-- 63
Cdd:PRK00635 601 LTLSKATKHNLKDLTISLPLGRLTVVTGVSGSGKSSLINdtlVPAVEefieqgfcsnLSIQWGAISrlvhitrdLPGRsq 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 64 ---PLADWAGQERARRL-AVLPQVSSLG-----FSFRVE-----EVVGMGRM-----------PHGTGQRRDAEIVE--- 115
Cdd:PRK00635 681 rsiPLTYIKAFDDLRELfAEQPRSKRLGltkshFSFNTPlgacaECQGLGSItttdnrtsipcPSCLGKRFLPQVLEvry 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 116 -----AALRAADAW----------HLVER---------SYL-------ALSGGERQRVHLARVLaqLWPGEEGSTLLLDE 164
Cdd:PRK00635 761 kgkniADILEMTAYeaekffldepSIHEKihalcslglDYLplgrplsSLSGGEIQRLKLAYEL--LAPSKKPTLYVLDE 838
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 939342971 165 PTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLaARYCDRILLL 211
Cdd:PRK00635 839 PTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHV-VKVADYVLEL 884
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
12-170 |
9.67e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 49.07 E-value: 9.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 12 GSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLL-------SVLCGELAPDRGRVTlqgrpladwaGQERARR-------- 76
Cdd:PRK11650 15 GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLrmvagleRITSGEIWIGGRVVN----------ELEPADRdiamvfqn 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 77 LAVLPQVSslgfsfrVEEVVGMG----RMPHGTGQRRdaeiVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQlw 152
Cdd:PRK11650 85 YALYPHMS-------VRENMAYGlkirGMPKAEIEER----VAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVR-- 151
|
170
....*....|....*...
gi 939342971 153 pgeEGSTLLLDEPTSMLD 170
Cdd:PRK11650 152 ---EPAVFLFDEPLSNLD 166
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
15-215 |
2.29e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.62 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 15 EVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRV------------------TLQGRPLadWAGQERARR 76
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVwaersiayvpqqawimnaTVRGNIL--FFDEEDAAR 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 77 LAVLPQVSSLGfsfrveevVGMGRMPHGTgqrrDAEIVEAALRaadawhlversylaLSGGERQRVHLAR-VLAqlwpge 155
Cdd:PTZ00243 752 LADAVRVSQLE--------ADLAQLGGGL----ETEIGEKGVN--------------LSGGQKARVSLARaVYA------ 799
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 156 EGSTLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARyCDRILLLEQGR 215
Cdd:PTZ00243 800 NRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPR-ADYVVALGDGR 858
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
129-198 |
2.37e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 48.47 E-value: 2.37e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 939342971 129 RSYLALSGGERQRVHLARVLAQlwpGEEGSTL-LLDEPTSmldPLHQHTT---LEAVRRFADCGAAVLVILHDL 198
Cdd:TIGR00630 825 QPATTLSGGEAQRIKLAKELSK---RSTGRTLyILDEPTT---GLHFDDIkklLEVLQRLVDKGNTVVVIEHNL 892
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
128-197 |
2.57e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 48.09 E-value: 2.57e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 128 ERSYLALSGGERQRVHLArvlAQLWPGEEGSTLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHD 197
Cdd:TIGR00630 483 SRAAGTLSGGEAQRIRLA---TQIGSGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHD 549
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
31-208 |
4.63e-06 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 46.11 E-value: 4.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 31 GVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAVLPQVSslGFSFRVEEVVGMgrmphgtgqrrD 110
Cdd:cd03279 32 LICGPTGAGKSTILDAITYALYGKTPRYGRQENLRSVFAPGEDTAEVSFTFQLG--GKKYRVERSRGL-----------D 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 111 AE--IVEAALRAADAWHLVERSYLALSGGERQRVHLARVLA-----QLWPGEEGSTLLLDEPTSMLDPLHQHTTLEAVRR 183
Cdd:cd03279 99 YDqfTRIVLLPQGEFDRFLARPVSTLSGGETFLASLSLALAlsevlQNRGGARLEALFIDEGFGTLDPEALEAVATALEL 178
|
170 180
....*....|....*....|....*
gi 939342971 184 FADCGAAVLVILHDLNLAARYCDRI 208
Cdd:cd03279 179 IRTENRMVGVISHVEELKERIPQRL 203
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-234 |
4.74e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 47.01 E-value: 4.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 19 DIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADW-AGQERARR--LAVLPQ--VSSLGFSFRVE 93
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMkDDEWRAVRsdIQMIFQdpLASLNPRMTIG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 94 EVVG---MGRMPHGTGQRRDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQlwpgeEGSTLLLDEPTSMLD 170
Cdd:PRK15079 119 EIIAeplRTYHPKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALIL-----EPKLIICDEPVSALD 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 939342971 171 PLHQHTT---LEAVRRfaDCGAAVLVILHDLNLAARYCDRILLL------EQGRCHA-FATPEAALTPAALKAV 234
Cdd:PRK15079 194 VSIQAQVvnlLQQLQR--EMGLSLIFIAHDLAVVKHISDRVLVMylghavELGTYDEvYHNPLHPYTKALMSAV 265
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
1-214 |
6.53e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.08 E-value: 6.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLrrgsneVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSV------LCGelapdrGRVTLQGRPLADWAGQERA 74
Cdd:PTZ00243 1316 MRYREGLPL------VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTfmrmveVCG------GEIRVNGREIGAYGLRELR 1383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 75 RRLAVLPQVSSLgFSFRVE------------------EVVGMGRMPHGTGQRRDAEIVEAALraadawhlverSYlalSG 136
Cdd:PTZ00243 1384 RQFSMIPQDPVL-FDGTVRqnvdpfleassaevwaalELVGLRERVASESEGIDSRVLEGGS-----------NY---SV 1448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 939342971 137 GERQRVHLARVLAQlwpgeEGST-LLLDEPTSMLDPLHQHtTLEAVRRFADCGAAVLVILHDLNLAARYcDRILLLEQG 214
Cdd:PTZ00243 1449 GQRQLMCMARALLK-----KGSGfILMDEATANIDPALDR-QIQATVMSAFSAYTVITIAHRLHTVAQY-DKIIVMDHG 1520
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
20-251 |
9.28e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 45.95 E-value: 9.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 20 IHLQLPPGQVVGVLGPNGAGKSSLLSVLCGeLAPDRGRVTLQGRPLAD---WAGQERARRLAV---------LPQvSSLG 87
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICG-VTKDNWRVTADRMRFDDidlLRLSPRERRKLVghnvsmifqEPQ-SCLD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 88 FSFRVEEVVgMGRMPHGTGQRRDAEIVEAAL-RAADAWHLV--------ERSY-LALSGGERQRVHLARVLAQlwpgeEG 157
Cdd:PRK15093 104 PSERVGRQL-MQNIPGWTYKGRWWQRFGWRKrRAIELLHRVgikdhkdaMRSFpYELTEGECQKVMIAIALAN-----QP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 158 STLLLDEPTSMLDPLHQHTTLEAVRRF-ADCGAAVLVILHDLNLAARYCDRILLLEQGRCHAFATPEAALTpaALKAVYg 236
Cdd:PRK15093 178 RLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVT--TPHHPY- 254
|
250
....*....|....*
gi 939342971 237 IDVLVQAHPERGHPL 251
Cdd:PRK15093 255 TQALIRAIPDFGSAM 269
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-218 |
1.08e-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: 45.97 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 19 DIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELaPDR--GRVTLQGRPLADWAGQERARR-LAVLPQ-------VSSLGF 88
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAY-PGKfeGNVFINGKPVDIRNPAQAIRAgIAMVPEdrkrhgiVPILGV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 89 SFRV-----EEVVGMGRMPHGTGQRR-DAEIVEAALRAADAWHLVERsylaLSGGERQRVHLARVLAqLWPgeegSTLLL 162
Cdd:TIGR02633 357 GKNItlsvlKSFCFKMRIDAAAELQIiGSAIQRLKVKTASPFLPIGR----LSGGNQQKAVLAKMLL-TNP----RVLIL 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 939342971 163 DEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGRCHA 218
Cdd:TIGR02633 428 DEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKG 483
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-215 |
1.09e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 46.26 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 16 VLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGEL----APDRGRVTLQGRPLADWAGQERARRLAV------LPQVS- 84
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTdgfhIGVEGVITYDGITPEEIKKHYRGDVVYNaetdvhFPHLTv 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 85 --SLGFSFRVEevvgmgrmphgTGQRRdAEIVEAALRAADAWHLVERSY---------------LALSGGERQRVHLARV 147
Cdd:TIGR00956 156 geTLDFAARCK-----------TPQNR-PDGVSREEYAKHIADVYMATYglshtrntkvgndfvRGVSGGERKRVSIAEA 223
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 939342971 148 LAQlwpgeEGSTLLLDEPTSMLDplhQHTTLEavrrFADCGAAVLVILHDLNLAARY-C--------DRILLLEQGR 215
Cdd:TIGR00956 224 SLG-----GAKIQCWDNATRGLD---SATALE----FIRALKTSANILDTTPLVAIYqCsqdayelfDKVIVLYEGY 288
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
20-215 |
1.31e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 45.73 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 20 IHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADwAGQERARRLavlpqvsslgFSFRVEEVVGMG 99
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTA-EQPEDYRKL----------FSAVFTDFHLFD 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 100 RMPHGTGQRRDAEIVEAALRAADAWHLVER-----SYLALSGGERQRVHLARVLAqlwpgEEGSTLLLDEPTSMLDPlhq 174
Cdd:PRK10522 411 QLLGPEGKPANPALVEKWLERLKMAHKLELedgriSNLKLSKGQKKRLALLLALA-----EERDILLLDEWAADQDP--- 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 939342971 175 httleAVRRF---------ADCGAAVLVILHDlNLAARYCDRILLLEQGR 215
Cdd:PRK10522 483 -----HFRREfyqvllpllQEMGKTIFAISHD-DHYFIHADRLLEMRNGQ 526
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-215 |
2.19e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.11 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 17 LHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARR-LAVLPQVSSLGFSFRVEEV 95
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENgISMVHQELNLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 96 VGMGRMP-------HGTGQRRDAEIVEAALRAADAWHLVERsylaLSGGERQRVHLARVLAQlwpgeEGSTLLLDEPTSM 168
Cdd:PRK10982 94 MWLGRYPtkgmfvdQDKMYRDTKAIFDELDIDIDPRAKVAT----LSVSQMQMIEIAKAFSY-----NAKIVIMDEPTSS 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 939342971 169 LDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGR 215
Cdd:PRK10982 165 LTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
31-199 |
3.35e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.50 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 31 GVLGPNGAGKSSLLSVLCGELAPDRGRVTLqgrpladwagqERARRLAVLPQvSSLGF-SFRVEEVVGMGrmpHG----T 105
Cdd:PRK15064 31 GLIGANGCGKSTFMKILGGDLEPSAGNVSL-----------DPNERLGKLRQ-DQFAFeEFTVLDTVIMG---HTelweV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 106 GQRRDA-----EIVEA-ALRAAD----------------AWHL-------VERSYLALSG---GERQRVHLARVLAQlwp 153
Cdd:PRK15064 96 KQERDRiyalpEMSEEdGMKVADlevkfaemdgytaearAGELllgvgipEEQHYGLMSEvapGWKLRVLLAQALFS--- 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 939342971 154 geEGSTLLLDEPTSMLDpLHQHTTLEAVRRFADCgaAVLVILHD---LN 199
Cdd:PRK15064 173 --NPDILLLDEPTNNLD-INTIRWLEDVLNERNS--TMIIISHDrhfLN 216
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
26-211 |
3.47e-05 |
|
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: 42.75 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 26 PGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVtlqgrpladwagqerarrlavlpqvsslgfsFRVeevvgmgrmphgt 105
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV-------------------------------IYI------------- 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 106 gqrrDAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLAQLwpgeeGSTLLLDEPTSMLDPLHQHTTLEAVRRFA 185
Cdd:smart00382 37 ----DGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLK-----PDVLILDEITSLLDAEQEALLLLLEELRL 107
|
170 180 190
....*....|....*....|....*....|....*...
gi 939342971 186 DCGAA----VLVILH--------DLNLAARYCDRILLL 211
Cdd:smart00382 108 LLLLKseknLTVILTtndekdlgPALLRRRFDRRIVLL 145
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
6-148 |
3.84e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 44.01 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 6 GLYlRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRPLADWAGQERARRLAVLPQVSS 85
Cdd:PRK15112 19 GWF-RRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 86 LGFSFRveevvgmgrmphgtgqRRDAEIVEAALRAADAWHLVER------------------SYL--ALSGGERQRVHLA 145
Cdd:PRK15112 98 TSLNPR----------------QRISQILDFPLRLNTDLEPEQRekqiietlrqvgllpdhaSYYphMLAPGQKQRLGLA 161
|
...
gi 939342971 146 RVL 148
Cdd:PRK15112 162 RAL 164
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
9-250 |
4.71e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 44.08 E-value: 4.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 9 LRRGSNEV--LHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGR---PLADWAGQERARRL------ 77
Cdd:PRK10261 330 LNRVTREVhaVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSPGKLQALRRDIqfifqd 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 78 --AVLPQVSSLGFSFrVEEVVGMGRMPHGTGQRRDAEIVE-AALRAADAWhlveRSYLALSGGERQRVHLARVLAqLWPg 154
Cdd:PRK10261 410 pyASLDPRQTVGDSI-MEPLRVHGLLPGKAAAARVAWLLErVGLLPEHAW----RYPHEFSGGQRQRICIARALA-LNP- 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 155 eegSTLLLDEPTSMLDPLHQHTTLEAVRRFA-DCGAAVLVILHDLNLAARYCDRILLLEQG-------RCHAFATPEAAL 226
Cdd:PRK10261 483 ---KVIIADEAVSALDVSIRGQIINLLLDLQrDFGIAYLFISHDMAVVERISHRVAVMYLGqiveigpRRAVFENPQHPY 559
|
250 260
....*....|....*....|....
gi 939342971 227 TPAALKAVygidvlVQAHPERGHP 250
Cdd:PRK10261 560 TRKLMAAV------PVADPSRQRP 577
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
20-234 |
9.29e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 42.81 E-value: 9.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 20 IHLQLPPGQVVGVLGPNGAGKS-SLLSVLcgelapdrGRVTLQGRPLAD---WAGQ------ERARRLAVLPQVS----- 84
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSvSSLAIM--------GLIDYPGRVMAEkleFNGQdlqrisEKERRNLVGAEVAmifqd 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 85 ---SLGFSFRVEEVVGMGRMPHGTGQRRdaeivEAALRAADAWHLV----ERSYL-----ALSGGERQRVHLARVLAQlw 152
Cdd:PRK11022 98 pmtSLNPCYTVGFQIMEAIKVHQGGNKK-----TRRQRAIDLLNQVgipdPASRLdvyphQLSGGMSQRVMIAMAIAC-- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 153 pgeEGSTLLLDEPTSMLDPLHQHTTLEAVRRFADC-GAAVLVILHDLNLAARYCDRILLL------EQGRCHA-FATPEA 224
Cdd:PRK11022 171 ---RPKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMyagqvvETGKAHDiFRAPRH 247
|
250
....*....|
gi 939342971 225 ALTPAALKAV 234
Cdd:PRK11022 248 PYTQALLRAL 257
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
134-198 |
1.02e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 43.14 E-value: 1.02e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 939342971 134 LSGGERQRVHLARVLAQLwpgEEGSTL-LLDEPTSmldPLHQHTT---LEAVRRFADCGAAVLVILHDL 198
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKR---STGKTLyILDEPTT---GLHFEDIrklLEVLHRLVDKGNTVVVIEHNL 893
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
16-50 |
1.39e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.69 E-value: 1.39e-04
10 20 30
....*....|....*....|....*....|....*
gi 939342971 16 VLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGE 50
Cdd:PRK10938 275 ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGD 309
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-170 |
3.55e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.54 E-value: 3.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 1 MLHVEGLYLRRGSNEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQGRpladwagqeRARRLAV- 79
Cdd:PRK10938 3 SLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFS---------HITRLSFe 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 80 -LPQVSSLGFSFRVEEVVGMGrmPHGTGqRRDAEIVEAALRAADAW----------HLVERSYLALSGGERQRVHLARVL 148
Cdd:PRK10938 74 qLQKLVSDEWQRNNTDMLSPG--EDDTG-RTTAEIIQDEVKDPARCeqlaqqfgitALLDRRFKYLSTGETRKTLLCQAL 150
|
170 180
....*....|....*....|..
gi 939342971 149 AQlwpgeEGSTLLLDEPTSMLD 170
Cdd:PRK10938 151 MS-----EPDLLILDEPFDGLD 167
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
15-215 |
3.88e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 41.45 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 15 EVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELaPDR--GRVTLQGRPL-------ADWAG-----QERARR---- 76
Cdd:PRK13549 276 KRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAY-PGRweGEIFIDGKPVkirnpqqAIAQGiamvpEDRKRDgivp 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 77 ---------LAVLPQVSslgfsfrveevvGMGRMPHGTGQRR-DAEIVEAALRAADAWHLVERsylaLSGGERQRVHLAR 146
Cdd:PRK13549 355 vmgvgknitLAALDRFT------------GGSRIDDAAELKTiLESIQRLKVKTASPELAIAR----LSGGNQQKAVLAK 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 939342971 147 VLAqLWPgeegSTLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGR 215
Cdd:PRK13549 419 CLL-LNP----KILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGK 482
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
125-200 |
5.85e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 40.45 E-value: 5.85e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 939342971 125 HLVERSYLALSGGERQrvhLARVLAQLW-PGEEGSTLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNL 200
Cdd:pfam13304 228 GGGELPAFELSDGTKR---LLALLAALLsALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPLL 301
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
134-197 |
6.42e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.78 E-value: 6.42e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 939342971 134 LSGGERQRVHLARvlaQLwpgeeGSTL-----LLDEPTSmldPLHQHTT---LEAVRRFADCGAAVLVILHD 197
Cdd:COG0178 486 LSGGEAQRIRLAT---QI-----GSGLvgvlyVLDEPSI---GLHQRDNdrlIETLKRLRDLGNTVIVVEHD 546
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
17-62 |
1.05e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 39.41 E-value: 1.05e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 939342971 17 LHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQG 62
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG 85
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
14-172 |
1.56e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 38.70 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 14 NEVLHDIHLQLPPGQVVGVLGPNGAGKSSLLSVLCGELAPDRGRVTLQG-------RPLADWAGQERARRLavlpqvssl 86
Cdd:PRK13541 13 QKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNcninniaKPYCTYIGHNLGLKL--------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 87 gfSFRVEEVVGMGRMPHGTgqrrdAEIVEAALRAADAWHLVERSYLALSGGERQRVHLARVLA---QLWPGEEGSTLLLD 163
Cdd:PRK13541 84 --EMTVFENLKFWSEIYNS-----AETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIAcqsDLWLLDEVETNLSK 156
|
....*....
gi 939342971 164 EPTSMLDPL 172
Cdd:PRK13541 157 ENRDLLNNL 165
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
133-170 |
3.71e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 38.47 E-value: 3.71e-03
10 20 30
....*....|....*....|....*....|....*...
gi 939342971 133 ALSGGERQRVHLARVLAQlwpgeEGSTLLLDEPTSMLD 170
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLR-----EPKILLLDEATSSLD 1390
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
30-70 |
3.93e-03 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 36.06 E-value: 3.93e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 939342971 30 VGVLG-PNgAGKSSLLSVLCGELA-----------PDRGRVTLQGRP--LADWAG 70
Cdd:pfam01926 2 VALVGrPN-VGKSTLINALTGAKAivsdypgttrdPNEGRLELKGKQiiLVDTPG 55
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
135-238 |
3.94e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 38.02 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 135 SGGERQRVHLARVLaQLWPgeegSTLLLDEPTSMLDPLHQHTTLEAvrrFADC----GAAVLVILHDLNLAARYCDRILL 210
Cdd:PRK11308 156 SGGQRQRIAIARAL-MLDP----DVVVADEPVSALDVSVQAQVLNL---MMDLqqelGLSYVFISHDLSVVEHIADEVMV 227
|
90 100 110
....*....|....*....|....*....|....*
gi 939342971 211 LEQGRC-------HAFATPEAALTPAALKAVYGID 238
Cdd:PRK11308 228 MYLGRCvekgtkeQIFNNPRHPYTQALLSATPRLN 262
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
16-215 |
5.90e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 37.46 E-value: 5.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 16 VLHDIHLQLPPGQVVGVLGPNGAGKSsllsvlcgELAPD----------RGRVTLQGRP-------------LAdWAGQE 72
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRT--------ELAMSvfgrsygrniSGTVFKDGKEvdvstvsdaidagLA-YVTED 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 73 RA----------RR---LAVLPQVSSLGFSFRVEEVVgmgrmpHGTGQRRDAEIveaalRAADAWHLVERsylaLSGGER 139
Cdd:NF040905 346 RKgyglnliddiKRnitLANLGKVSRRGVIDENEEIK------VAEEYRKKMNI-----KTPSVFQKVGN----LSGGNQ 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 939342971 140 QRVHLARvlaqlWPGEEGSTLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLAARYCDRILLLEQGR 215
Cdd:NF040905 411 QKVVLSK-----WLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGR 481
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
133-214 |
5.96e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 37.89 E-value: 5.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 939342971 133 ALSGGERQRVHLARVLAQlwPGEEGSTLLLDEPTSMLDPLHQHTTLEAVRRFADCGAAVLVILHDLNLaARYCDRILLLE 212
Cdd:PRK00635 1699 SLSLSEKIAIKIAKFLYL--PPKHPTLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDPAL-LKQADYLIEMG 1775
|
..
gi 939342971 213 QG 214
Cdd:PRK00635 1776 PG 1777
|
|
| |
