|
Name |
Accession |
Description |
Interval |
E-value |
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
2-230 |
6.37e-112 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 320.24 E-value: 6.37e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVARGMAYV 81
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 82 PQGQQCFPHLTAAENLRLVADARRDGAVAT-AEALDLFPALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTE 160
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTGLAALPRRSRKIpDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 161 GIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGDGGVTAEREVRAALAV 230
Cdd:TIGR03410 161 GIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDKVRRYLAV 230
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-227 |
2.70e-105 |
|
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: 303.44 E-value: 2.70e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVARGMAY 80
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 81 VPQGQQCFPHLTAAENLRLVADARRDGAVATA---EALDLFPALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDE 157
Cdd:COG0410 83 VPEGRRIFPSLTVEENLLLGAYARRDRAEVRAdleRVYELFPRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1033140466 158 PTEGIQPSVVAEIQERIVELtRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGDGG-VTAEREVRAA 227
Cdd:COG0410 163 PSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAeLLADPEVREA 232
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-216 |
3.13e-99 |
|
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: 287.79 E-value: 3.13e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVARGMAYV 81
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 82 PQGQQCFPHLTAAENLRLVADARRDGAVAT--AEALDLFPALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPT 159
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRRAKRKArlERVYELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1033140466 160 EGIQPSVVAEIQERIVELtRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGDG 216
Cdd:cd03224 161 EGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTA 216
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-227 |
2.84e-56 |
|
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: 179.46 E-value: 2.84e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVARGMAY 80
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLGIAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 81 VPQGQQCFPHLTAAENLRLVADARRDGAV----------------ATAEALDL--FPALRPLLRRRAGLLSGGQRQQLAI 142
Cdd:COG0411 84 TFQNPRLFPELTVLENVLVAAHARLGRGLlaallrlprarreereARERAEELleRVGLADRADEPAGNLSYGQQRRLEI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 143 ARALITRPRLLMLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGD-GGVTAE 221
Cdd:COG0411 164 ARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTpAEVRAD 243
|
....*.
gi 1033140466 222 REVRAA 227
Cdd:COG0411 244 PRVIEA 249
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-215 |
8.12e-56 |
|
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: 177.63 E-value: 8.12e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVARGMAYV 81
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 82 PQGQQCFPHLTAAENLRLVADARRDGAVATA--------------EALDLFpALRPLLRRRAGLLSGGQRQQLAIARALI 147
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAQARTGSGLLLArarreereareraeELLERV-GLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1033140466 148 TRPRLLMLDEPTEGIQPSVVAEIQERIVELtRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGD 215
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGT 226
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-215 |
2.87e-55 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 176.41 E-value: 2.87e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAphERVARGMAYV 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDP--AEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 82 PQGQQCFPHLTAAENLRLVADARR-DGAVATA---EALDLFpALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDE 157
Cdd:COG1131 79 PQEPALYPDLTVRENLRFFARLYGlPRKEAREridELLELF-GLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1033140466 158 PTEGIQPSVVAEIQERIVELTRQsGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGD 215
Cdd:COG1131 158 PTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGT 214
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-210 |
2.59e-51 |
|
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: 164.11 E-value: 2.59e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRlaPHERVARGMAYV 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK--EPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 82 PQGQQCFPHLTAAENLRlvadarrdgavataealdlfpalrpllrrraglLSGGQRQQLAIARALITRPRLLMLDEPTEG 161
Cdd:cd03230 79 PEEPSLYENLTVRENLK---------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSG 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1033140466 162 IQPSVVAEIQERIVELTRQsGFSVLLVEQHLGFALRVANRYHVLESGRV 210
Cdd:cd03230 126 LDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-215 |
4.20e-51 |
|
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: 166.37 E-value: 4.20e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERvARGMAY 80
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRREL-ARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 81 VPQGQQCFPHLTAAEnlrLVA------------DARRDGAVAtAEALDLFpALRPLLRRRAGLLSGGQRQQLAIARALIT 148
Cdd:COG1120 80 VPQEPPAPFGLTVRE---LVAlgryphlglfgrPSAEDREAV-EEALERT-GLEHLADRPVDELSGGERQRVLIARALAQ 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1033140466 149 RPRLLMLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGD 215
Cdd:COG1120 155 EPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGP 221
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-210 |
2.10e-50 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 167.58 E-value: 2.10e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHErvaRGMAY 80
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK---RNVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 81 VPQGQQCFPHLTAAEN------LRLVADARRDGAVatAEALDLFpALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLM 154
Cdd:COG3842 82 VFQDYALFPHLTVAENvafglrMRGVPKAEIRARV--AELLELV-GLEGLADRYPHQLSGGQQQRVALARALAPEPRVLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1033140466 155 LDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLV-----EqhlgfALRVANRYHVLESGRV 210
Cdd:COG3842 159 LDEPLSALDAKLREEMREELRRLQRELGITFIYVthdqeE-----ALALADRIAVMNDGRI 214
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-215 |
3.95e-50 |
|
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: 163.10 E-value: 3.95e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVARGMAYV 81
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 82 PQGQQCFPHLTAAENLRLVADAR---RDGAVATAEA-LDLFpALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDE 157
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRglsKKEREEKLEElLEEF-HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1033140466 158 PTEGIQPSVVAEIQERIVELtRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGD 215
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIKIL-KDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGT 216
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-214 |
1.94e-49 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 160.76 E-value: 1.94e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHErvaRGMAYV 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER---RNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 82 PQGQQCFPHLTAAEN----LRLVADARRDGAVATAEALDLFpALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDE 157
Cdd:cd03259 78 FQDYALFPHLTVAENiafgLKLRGVPKAEIRARVRELLELV-GLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1033140466 158 PTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHG 214
Cdd:cd03259 157 PLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-228 |
1.83e-48 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 159.25 E-value: 1.83e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERvaRGMAY 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREAR--RQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 81 VPQGQQCFPHLTAAENLRLVADA----RRDGAVATAEALDLFpALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLD 156
Cdd:COG4555 79 LPDERGLYDRLTVRENIRYFAELyglfDEELKKRIEELIELL-GLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1033140466 157 EPTEGIQPSVVAEIQERIVELtRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGDGGVTAEREVRAAL 228
Cdd:COG4555 158 EPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEENL 228
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-215 |
2.24e-47 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 156.34 E-value: 2.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVARGMAY 80
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 81 VPQGQQCFPHLTAAENLRLVADAR---RDGAVATAEAL-DLFpALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLD 156
Cdd:COG1137 83 LPQEASIFRKLTVEDNILAVLELRklsKKEREERLEELlEEF-GITHLRKSKAYSLSGGERRRVEIARALATNPKFILLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1033140466 157 EPTEGIQPSVVAEIQERIVELtRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGD 215
Cdd:COG1137 162 EPFAGVDPIAVADIQKIIRHL-KERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGT 219
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-210 |
6.04e-45 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 153.30 E-value: 6.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHErvaRGMAY 80
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD---RNIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 81 VPQGQQCFPHLTAAEN----LRL--VADARRDGAVA-TAEALDlfpaLRPLLRRRAGLLSGGQRQQLAIARALITRPRLL 153
Cdd:COG3839 80 VFQSYALYPHMTVYENiafpLKLrkVPKAEIDRRVReAAELLG----LEDLLDRKPKQLSGGQRQRVALGRALVREPKVF 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1033140466 154 MLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLV--EQH--LGFALRVAnryhVLESGRV 210
Cdd:COG3839 156 LLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVthDQVeaMTLADRIA----VMNDGRI 212
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-227 |
1.48e-44 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 149.26 E-value: 1.48e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVARGMAY 80
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 81 VPQGQQCFPHLTAAENLRL---VADaRRDGAVATAEALDLFPALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDE 157
Cdd:PRK11614 85 VPEGRRVFSRMTVEENLAMggfFAE-RDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1033140466 158 PTEGIQPSVVAEIQERIVELtRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGDG-GVTAEREVRAA 227
Cdd:PRK11614 164 PSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGdALLANEAVRSA 233
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-215 |
1.75e-44 |
|
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: 149.18 E-value: 1.75e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYG----RSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERvAR 76
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAF-RR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 77 GMAYVPQ--GQQCFPHLTAAENLR--LVADARRDGAVATAEALDLFpALRP-LLRRRAGLLSGGQRQQLAIARALITRPR 151
Cdd:COG1124 80 RVQMVFQdpYASLHPRHTVDRILAepLRIHGLPDREERIAELLEQV-GLPPsFLDRYPHQLSGGQRQRVAIARALILEPE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1033140466 152 LLMLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGD 215
Cdd:COG1124 159 LLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELT 222
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-214 |
2.27e-44 |
|
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: 146.81 E-value: 2.27e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 3 TLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERvARGMAYVP 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL-ARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 83 QgqqcfphltaaenlrlvadarrdgavataeALDLFpALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGI 162
Cdd:cd03214 80 Q------------------------------ALELL-GLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1033140466 163 QPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHG 214
Cdd:cd03214 129 DIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-210 |
6.08e-44 |
|
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: 147.26 E-value: 6.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 4 LRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHE--RVARGMAYV 81
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyRLRRRMGML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 82 PQGQQCFPHLTAAEN--------LRLVADARRDgavATAEALDLFpALRPLLRRRAGLLSGGQRQQLAIARALITRPRLL 153
Cdd:cd03261 83 FQSGALFDSLTVFENvafplrehTRLSEEEIRE---IVLEKLEAV-GLRGAEDLYPAELSGGMKKRVALARALALDPELL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1033140466 154 MLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRV 210
Cdd:cd03261 159 LYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKI 215
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-209 |
6.19e-44 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 145.41 E-value: 6.19e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVARG-MAY 80
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRrIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 81 VPQGQQCFPHLTAAENLRLvadarrdgavataealdlfpalrpllrrragLLSGGQRQQLAIARALITRPRLLMLDEPTE 160
Cdd:cd03229 81 VFQDFALFPHLTVLENIAL-------------------------------GLSGGQQQRVALARALAMDPDVLLLDEPTS 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1033140466 161 GIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGR 209
Cdd:cd03229 130 ALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-215 |
6.85e-44 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 153.91 E-value: 6.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGY-----GRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHER-- 73
Cdd:COG1123 260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLre 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 74 VARGMAYVPQG--QQCFPHLTAAE-------NLRLVADARRDGAVAtaEALDLFpALRP-LLRRRAGLLSGGQRQQLAIA 143
Cdd:COG1123 340 LRRRVQMVFQDpySSLNPRMTVGDiiaeplrLHGLLSRAERRERVA--ELLERV-GLPPdLADRYPHELSGGQRQRVAIA 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1033140466 144 RALITRPRLLMLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGD 215
Cdd:COG1123 417 RALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGP 488
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-187 |
7.19e-44 |
|
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: 146.08 E-value: 7.19e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAphERVARGMAY 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR--EDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 81 VPQGQQCFPHLTAAENLRLVADAR--RDGAVATAEALDLFpALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEP 158
Cdd:COG4133 80 LGHADGLKPELTVRENLRFWAALYglRADREAIDEALEAV-GLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180
....*....|....*....|....*....
gi 1033140466 159 TEGIQPSVVAEIQERIVELtRQSGFSVLL 187
Cdd:COG4133 159 FTALDAAGVALLAELIAAH-LARGGAVLL 186
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-215 |
1.00e-43 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 147.05 E-value: 1.00e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVA--RGM 78
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYElrRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 79 AYVPQGQQCFPHLTAAENL--------RLVADARRD------GAVATAEALDLFPAlrpllrrragLLSGGQRQQLAIAR 144
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVafplrehtDLSEAEIRElvleklELVGLPGAADKMPS----------ELSGGMRKRVALAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1033140466 145 ALITRPRLLMLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGD 215
Cdd:COG1127 155 ALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGT 225
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-215 |
1.38e-43 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 146.77 E-value: 1.38e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVtrlaphERVARGMAY 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP------RRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 81 VPQGQQC---FPhLTAAE--------NLRLVADARRDGAVATAEALDLFpALRPLLRRRAGLLSGGQRQQLAIARALITR 149
Cdd:COG1121 80 VPQRAEVdwdFP-ITVRDvvlmgrygRRGLFRRPSRADREAVDEALERV-GLEDLADRPIGELSGGQQQRVLLARALAQD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1033140466 150 PRLLMLDEPTEGIQPSVVAEIQERIVELtRQSGFSVLLVEQHLGFALRVANRYHVLeSGRVTSHGD 215
Cdd:COG1121 158 PDLLLLDEPFAGVDAATEEALYELLREL-RREGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGP 221
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-215 |
1.66e-43 |
|
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: 145.94 E-value: 1.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGY-GRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHErVARGMAY 80
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRE-LRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 81 VPQgqqcFPH--LTAA----------ENLRLVADARRDgavATAEALDLFpALRPLLRRRAGLLSGGQRQQLAIARALIT 148
Cdd:COG1122 80 VFQ----NPDdqLFAPtveedvafgpENLGLPREEIRE---RVEEALELV-GLEHLADRPPHELSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1033140466 149 RPRLLMLDEPTEGIQPSVVAEIQERIVELtRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGD 215
Cdd:COG1122 152 EPEVLVLDEPTAGLDPRGRRELLELLKRL-NKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGT 217
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-212 |
5.40e-42 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 142.10 E-value: 5.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVH----AGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVA- 75
Cdd:COG1136 4 LLELRNLTksygTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 76 --RGMAYVPQGQQCFPHLTAAENLRLVAD-ARRDGAVATAEALDLFPA--LRPLLRRRAGLLSGGQRQQLAIARALITRP 150
Cdd:COG1136 84 rrRHIGFVFQFFNLLPELTALENVALPLLlAGVSRKERRERARELLERvgLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1033140466 151 RLLMLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLV--EQHLgfaLRVANRYHVLESGRVTS 212
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVthDPEL---AARADRVIRLRDGRIVS 224
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-215 |
1.08e-41 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 141.67 E-value: 1.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTrlAPHERVAR---- 76
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT--DSKKDINKlrrk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 77 -GMayVPQGQQCFPHLTAAEN----LRLVAdaRRDGAVATAEALDLFpalrpllrRRAGL----------LSGGQRQQLA 141
Cdd:COG1126 79 vGM--VFQQFNLFPHLTVLENvtlaPIKVK--KMSKAEAEERAMELL--------ERVGLadkadaypaqLSGGQQQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1033140466 142 IARALITRPRLLMLDEPTEGIQPSVVAEIQERIVELtRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGD 215
Cdd:COG1126 147 IARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDL-AKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGP 219
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-210 |
1.15e-41 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 144.52 E-value: 1.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDV-TRLAPHErvaRGMAY 80
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRE---RRVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 81 VPQGQQCFPHLTAAENL------RLVADARRDGAVatAEALDLFpALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLM 154
Cdd:COG1118 80 VFQHYALFPHMTVAENIafglrvRPPSKAEIRARV--EELLELV-QLEGLADRYPSQLSGGQRQRVALARALAVEPEVLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1033140466 155 LDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRV 210
Cdd:COG1118 157 LDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRI 212
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-214 |
1.78e-41 |
|
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: 140.72 E-value: 1.78e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGY----GRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVAR 76
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 77 G--MAYVPQG-QQCF-PHLTA----AENLRLVADARRDGA--VATAEALDLFPALRPLLRRRAGLLSGGQRQQLAIARAL 146
Cdd:cd03257 81 RkeIQMVFQDpMSSLnPRMTIgeqiAEPLRIHGKLSKKEArkEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1033140466 147 ITRPRLLMLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHG 214
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-224 |
2.19e-41 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 141.38 E-value: 2.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGY----GRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHervar 76
Cdd:COG1116 7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 77 gMAYVPQGQQCFPHLTAAENLRLVADAR---RDGAVATA-EALDLFpALRPLLRRRAGLLSGGQRQQLAIARALITRPRL 152
Cdd:COG1116 82 -RGVVFQEPALLPWLTVLDNVALGLELRgvpKAERRERArELLELV-GLAGFEDAYPHQLSGGMRQRVAIARALANDPEV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 153 LMLDEP-------TEgiqpsvvAEIQERIVELTRQSGFSVLLV-----EqhlgfALRVANRYHVLesgrvtSHGDGGVTA 220
Cdd:COG1116 160 LLMDEPfgaldalTR-------ERLQDELLRLWQETGKTVLFVthdvdE-----AVFLADRVVVL------SARPGRIVE 221
|
....
gi 1033140466 221 EREV 224
Cdd:COG1116 222 EIDV 225
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-210 |
2.47e-41 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 140.30 E-value: 2.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGYGRSR----VLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHervarg 77
Cdd:cd03293 1 LEVRNVSKTYGGGGgavtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 78 MAYVPQGQQCFPHLTAAEN----LRLVADARRDGAVATAEALDLFPaLRPLLRRRAGLLSGGQRQQLAIARALITRPRLL 153
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNvalgLELQGVPKAEARERAEELLELVG-LSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1033140466 154 MLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLES--GRV 210
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRI 212
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
4-209 |
4.48e-41 |
|
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: 139.14 E-value: 4.48e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 4 LRGVHAGYGRSR--VLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERvARGMAYV 81
Cdd:cd03225 2 LKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKEL-RRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 82 ---PQGQQCFPHLT-----AAENLRLVADARRDGAVATAEALDlfpaLRPLLRRRAGLLSGGQRQQLAIARALITRPRLL 153
Cdd:cd03225 81 fqnPDDQFFGPTVEeevafGLENLGLPEEEIEERVEEALELVG----LEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1033140466 154 MLDEPTEGIQPSVVAEIQERIVELtRQSGFSVLLVEQHLGFALRVANRYHVLESGR 209
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKL-KAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-210 |
1.17e-40 |
|
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: 138.05 E-value: 1.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVT-RLAPHERVARGMAY 80
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTdDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 81 VPQGQQCFPHLTAAENLRL----VADARRDGAVATAEALdlfpalrpllRRRAGL----------LSGGQRQQLAIARAL 146
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLapikVKGMSKAEAEERALEL----------LEKVGLadkadaypaqLSGGQQQRVAIARAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1033140466 147 ITRPRLLMLDEPTEGIQPSVVAEIQERIVELTrQSGFSVLLVEQHLGFALRVANRYHVLESGRV 210
Cdd:cd03262 151 AMNPKVMLFDEPTSALDPELVGEVLDVMKDLA-EEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-159 |
1.89e-40 |
|
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: 135.85 E-value: 1.89e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 17 LHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLaPHERVARGMAYVPQGQQCFPHLTAAEN 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDD-ERKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 97 LRLVAD-ARRDGAVATAEA------LDLFPALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPT 159
Cdd:pfam00005 80 LRLGLLlKGLSKREKDARAeealekLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-188 |
2.82e-40 |
|
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: 137.24 E-value: 2.82e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGV----HAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVA-- 75
Cdd:cd03255 1 IELKNLsktyGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAfr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 76 -RGMAYVPQGQQCFPHLTAAEN----LRLVADARRDGAVATAEALDLFpALRPLLRRRAGLLSGGQRQQLAIARALITRP 150
Cdd:cd03255 81 rRHIGFVFQSFNLLPDLTALENvelpLLLAGVPKKERRERAEELLERV-GLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 1033140466 151 RLLMLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLV 188
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVV 197
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-226 |
6.41e-40 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 142.85 E-value: 6.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVARGMAY 80
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAGIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 81 VPQGQQCFPHLTAAENLRLVADARRDGAV-------ATAEALDLF-PALRPllRRRAGLLSGGQRQQLAIARALITRPRL 152
Cdd:COG1129 84 IHQELNLVPNLSVAENIFLGREPRRGGLIdwramrrRARELLARLgLDIDP--DTPVGDLSVAQQQLVEIARALSRDARV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1033140466 153 LMLDEPTEGIQPSVVAEIQERIVELtRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGD-GGVTAEREVRA 226
Cdd:COG1129 162 LILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPvAELTEDELVRL 235
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
20-215 |
1.12e-39 |
|
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: 139.47 E-value: 1.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 20 VDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDV------TRLAPHervARGMAYVPQGQQCFPHLTA 93
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdsargIFLPPH---RRRIGYVFQEARLFPHLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 94 AENLRLVAD--ARRDGAVATAEALDLFpALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVAEIQ 171
Cdd:COG4148 95 RGNLLYGRKraPRAERRISFDEVVELL-GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEIL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1033140466 172 ERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGD 215
Cdd:COG4148 174 PYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGP 217
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-214 |
1.19e-39 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 137.04 E-value: 1.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVARGMAY 80
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 81 VPQGQQCFPHLTAAENLrLVADARR------DGAVAT-------AEALDL------FPALRPLLRRRAGLLSGGQRQQLA 141
Cdd:PRK11300 85 TFQHVRLFREMTVIENL-LVAQHQQlktglfSGLLKTpafrraeSEALDRaatwleRVGLLEHANRQAGNLAYGQQRRLE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1033140466 142 IARALITRPRLLMLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHG 214
Cdd:PRK11300 164 IARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANG 236
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-210 |
1.46e-39 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 136.34 E-value: 1.46e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGY-GRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHE--RVARG 77
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 78 MAYVPQGQQCFPHLTAAEN---------------LRLVADARRDGAVATAEALDLfpalRPLLRRRAGLLSGGQRQQLAI 142
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNvlagrlgrtstwrslLGLFPPEDRERALEALERVGL----ADKAYQRADQLSGGQQQRVAI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1033140466 143 ARALITRPRLLMLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRV 210
Cdd:COG3638 158 ARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRV 225
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-229 |
2.67e-39 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 135.27 E-value: 2.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSRvLHgVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHErvaRGMAY 80
Cdd:COG3840 1 MLRLDDLTYRYGDFP-LR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE---RPVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 81 VPQGQQCFPHLTAAEN--------LRLVADARRDGAVATAEAldlfpALRPLLRRRAGLLSGGQRQQLAIARALITRPRL 152
Cdd:COG3840 76 LFQENNLFPHLTVAQNiglglrpgLKLTAEQRAQVEQALERV-----GLAGLLDRLPGQLSGGQRQRVALARCLVRKRPI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1033140466 153 LMLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGDGGVTAEREVRAALA 229
Cdd:COG3840 151 LLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALA 227
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-210 |
4.01e-39 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 134.17 E-value: 4.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHE-RvaRGMAY 80
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwR--RQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 81 VPQGQQCFPHlTAAENLRLVADARRDgAVATAEALDLFPAL-RP--LLRRRAGLLSGGQRQQLAIARALITRPRLLMLDE 157
Cdd:COG4619 79 VPQEPALWGG-TVRDNLPFPFQLRER-KFDRERALELLERLgLPpdILDKPVERLSGGERQRLALIRALLLQPDVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1033140466 158 PTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRV 210
Cdd:COG4619 157 PTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-210 |
6.27e-39 |
|
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: 133.50 E-value: 6.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPherVARGMAYV 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIE---ALRRIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 82 PQGQQCFPHLTAAENLRLVADARRDGAVATAEALDLFpALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEG 161
Cdd:cd03268 78 IEAPGFYPNLTARENLRLLARLLGIRKKRIDEVLDVV-GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1033140466 162 IQPSVVAEIQERIVELtRQSGFSVLLVEQHLGFALRVANRYHVLESGRV 210
Cdd:cd03268 157 LDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
16-215 |
1.82e-38 |
|
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: 133.23 E-value: 1.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 16 VLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERvarGMAYVPQGQQCFPHLTAAE 95
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKR---DISYVPQNYALFPHMTVYK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 96 NL------RLVADARRDGAV-ATAEALdlfpALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVA 168
Cdd:cd03299 91 NIayglkkRKVDKKEIERKVlEIAEML----GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1033140466 169 EIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGD 215
Cdd:cd03299 167 KLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGK 213
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-209 |
2.90e-38 |
|
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: 130.44 E-value: 2.90e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 3 TLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHErVARGMAYVP 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEE-LRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 83 QgqqcfphltaaenlrlvadarrdgavataealdlfpalrpllrrraglLSGGQRQQLAIARALITRPRLLMLDEPTEGI 162
Cdd:cd00267 80 Q------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGL 111
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1033140466 163 QPSVVAEIQERIVELtRQSGFSVLLVEQHLGFALRVANRYHVLESGR 209
Cdd:cd00267 112 DPASRERLLELLREL-AEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-210 |
4.39e-38 |
|
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: 132.36 E-value: 4.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHErvaRGMAYV 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK---RPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 82 PQGQQCFPHLTAAEN----LRLVADARRDGAVATAEALDLFpALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDE 157
Cdd:cd03300 78 FQNYALFPHLTVFENiafgLRLKKLPKAEIKERVAEALDLV-QLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1033140466 158 PTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRV 210
Cdd:cd03300 157 PLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-210 |
4.41e-38 |
|
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: 132.31 E-value: 4.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGYGRSR-VLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHE-RVARG-M 78
Cdd:cd03256 1 IEVENLSKTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlRQLRRqI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 79 AYVPQGQQCFPHLTAAEN---------------LRLVADARRDGAVATAEALDLfpalRPLLRRRAGLLSGGQRQQLAIA 143
Cdd:cd03256 81 GMIFQQFNLIERLSVLENvlsgrlgrrstwrslFGLFPKEEKQRALAALERVGL----LDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1033140466 144 RALITRPRLLMLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRV 210
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRI 223
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-215 |
5.23e-38 |
|
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: 131.92 E-value: 5.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLL-----RPSAGTVELDGEDV-----TRLAPH 71
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIydldvDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 72 ERVarGMAYvpqgQQCFP-HLTAAEN----LRLVADARRDGAVATAEALDLFPALRPLLRRRAGL--LSGGQRQQLAIAR 144
Cdd:cd03260 81 RRV--GMVF----QKPNPfPGSIYDNvaygLRLHGIKLKEELDERVEEALRKAALWDEVKDRLHAlgLSGGQQQRLCLAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1033140466 145 ALITRPRLLMLDEPTEGIQPSVVAEIQERIVELTRQsgFSVLLVEQHLGFALRVANRYHVLESGRVTSHGD 215
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGP 223
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-214 |
2.03e-37 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 130.01 E-value: 2.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGYGRSRVLHGVDLAVPPdGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERvaRGMAYV 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGP-GMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLR--RRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 82 PQGQQCFPHLTAAENLRLVA------DARRDGAVATA-EALDLFPAlrplLRRRAGLLSGGQRQQLAIARALITRPRLLM 154
Cdd:cd03264 78 PQEFGVYPNFTVREFLDYIAwlkgipSKEVKARVDEVlELVNLGDR----AKKKIGSLSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1033140466 155 LDEPTEGIQPsvvaeiQERIV---ELTRQSGFSVLLVEQHL-GFALRVANRYHVLESGRVTSHG 214
Cdd:cd03264 154 VDEPTAGLDP------EERIRfrnLLSELGEDRIVILSTHIvEDVESLCNQVAVLNKGKLVFEG 211
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-210 |
2.07e-37 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 131.36 E-value: 2.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVH----AGYGRS-RVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHER-- 73
Cdd:COG1101 1 MLELKNLSktfnPGTVNEkRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRak 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 74 -VAR-------GMAyvpqgqqcfPHLTAAENLRL-------------VADARRDGAVATAEALDLfpALRPLLRRRAGLL 132
Cdd:COG1101 81 yIGRvfqdpmmGTA---------PSMTIEENLALayrrgkrrglrrgLTKKRRELFRELLATLGL--GLENRLDTKVGLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 133 SGGQRQQLAIARALITRPRLLMLDEPTEGIQPS---VVAEIQERIVEltrQSGFSVLLVEQHLGFALRVANRYHVLESGR 209
Cdd:COG1101 150 SGGQRQALSLLMATLTKPKLLLLDEHTAALDPKtaaLVLELTEKIVE---ENNLTTLMVTHNMEQALDYGNRLIMMHEGR 226
|
.
gi 1033140466 210 V 210
Cdd:COG1101 227 I 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-215 |
3.23e-37 |
|
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: 135.80 E-value: 3.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGY--GRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSA---GTVELDGEDVTRLAPHERvA 75
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALR-G 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 76 RGMAYVPQ--GQQCFPhLTAAENLRLVADARR-DGAVATAEALDLFPA--LRPLLRRRAGLLSGGQRQQLAIARALITRP 150
Cdd:COG1123 83 RRIGMVFQdpMTQLNP-VTVGDQIAEALENLGlSRAEARARVLELLEAvgLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1033140466 151 RLLMLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGD 215
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGP 226
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
10-214 |
1.36e-36 |
|
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: 127.65 E-value: 1.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 10 GYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEdvtrlaPHERVARGMAYVPQG---QQ 86
Cdd:cd03235 8 SYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK------PLEKERKRIGYVPQRrsiDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 87 CFPhLTAAE--------NLRLVADARRDGAVATAEALDLFpALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEP 158
Cdd:cd03235 82 DFP-ISVRDvvlmglygHKGLFRRLSKADKAKVDEALERV-GLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1033140466 159 TEGIQPSVVAEIQERIVELtRQSGFSVLLVEQHLGFALRVANRYhVLESGRVTSHG 214
Cdd:cd03235 160 FAGVDPKTQEDIYELLREL-RREGMTILVVTHDLGLVLEYFDRV-LLLNRTVVASG 213
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
26-214 |
1.69e-36 |
|
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: 127.41 E-value: 1.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 26 PDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDG------EDVTRLAPHERvarGMAYVPQGQQCFPHLTAAENLRL 99
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsRKKINLPPQQR---KIGLVFQQYALFPHLNVRENLAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 100 VADARRDGA--VATAEALDLFpALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVAEIQERIVEL 177
Cdd:cd03297 99 GLKRKRNREdrISVDELLDLL-GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQI 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 1033140466 178 TRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHG 214
Cdd:cd03297 178 KKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-209 |
1.86e-36 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 125.96 E-value: 1.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGYGRS--RVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVARgMA 79
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN-IA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 80 YVPQGqqcfPHL---TAAENlrlvadarrdgavataealdlfpalrpllrrragLLSGGQRQQLAIARALITRPRLLMLD 156
Cdd:cd03228 80 YVPQD----PFLfsgTIREN----------------------------------ILSGGQRQRIAIARALLRDPPILILD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1033140466 157 EPTEGIQPSVVAEIQERIVELTRqsGFSVLLVEQHLGfALRVANRYHVLESGR 209
Cdd:cd03228 122 EATSALDPETEALILEALRALAK--GKTVIVIAHRLS-TIRDADRIIVLDDGR 171
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
20-214 |
3.54e-36 |
|
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: 130.23 E-value: 3.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 20 VDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTR------LAPHERvarGMAYVPQGQQCFPHLTA 93
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPEKR---RIGYVFQEARLFPHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 94 AENLRL-VADARRDGAVATAEALDLFPALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVAEIQE 172
Cdd:TIGR02142 93 RGNLRYgMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1033140466 173 RIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHG 214
Cdd:TIGR02142 173 YLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAG 214
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-218 |
4.15e-36 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 126.71 E-value: 4.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSR-VLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLaPHERVA---R 76
Cdd:COG2884 1 MIRFENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRL-KRREIPylrR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 77 GMAYVPQGQQCFPHLTAAENLRLV--------ADARRDgavaTAEALDLFpALRPLLRRRAGLLSGGQRQQLAIARALIT 148
Cdd:COG2884 80 RIGVVFQDFRLLPDRTVYENVALPlrvtgksrKEIRRR----VREVLDLV-GLSDKAKALPHELSGGEQQRVAIARALVN 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 149 RPRLLMLDEPTEGIQPSVVAEIQERIVELtRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGDGGV 218
Cdd:COG2884 155 RPELLLADEPTGNLDPETSWEIMELLEEI-NRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEARGV 223
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-215 |
9.45e-36 |
|
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: 126.16 E-value: 9.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVH----AGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVA- 75
Cdd:cd03258 1 MIELKNVSkvfgDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 76 -RGMAYVPQGQQCFPHLTAAENLRL---VADARRDGAVATAEALDLFPALRPLLRRRAGLLSGGQRQQLAIARALITRPR 151
Cdd:cd03258 81 rRRIGMIFQHFNLLSSRTVFENVALpleIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1033140466 152 LLMLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGD 215
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGT 224
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-215 |
1.36e-35 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 132.19 E-value: 1.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGY-GRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERvARGMAY 80
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW-RRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 81 VPQgQQCFPHLTAAENLRLVA----DARRDGAVATAEALDLFPALR-----PLLRRRAGlLSGGQRQQLAIARALITRPR 151
Cdd:COG4988 416 VPQ-NPYLFAGTIRENLRLGRpdasDEELEAALEAAGLDEFVAALPdgldtPLGEGGRG-LSGGQAQRLALARALLRDAP 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1033140466 152 LLMLDEPTEGIQPSVVAEIQERIVELTRQSgfSVLLVEQHLGfALRVANRYHVLESGRVTSHGD 215
Cdd:COG4988 494 LLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLA-LLAQADRILVLDDGRIVEQGT 554
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-214 |
5.17e-35 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 124.02 E-value: 5.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGY----GRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRlAPHErVAR 76
Cdd:cd03266 1 MITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAE-ARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 77 GMAYVPQGQQCFPHLTAAENLRLVAD---ARRDGAVATAEALDLFPALRPLLRRRAGLLSGGQRQQLAIARALITRPRLL 153
Cdd:cd03266 79 RLGFVSDSTGLYDRLTARENLEYFAGlygLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1033140466 154 MLDEPTEGIQPSVVAEIQERIVELtRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHG 214
Cdd:cd03266 159 LLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
11-214 |
1.64e-34 |
|
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: 122.48 E-value: 1.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 11 YGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAphERVARGMAYVPQGQQCFPH 90
Cdd:cd03265 10 YGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP--REVRRRIGIVFQDLSVDDE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 91 LTAAENL----RLVADARRDGAVATAEALDLFpALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSV 166
Cdd:cd03265 88 LTGWENLyihaRLYGVPGAERRERIDELLDFV-GLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQT 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1033140466 167 VAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHG 214
Cdd:cd03265 167 RAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-214 |
2.34e-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: 129.57 E-value: 2.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGYGRSR--VLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHErVARGMA 79
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPAS-LRRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 80 YVPQGQQCFpHLTAAENLRLVADARRDGAVatAEALDLFPALRPLLRRRAGL----------LSGGQRQQLAIARALITR 149
Cdd:COG2274 553 VVLQDVFLF-SGTIRENITLGDPDATDEEI--IEAARLAGLHDFIEALPMGYdtvvgeggsnLSGGQRQRLAIARALLRN 629
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1033140466 150 PRLLMLDEPTEGIQPSVVAEIQERIVELTRqsGFSVLLVEQHLGfALRVANRYHVLESGRVTSHG 214
Cdd:COG2274 630 PRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLS-TIRLADRIIVLDKGRIVEDG 691
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-211 |
3.01e-34 |
|
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: 120.23 E-value: 3.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVARGMAYV 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 82 PQgqqcfphltaaenlrlvadarrdgavataealdlfpalrpllrrraglLSGGQRQQLAIARALITRPRLLMLDEPTEG 161
Cdd:cd03216 81 YQ------------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAA 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1033140466 162 IQPSVVAEIQERIVELtRQSGFSVLLVEQHLGFALRVANRYHVLESGRVT 211
Cdd:cd03216 113 LTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-210 |
6.65e-34 |
|
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: 121.68 E-value: 6.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHErvaRGMAYV 81
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE---RNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 82 PQGQQCFPHLTAAEN----LRLVADARRDGAV---ATAEALDLFPALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLM 154
Cdd:cd03296 80 FQHYALFRHMTVFDNvafgLRVKPRSERPPEAeirAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1033140466 155 LDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRV 210
Cdd:cd03296 160 LDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-214 |
6.72e-34 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 127.59 E-value: 6.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGYGRSR-VLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHErVARGMAY 80
Cdd:COG1132 340 IEFENVSFSYPGDRpVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLES-LRRQIGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 81 VPQGQQCFpHLTAAENLRL-VADARRDG---AVATAEALDLFPALrP-----LLRRRAGLLSGGQRQQLAIARALITRPR 151
Cdd:COG1132 419 VPQDTFLF-SGTIRENIRYgRPDATDEEveeAAKAAQAHEFIEAL-PdgydtVVGERGVNLSGGQRQRIAIARALLKDPP 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1033140466 152 LLMLDEPTEGIQPSVVAEIQERIVELTRqsGFSVLLVEQHLGfALRVANRYHVLESGRVTSHG 214
Cdd:COG1132 497 ILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLS-TIRNADRILVLDDGRIVEQG 556
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-212 |
1.68e-33 |
|
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: 120.23 E-value: 1.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSR----VLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERV-- 74
Cdd:COG4181 8 IIELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARArl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 75 -ARGMAYVPQGQQCFPHLTAAENLRLVAD-ARRDGAVATAEALDLFPALRPLLRRRAGLLSGGQRQQLAIARALITRPRL 152
Cdd:COG4181 88 rARHVGFVFQSFQLLPTLTALENVMLPLElAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 153 LMLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHvLESGRVTS 212
Cdd:COG4181 168 LFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLR-LRAGRLVE 226
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-215 |
3.41e-33 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 119.81 E-value: 3.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVAR---G 77
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRqeaG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 78 MAYvpqgQQ--CFPHLTAAENL----RLVADARRDGAVATAEALdlfpaLRPL-LRRRAG----LLSGGQRQQLAIARAL 146
Cdd:PRK09493 81 MVF----QQfyLFPHLTALENVmfgpLRVRGASKEEAEKQAREL-----LAKVgLAERAHhypsELSGGQQQRVAIARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1033140466 147 ITRPRLLMLDEPTEGIQPSVVAEIQERIVELTRQsGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGD 215
Cdd:PRK09493 152 AVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGD 219
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-210 |
3.58e-33 |
|
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: 119.15 E-value: 3.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGYGRSR--VLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERvaRGMA 79
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAAR--QSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 80 YVPQGQQCFPHLTAAENLRLVADAR----RDGAVATAEALDLFpALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLML 155
Cdd:cd03263 79 YCPQFDALFDELTVREHLRFYARLKglpkSEIKEEVELLLRVL-GLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1033140466 156 DEPTEGIQPSVVAEIQERIVELTRQSgfSVLLVEQHLGFALRVANRYHVLESGRV 210
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKL 210
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
4-215 |
6.73e-33 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 118.96 E-value: 6.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 4 LRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGE--DVTRlAPHERVAR----- 76
Cdd:COG4161 5 LKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQ-KPSEKAIRllrqk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 77 -GMayVPQGQQCFPHLTAAENLrLVADARRDG---AVATAEALDLFPALR--PLLRRRAGLLSGGQRQQLAIARALITRP 150
Cdd:COG4161 84 vGM--VFQQYNLWPHLTVMENL-IEAPCKVLGlskEQAREKAMKLLARLRltDKADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1033140466 151 RLLMLDEPTEGIQPSVVAEIQERIVELTrQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGD 215
Cdd:COG4161 161 QVLLFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD 224
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-211 |
9.08e-33 |
|
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: 117.74 E-value: 9.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 3 TLRGVHAGYGRS-RVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDvtrLAPHERVaRGMAYV 81
Cdd:cd03226 1 RIENISFSYKKGtEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP---IKAKERR-KSIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 82 PQ--GQQCFPHlTAAENLRLVADARRDGAVATAEALDLFpALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPT 159
Cdd:cd03226 77 MQdvDYQLFTD-SVREELLLGLKELDAGNEQAETVLKDL-DLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1033140466 160 EGIQPSVVAEIQERIVELTRQsGFSVLLVEQHLGFALRVANRYHVLESGRVT 211
Cdd:cd03226 155 SGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-210 |
1.51e-32 |
|
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: 116.38 E-value: 1.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGygrsRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVARGMAY 80
Cdd:cd03215 4 VLEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 81 VP---QGQQCFPHLTAAENLRLvadarrdgavataealdlfpalrpllrrrAGLLSGGQRQQLAIARALITRPRLLMLDE 157
Cdd:cd03215 80 VPedrKREGLVLDLSVAENIAL-----------------------------SSLLSGGNQQKVVLARWLARDPRVLILDE 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1033140466 158 PTEGIQPSVVAEIQERIVELTRQsGFSVLLVEQHLGFALRVANRYHVLESGRV 210
Cdd:cd03215 131 PTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
21-214 |
2.07e-32 |
|
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: 116.82 E-value: 2.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 21 DLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERvarGMAYVPQGQQCFPHLTAAEN---- 96
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADR---PVSMLFQENNLFAHLTVEQNvglg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 97 ----LRLVADARRDGAVATAEAldlfpALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVAEIQE 172
Cdd:cd03298 95 lspgLKLTAEDRQAIEVALARV-----GLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1033140466 173 RIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHG 214
Cdd:cd03298 170 LVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-210 |
3.22e-32 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 116.59 E-value: 3.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHErvaRGMAYV 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD---RDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 82 PQGQQCFPHLTAAENLRL---VADARRDGAVA----TAEALDlfpaLRPLLRRRAGLLSGGQRQQLAIARALITRPRLLM 154
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFglkLRKVPKDEIDErvreVAELLQ----IEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1033140466 155 LDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRV 210
Cdd:cd03301 154 MDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-215 |
1.34e-31 |
|
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: 121.03 E-value: 1.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGY--GRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPhERVARGMA 79
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDE-DDLRRRIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 80 YVPQGqqcfPHL---TAAENLRLVADARRDGAVAtaEALDLFpALRPLLRR-RAGL----------LSGGQRQQLAIARA 145
Cdd:COG4987 413 VVPQR----PHLfdtTLRENLRLARPDATDEELW--AALERV-GLGDWLAAlPDGLdtwlgeggrrLSGGERRRLALARA 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 146 LITRPRLLMLDEPTEGIQPSVVAEIQERIVELTRQSgfSVLLVEQHLGfALRVANRYHVLESGRVTSHGD 215
Cdd:COG4987 486 LLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLA-GLERMDRILVLEDGRIVEQGT 552
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-215 |
2.09e-31 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 115.11 E-value: 2.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 4 LRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGE--DVTRlAPHERVAR----- 76
Cdd:PRK11124 5 LNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSK-TPSDKAIRelrrn 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 77 -GMayVPQGQQCFPHLTAAENLrLVADARRDG---AVATAEALDLFPALR--PLLRRRAGLLSGGQRQQLAIARALITRP 150
Cdd:PRK11124 84 vGM--VFQQYNLWPHLTVQQNL-IEAPCRVLGlskDQALARAEKLLERLRlkPYADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1033140466 151 RLLMLDEPTEGIQPSVVAEIQERIVELtRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGD 215
Cdd:PRK11124 161 QVLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD 224
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-215 |
3.63e-31 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 116.72 E-value: 3.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGV----HAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHE-RVA 75
Cdd:COG1135 1 MIELENLsktfPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 76 R---GMayVPQGQQCFPHLTAAEN----LRL--VADARRDGAVatAEALDLfpalrpllrrrAGL----------LSGGQ 136
Cdd:COG1135 81 RrkiGM--IFQHFNLLSSRTVAENvalpLEIagVPKAEIRKRV--AELLEL-----------VGLsdkadaypsqLSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1033140466 137 RQQLAIARALITRPRLLMLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGD 215
Cdd:COG1135 146 KQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGP 224
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-214 |
5.97e-31 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 113.84 E-value: 5.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVARGMAYV 81
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 82 PQGQQCFPHLTAAENLRLVADARRD-----GAVATAEALDLFPALRplLRRRAGL-LSGGQRQQLAIARALITRPRLLML 155
Cdd:PRK10895 84 PQEASIFRRLSVYDNLMAVLQIRDDlsaeqREDRANELMEEFHIEH--LRDSMGQsLSGGERRRVEIARALAANPKFILL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1033140466 156 DEPTEGIQPSVVAEIQeRIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHG 214
Cdd:PRK10895 162 DEPFAGVDPISVIDIK-RIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHG 219
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
32-215 |
6.95e-31 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 115.67 E-value: 6.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 32 VLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERvarGMAYVPQGQQCFPHLTAAEN----LRLVADARRDG 107
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLR---HINMVFQSYALFPHMTVEENvafgLKMRKVPRAEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 108 AVATAEALDLFpALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLL 187
Cdd:TIGR01187 78 KPRVLEALRLV-QLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVF 156
|
170 180
....*....|....*....|....*...
gi 1033140466 188 VEQHLGFALRVANRYHVLESGRVTSHGD 215
Cdd:TIGR01187 157 VTHDQEEAMTMSDRIAIMRKGKIAQIGT 184
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-195 |
1.38e-30 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 111.89 E-value: 1.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERvargMAY 80
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEA----CHY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 81 VPQGQQCFPHLTAAENLRLVADARRDGAVATAEALDLFpALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTE 160
Cdd:PRK13539 78 LGHRNAMKPALTVAENLEFWAAFLGGEELDIAAALEAV-GLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTA 156
|
170 180 190
....*....|....*....|....*....|....*
gi 1033140466 161 GIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFA 195
Cdd:PRK13539 157 ALDAAAVALFAELIRAHLAQGGIVIAATHIPLGLP 191
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-208 |
3.69e-30 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 111.79 E-value: 3.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 17 LHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVargmayVPQGQQCFPHLTAAEN 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV------VFQNYSLLPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 97 LRLVAD-ARRDGAVATAEA-----LDLFpALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVAEI 170
Cdd:TIGR01184 75 IALAVDrVLPDLSKSERRAiveehIALV-GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 1033140466 171 QERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESG 208
Cdd:TIGR01184 154 QEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-214 |
9.02e-30 |
|
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: 110.85 E-value: 9.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGYGRSR-VLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPhERVARGMAY 80
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDP-VELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 81 VPQGQQCFPHLTAAENLRLV------ADARRDGAVATAEAL-DLFPAlrPLLRRRAGLLSGGQRQQLAIARALITRPRLL 153
Cdd:cd03295 80 VIQQIGLFPHMTVEENIALVpkllkwPKEKIRERADELLALvGLDPA--EFADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1033140466 154 MLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHG 214
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVG 218
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-214 |
1.39e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 110.70 E-value: 1.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 5 RGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGL--LRPSA---GTVELDGEDV--TRLAPHErVARG 77
Cdd:PRK14267 8 VNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLleLNEEArveGEVRLFGRNIysPDVDPIE-VRRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 78 MAYVPQGQQCFPHLTAAENLRLvaDARRDGAVATAEALD-----------LFPALRPLLRRRAGLLSGGQRQQLAIARAL 146
Cdd:PRK14267 87 VGMVFQYPNPFPHLTIYDNVAI--GVKLNGLVKSKKELDervewalkkaaLWDEVKDRLNDYPSNLSGGQRQRLVIARAL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1033140466 147 ITRPRLLMLDEPTEGIQPSVVAEIQERIVELTRQsgFSVLLVEQHLGFALRVANRYHVLESGRVTSHG 214
Cdd:PRK14267 165 AMKPKILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVG 230
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
21-216 |
1.51e-29 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 109.57 E-value: 1.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 21 DLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERvarGMAYVPQGQQCFPHLTAAENLRL- 99
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQR---PVSMLFQENNLFAHLTVRQNIGLg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 100 ------VADARRDGAVATAEALdlfpALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVAEIQER 173
Cdd:TIGR01277 95 lhpglkLNAEQQEKVVDAAQQV----GIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLAL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1033140466 174 IVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGDG 216
Cdd:TIGR01277 171 VKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSDC 213
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-224 |
2.00e-29 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 111.44 E-value: 2.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVARGMayV 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGV--V 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 82 PQGQQCFPHLTAAENLRLVAdarRDGAVATAEALDLFPALRPLLR------RRAGLLSGGQRQQLAIARALITRPRLLML 155
Cdd:PRK13537 86 PQFDNLDPDFTVRENLLVFG---RYFGLSAAAARALVPPLLEFAKlenkadAKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1033140466 156 DEPTEGIQPSVVAEIQERIVELTrQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGDGGVTAEREV 224
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEI 230
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-214 |
2.04e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 110.39 E-value: 2.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGL--LRPSA---GTVELDGEDVTRLaPHERVAR 76
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPEArvsGEVYLDGQDIFKM-DVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 77 GMAYVPQGQQCFPHLTAAENLRL------VADARRDGAVATAEALD---LFPALRPLLRRRAGLLSGGQRQQLAIARALI 147
Cdd:PRK14247 83 RVQMVFQIPNPIPNLSIFENVALglklnrLVKSKKELQERVRWALEkaqLWDEVKDRLDAPAGKLSGGQQQRLCIARALA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1033140466 148 TRPRLLMLDEPTEGIQPSVVAEIQERIVELTRQsgFSVLLVEQHLGFALRVANRYHVLESGRVTSHG 214
Cdd:PRK14247 163 FQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWG 227
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-208 |
2.17e-29 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 112.51 E-value: 2.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHErvaRGMAYV 81
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ---RDICMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 82 PQGQQCFPHLTAAEN----LRLVADARRDGAVATAEALDLFPaLRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDE 157
Cdd:PRK11432 84 FQSYALFPHMSLGENvgygLKMLGVPKEERKQRVKEALELVD-LAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1033140466 158 PTEGIQPSVVAEIQERIVELTRQSGFSVLLV--EQHLGFALR----VANRYHVLESG 208
Cdd:PRK11432 163 PLSNLDANLRRSMREKIRELQQQFNITSLYVthDQSEAFAVSdtviVMNKGKIMQIG 219
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
16-214 |
5.95e-29 |
|
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: 108.06 E-value: 5.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 16 VLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHErVARGMAYVPQGqqcfPHL---T 92
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAD-LRRNIGYVPQD----VTLfygT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 93 AAENL---RLVADARRDGAVATAEALDLFPALRP-----LLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQP 164
Cdd:cd03245 94 LRDNItlgAPLADDERILRAAELAGVTDFVNKHPngldlQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDM 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1033140466 165 SVVAEIQERIVELTRQsgfSVLLVEQHLGFALRVANRYHVLESGRVTSHG 214
Cdd:cd03245 174 NSEERLKERLRQLLGD---KTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
10-230 |
7.37e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 112.80 E-value: 7.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 10 GYGRSRVLHGVDLAVPPD---GVAAVLGhngAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVARGMAYVP---Q 83
Cdd:COG1129 261 GLSVGGVVRDVSFSVRAGeilGIAGLVG---AGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAGIAYVPedrK 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 84 GQQCFPHLTAAENLRLVADARR------DGAVATAEALDLFPALR---PLLRRRAGLLSGGQRQQLAIARALITRPRLLM 154
Cdd:COG1129 338 GEGLVLDLSIRENITLASLDRLsrggllDRRRERALAEEYIKRLRiktPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLI 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1033140466 155 LDEPTEGIQPSVVAEIQERIVELTRQsGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGDGG-VTAEREVRAALAV 230
Cdd:COG1129 418 LDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIVGELDREeATEEAIMAAATGG 493
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
5-214 |
1.31e-28 |
|
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: 107.70 E-value: 1.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 5 RGVHAGYGRSR-VLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLaPHERVARGMAYVPQ 83
Cdd:cd03254 6 ENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDI-SRKSLRSMIGVVLQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 84 GQQCFPHlTAAENLRL-VADARRDGAVATAEALDLFPALRPL-------LRRRAGLLSGGQRQQLAIARALITRPRLLML 155
Cdd:cd03254 85 DTFLFSG-TIMENIRLgRPNATDEEVIEAAKEAGAHDFIMKLpngydtvLGENGGNLSQGERQLLAIARAMLRDPKILIL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1033140466 156 DEPTEGIQPSVVAEIQERIVELtrQSGFSVLLVEQHLGfALRVANRYHVLESGRVTSHG 214
Cdd:cd03254 164 DEATSNIDTETEKLIQEALEKL--MKGRTSIIIAHRLS-TIKNADKILVLDDGKIIEEG 219
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
16-210 |
1.72e-28 |
|
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: 107.77 E-value: 1.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 16 VLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHE--RVARGMAYVPQGQQCFPHLTA 93
Cdd:TIGR02315 17 ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrKLRRRIGMIFQHYNLIERLTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 94 AENLrLVADARRDGAVATAeaLDLFP------ALRPLLR--------RRAGLLSGGQRQQLAIARALITRPRLLMLDEPT 159
Cdd:TIGR02315 97 LENV-LHGRLGYKPTWRSL--LGRFSeedkerALSALERvgladkayQRADQLSGGQQQRVAIARALAQQPDLILADEPI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1033140466 160 EGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRV 210
Cdd:TIGR02315 174 ASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEI 224
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-215 |
2.06e-28 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 107.53 E-value: 2.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELdGE---DVTR-LAPHERVAR 76
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRV-GDitiDTARsLSQQKGLIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 77 GM----AYVPQGQQCFPHLTAAENL----RLVADARRDGAVATAEAL----------DLFPalrpllrRRaglLSGGQRQ 138
Cdd:PRK11264 82 QLrqhvGFVFQNFNLFPHRTVLENIiegpVIVKGEPKEEATARARELlakvglagkeTSYP-------RR---LSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1033140466 139 QLAIARALITRPRLLMLDEPTEGIQPSVVAEIQERIVELTrQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGD 215
Cdd:PRK11264 152 RVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLA-QEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGP 227
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-210 |
2.74e-28 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 107.46 E-value: 2.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVeLDGEdvtrlAPHERVARGMAYV 81
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGT-----APLAEAREDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 82 PQGQQCFPHLTAAENLRL-VADARRDGAVATAEALDLFPalrpllrrRAG----LLSGGQRQQLAIARALITRPRLLMLD 156
Cdd:PRK11247 87 FQDARLLPWKKVIDNVGLgLKGQWRDAALQALAAVGLAD--------RANewpaALSGGQKQRVALARALIHRPGLLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1033140466 157 EPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRV 210
Cdd:PRK11247 159 EPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-210 |
3.45e-28 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 109.12 E-value: 3.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVH---AGYGRSRV-LHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHE-RVA 75
Cdd:PRK11153 1 MIELKNISkvfPQGGRTIHaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 76 R---GMAYvpqgqQCFPHL---TAAEN----LRLVADARRDGAVATAEALDL---------FPAlrpllrrragLLSGGQ 136
Cdd:PRK11153 81 RrqiGMIF-----QHFNLLssrTVFDNvalpLELAGTPKAEIKARVTELLELvglsdkadrYPA----------QLSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1033140466 137 RQQLAIARALITRPRLLMLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRV 210
Cdd:PRK11153 146 KQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-210 |
5.64e-28 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 108.88 E-value: 5.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHervARGMAYV 81
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE---NRHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 82 PQGQQCFPHLTAAEN----LRLVADARRDGAVATAEALDLFpALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDE 157
Cdd:PRK09452 92 FQSYALFPHMTVFENvafgLRMQKTPAAEITPRVMEALRMV-QLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1033140466 158 PTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRV 210
Cdd:PRK09452 171 SLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRI 223
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-214 |
7.54e-28 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 106.35 E-value: 7.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERvARGMAY 80
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWEL-ARRRAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 81 VPQGQQC-FPhLTAAENLRL-----VADARRDGAVAtAEALDLFpALRPLLRRRAGLLSGGQRQQLAIARALI------- 147
Cdd:COG4559 80 LPQHSSLaFP-FTVEEVVALgraphGSSAAQDRQIV-REALALV-GLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvd 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 148 TRPRLLMLDEPTEGIQPSVvaeiQERIVELTRQ---SGFSVLLVEQHLGFALRVANRYHVLESGRVTSHG 214
Cdd:COG4559 157 GGPRWLFLDEPTSALDLAH----QHAVLRLARQlarRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQG 222
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
21-227 |
1.03e-27 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 105.43 E-value: 1.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 21 DLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVArGMAYvpQGQQCFPHLTAAEN---- 96
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPV-SMLF--QENNLFSHLTVAQNiglg 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 97 ----LRLVAdARRDGAVATAEALdlfpALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVAEIQE 172
Cdd:PRK10771 96 lnpgLKLNA-AQREKLHAIARQM----GIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1033140466 173 RIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGDGGVTAEREVRAA 227
Cdd:PRK10771 171 LVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKASAS 225
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-210 |
1.37e-27 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 107.06 E-value: 1.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGY----GRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRP---SAGTVELDGEDVTRLAPHE- 72
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 73 RVARG--MAYVPQ------------GQQcfphltAAENLRLVADARRDGAVATA-EALDL----FPALRplLRRRAGLLS 133
Cdd:COG0444 81 RKIRGreIQMIFQdpmtslnpvmtvGDQ------IAEPLRIHGGLSKAEARERAiELLERvglpDPERR--LDRYPHELS 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1033140466 134 GGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRV 210
Cdd:COG0444 153 GGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRI 229
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-223 |
2.62e-27 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 108.58 E-value: 2.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVARGMAY 80
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALGIGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 81 VPQGQQCFPHLTAAENLRLVADARRDGAVATAEA------------LDLFPalrpllRRRAGLLSGGQRQQLAIARALIT 148
Cdd:COG3845 85 VHQHFMLVPNLTVAENIVLGLEPTKGGRLDRKAArarirelserygLDVDP------DAKVEDLSVGEQQRVEILKALYR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1033140466 149 RPRLLMLDEPTEGIQPsvvAEIQE--RIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGDGGVTAERE 223
Cdd:COG3845 159 GARILILDEPTAVLTP---QEADElfEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEE 232
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-214 |
3.04e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 104.47 E-value: 3.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERvARGMAY 80
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAEL-ARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 81 VPQ-GQQCFPhLTAAENLRL----VADARRDGAVATAEALDLFpALRPLLRRRAGLLSGGQRQQLAIARALI------TR 149
Cdd:PRK13548 81 LPQhSSLSFP-FTVEEVVAMgrapHGLSRAEDDALVAAALAQV-DLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1033140466 150 PRLLMLDEPTEGIQPSVvaeiQERIV----ELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHG 214
Cdd:PRK13548 159 PRWLLLDEPTSALDLAH----QHHVLrlarQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADG 223
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-214 |
3.27e-27 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 104.71 E-value: 3.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHErVARGMAY 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQ-LARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 81 VPQgqqcfpHLTAAENL---RLVADAR------------RDGAVATAEALDLfpALRPLLRRRAGLLSGGQRQQLAIARA 145
Cdd:PRK11231 81 LPQ------HHLTPEGItvrELVAYGRspwlslwgrlsaEDNARVNQAMEQT--RINHLADRRLTDLSGGQRQRAFLAMV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1033140466 146 LITRPRLLMLDEPTEGIQPSVVAEIQERIVELtRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHG 214
Cdd:PRK11231 153 LAQDTPVVLLDEPTTYLDINHQVELMRLMREL-NTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQG 220
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-215 |
7.61e-27 |
|
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: 102.22 E-value: 7.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGL--LRPSAGTVELDGEDVTRLAPHERVARGMA 79
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 80 YVPQGQQCFPHLTAAENLRLVADArrdgavataealdlfpalrpllrrraglLSGGQRQQLAIARALITRPRLLMLDEPT 159
Cdd:cd03217 81 LAFQYPPEIPGVKNADFLRYVNEG----------------------------FSGGEKKRNEILQLLLLEPDLAILDEPD 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1033140466 160 EGIQPSVVAEIQERIVELtRQSGFSVLLVeQHLG--FALRVANRYHVLESGRVTSHGD 215
Cdd:cd03217 133 SGLDIDALRLVAEVINKL-REEGKSVLII-THYQrlLDYIKPDRVHVLYDGRIVKSGD 188
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-214 |
1.11e-26 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 102.85 E-value: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRlAPHERVARGMAY 80
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVAT-TPSRELAKRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 81 VPQGQQCFPHLTAAEnlrLVADAR---------RDGAVATAEALDLFpALRPLLRRRAGLLSGGQRQQLAIARALITRPR 151
Cdd:COG4604 80 LRQENHINSRLTVRE---LVAFGRfpyskgrltAEDREIIDEAIAYL-DLEDLADRYLDELSGGQRQRAFIAMVLAQDTD 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1033140466 152 LLMLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHG 214
Cdd:COG4604 156 YVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQG 218
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
2-193 |
1.26e-26 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 101.67 E-value: 1.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHErvARGMAYV 81
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP--HENILYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 82 PQGQQCFPHLTAAENLRLVADARRDGAVATAEALDLFpALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEG 161
Cdd:TIGR01189 79 GHLPGLKPELSALENLHFWAAIHGGAQRTIEDALAAV-GLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170 180 190
....*....|....*....|....*....|..
gi 1033140466 162 IQPSVVAEIQERIVELTRQSGFSVLLVEQHLG 193
Cdd:TIGR01189 158 LDKAGVALLAGLLRAHLARGGIVLLTTHQDLG 189
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-214 |
1.37e-26 |
|
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: 101.59 E-value: 1.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHErvargMAYV 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNR-----IGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 82 PQGQQCFPHLTAAENLRLVAD----ARRDgavATAEALDLFP--ALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLML 155
Cdd:cd03269 76 PEERGLYPKMKVIDQLVYLAQlkglKKEE---ARRRIDEWLErlELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1033140466 156 DEPTEGIQPSVVAEIQERIVELTRQsGFSVLLVEQHLGFALRVANRYHVLESGRVTSHG 214
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-211 |
1.59e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 106.26 E-value: 1.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHA-GYGRSRVLHGVDLAVPPD---GVAAVlghNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVARG 77
Cdd:COG3845 258 LEVENLSVrDDRGVPALKDVSLEVRAGeilGIAGV---AGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLG 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 78 MAYVP---QGQQCFPHLTAAENlrLVADARRDGAVATAEALDlFPALR--------------PLLRRRAGLLSGGQRQQL 140
Cdd:COG3845 335 VAYIPedrLGRGLVPDMSVAEN--LILGRYRRPPFSRGGFLD-RKAIRafaeelieefdvrtPGPDTPARSLSGGNQQKV 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1033140466 141 AIARALITRPRLLMLDEPTEGIQPSVVAEIQERIVELtRQSGFSVLLVEQHLGFALRVANRYHVLESGRVT 211
Cdd:COG3845 412 ILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
17-210 |
1.87e-26 |
|
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: 102.72 E-value: 1.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 17 LHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVA---RGMAYVPQGQQCFPHLTA 93
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrKKISMVFQSFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 94 AEN----LRLVADARRDGAVATAEALDLFpALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVAE 169
Cdd:cd03294 120 LENvafgLEVQGVPRAEREERAAEALELV-GLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRRE 198
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1033140466 170 IQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRV 210
Cdd:cd03294 199 MQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-215 |
2.81e-26 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 104.53 E-value: 2.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVARGMAy 80
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMF- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 81 vpQGQQCFPHLTAAENLR--LVAD--ARRDGAVATAEALDLFpALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLD 156
Cdd:PRK11607 98 --QSYALFPHMTVEQNIAfgLKQDklPKAEIASRVNEMLGLV-HMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1033140466 157 EPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGD 215
Cdd:PRK11607 175 EPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGE 233
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-215 |
2.94e-26 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 102.19 E-value: 2.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVtRLAPH--------- 71
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEI-RLKPDrdgelvpad 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 72 ----ERVARGMAYVPQGQQCFPHLTAAENL----RLVADARRDGAVATAEAL----------DLFPALrpllrrraglLS 133
Cdd:COG4598 87 rrqlQRIRTRLGMVFQSFNLWSHMTVLENVieapVHVLGRPKAEAIERAEALlakvgladkrDAYPAH----------LS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 134 GGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVAEIQERIVELTRQsGFSVLLVEQHLGFALRVANRYHVLESGRVTSH 213
Cdd:COG4598 157 GGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQ 235
|
..
gi 1033140466 214 GD 215
Cdd:COG4598 236 GP 237
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
16-214 |
3.19e-26 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 106.10 E-value: 3.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 16 VLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHErVARGMAYVPQGQQCFpHLTAAE 95
Cdd:TIGR03375 480 ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPAD-LRRNIGYVPQDPRLF-YGTLRD 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 96 NLRLVADARRDGAV---ATAEALDLFPALRP-----LLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVV 167
Cdd:TIGR03375 558 NIALGAPYADDEEIlraAELAGVTEFVRRHPdgldmQIGERGRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSE 637
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1033140466 168 AEIQERiveLTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHG 214
Cdd:TIGR03375 638 ERFKDR---LKRWLAGKTLVLVTHRTSLLDLVDRIIVMDNGRIVADG 681
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
2-215 |
3.31e-26 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 101.68 E-value: 3.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGL--LRPSAGTVELDGEDVTRLAPHERVARGMA 79
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPDERARAGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 80 YVPQGQQCFPHLTAAENLRLVADARRDGAVATAEALDLfpaLRPLLRR---------R---AGLlSGGQRQQLAIARALI 147
Cdd:COG0396 81 LAFQYPVEIPGVSVSNFLRTALNARRGEELSAREFLKL---LKEKMKElgldedfldRyvnEGF-SGGEKKRNEILQMLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1033140466 148 TRPRLLMLDEPTEGI-----QpsVVAEIQERIveltRQSGFSVLLVeQHLGFALR--VANRYHVLESGRVTSHGD 215
Cdd:COG0396 157 LEPKLAILDETDSGLdidalR--IVAEGVNKL----RSPDRGILII-THYQRILDyiKPDFVHVLVDGRIVKSGG 224
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-214 |
4.67e-26 |
|
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: 101.31 E-value: 4.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTV------ELDGEDVTRLAPHerv 74
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDvrlfgeRRGGEDVWELRKR--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 75 argMAYV-PQGQQCFPHLTAAENL------------RLVADARRDGAVATAEALDLfpalRPLLRRRAGLLSGGQRQQLA 141
Cdd:COG1119 80 ---IGLVsPALQLRFPRDETVLDVvlsgffdsiglyREPTDEQRERARELLELLGL----AHLADRPFGTLSQGEQRRVL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1033140466 142 IARALITRPRLLMLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHG 214
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAG 225
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-159 |
5.40e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 104.76 E-value: 5.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELdGEDVTrlaphervargMAY 80
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK-----------IGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 81 VPQGQQCF-PHLTAAENLRLVADARRDGAV-ATAEALdLFPALRplLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEP 158
Cdd:COG0488 383 FDQHQEELdPDKTVLDELRDGAPGGTEQEVrGYLGRF-LFSGDD--AFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEP 459
|
.
gi 1033140466 159 T 159
Cdd:COG0488 460 T 460
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-214 |
8.34e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 102.60 E-value: 8.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 4 LRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLApheRVAR-GMAYVP 82
Cdd:PRK13536 44 LAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARA---RLARaRIGVVP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 83 QGQQCFPHLTAAENL----RLVADARRDGAVATAEALDlFPALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEP 158
Cdd:PRK13536 121 QFDNLDLEFTVRENLlvfgRYFGMSTREIEAVIPSLLE-FARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEP 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1033140466 159 TEGIQPSVVAEIQERIVELTRQsGFSVLLVEQHLGFALRVANRYHVLESGRVTSHG 214
Cdd:PRK13536 200 TTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
16-210 |
8.94e-26 |
|
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: 98.44 E-value: 8.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 16 VLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVARgMAYVPQGQQCFPHlTAAE 95
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDH-VGYLPQDDELFSG-SIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 96 NlrlvadarrdgavataealdlfpalrpllrrragLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVAEIQERIV 175
Cdd:cd03246 95 N----------------------------------ILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIA 140
|
170 180 190
....*....|....*....|....*....|....*
gi 1033140466 176 ELtRQSGFSVLLVeQHLGFALRVANRYHVLESGRV 210
Cdd:cd03246 141 AL-KAAGATRIVI-AHRPETLASADRILVLEDGRV 173
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-215 |
9.14e-26 |
|
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: 104.44 E-value: 9.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGYGRSR--VLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPhERVARGMA 79
Cdd:COG4618 331 LSVENLTVVPPGSKrpILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDR-EELGRHIG 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 80 YVPQGQQCFPHlTAAENLRLVADARRDGAVATAealdlfpalrpllrRRAGL---------------------LSGGQRQ 138
Cdd:COG4618 410 YLPQDVELFDG-TIAENIARFGDADPEKVVAAA--------------KLAGVhemilrlpdgydtrigeggarLSGGQRQ 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 139 QLAIARALITRPRLLMLDEP-----TEGIQpSVVAEIQErivelTRQSGFSVLLVEQHLGfALRVANRYHVLESGRVTSH 213
Cdd:COG4618 475 RIGLARALYGDPRLVVLDEPnsnldDEGEA-ALAAAIRA-----LKARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAF 547
|
..
gi 1033140466 214 GD 215
Cdd:COG4618 548 GP 549
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
15-214 |
9.33e-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 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: 100.99 E-value: 9.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 15 RVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVT-----RLAP-----------------HE 72
Cdd:TIGR04521 19 KALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITakkkkKLKDlrkkvglvfqfpehqlfEE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 73 RVARGMAYVPQGQQcfphLTAAEnlrlvADARrdgavaTAEALDLfpalrpllrrrAGL-----------LSGGQRQQLA 141
Cdd:TIGR04521 99 TVYKDIAFGPKNLG----LSEEE-----AEER------VKEALEL-----------VGLdeeylerspfeLSGGQMRRVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1033140466 142 IARALITRPRLLMLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHG 214
Cdd:TIGR04521 153 IAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDG 225
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-211 |
9.58e-26 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 100.71 E-value: 9.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSR----VLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPhERvar 76
Cdd:COG4525 3 MLTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGA-DR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 77 gmAYVPQGQQCFPHLTAAEN----LRL--VADARRDgavATAEALDLFPALRPLLRRRAGLLSGGQRQQLAIARALITRP 150
Cdd:COG4525 79 --GVVFQKDALLPWLNVLDNvafgLRLrgVPKAERR---ARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1033140466 151 RLLMLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLES--GRVT 211
Cdd:COG4525 154 RFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPgpGRIV 216
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-158 |
1.10e-25 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 102.61 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGY-GRSRVLHGVDLAVPpDGVAAVL-GHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHErvaRGM 78
Cdd:PRK11650 3 GLKLQAVRKSYdGKTQVIKGIDLDVA-DGEFIVLvGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD---RDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 79 AYVPQGQQCFPHLTAAENL------RLVADARRDGAVA-TAEALDlfpaLRPLLRRRAGLLSGGQRQQLAIARALITRPR 151
Cdd:PRK11650 79 AMVFQNYALYPHMSVRENMayglkiRGMPKAEIEERVAeAARILE----LEPLLDRKPRELSGGQRQRVAMGRAIVREPA 154
|
....*..
gi 1033140466 152 LLMLDEP 158
Cdd:PRK11650 155 VFLFDEP 161
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-188 |
1.66e-25 |
|
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: 103.52 E-value: 1.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGV-HAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERvARGMAY 80
Cdd:TIGR02857 322 LEFSGVsVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW-RDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 81 VPQGQQCFPHlTAAENLRL----VADARRDGAVATAEALDLFPALRPLLRRRAG----LLSGGQRQQLAIARALITRPRL 152
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENIRLarpdASDAEIREALERAGLDEFVAALPQGLDTPIGeggaGLSGGQAQRLALARAFLRDAPL 479
|
170 180 190
....*....|....*....|....*....|....*.
gi 1033140466 153 LMLDEPTEGIQPSVVAEIQERIVELTRqsGFSVLLV 188
Cdd:TIGR02857 480 LLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLV 513
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
11-210 |
2.31e-25 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 101.70 E-value: 2.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 11 YGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLapHERvARGMAYVPQGQQCFPH 90
Cdd:PRK10851 12 FGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL--HAR-DRKVGFVFQHYALFRH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 91 LTAAEN----LRLVADARR-DGAVATAEALDLFP--ALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQ 163
Cdd:PRK10851 89 MTVFDNiafgLTVLPRRERpNAAAIKAKVTQLLEmvQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1033140466 164 PSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRV 210
Cdd:PRK10851 169 AQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
3-215 |
2.77e-25 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 99.15 E-value: 2.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 3 TLRGVHAGYgRSR----VLHGVDLAVPPDGVAAVLGHNGAGKSTllrVAAGLLR---PSAGTVELDGEDVTRLAPHERVA 75
Cdd:cd03249 2 EFKNVSFRY-PSRpdvpILKGLSLTIPPGKTVALVGSSGCGKST---VVSLLERfydPTSGEILLDGVDIRDLNLRWLRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 76 RgMAYVPQGqqcfPHL---TAAENLRL----VADARRDGAVATAEALDL---FP-ALRPLLRRRAGLLSGGQRQQLAIAR 144
Cdd:cd03249 78 Q-IGLVSQE----PVLfdgTIAENIRYgkpdATDEEVEEAAKKANIHDFimsLPdGYDTLVGERGSQLSGGQKQRIAIAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1033140466 145 ALITRPRLLMLDEPTEGIQPSVVAEIQERIVELTRqsGFSVLLVeQHLGFALRVANRYHVLESGRVTSHGD 215
Cdd:cd03249 153 ALLRNPKILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVI-AHRLSTIRNADLIAVLQNGQVVEQGT 220
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-188 |
6.97e-25 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 97.17 E-value: 6.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRP---SAGTVELDGEDVTRLAPHervARG 77
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAE---QRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 78 MAYVPQGQQCFPHLTAAENLRL-----VADARRDGAVATA--EAldlfpALRPLLRRRAGLLSGGQRQQLAIARALITRP 150
Cdd:COG4136 78 IGILFQDDLLFPHLSVGENLAFalpptIGRAQRRARVEQAleEA-----GLAGFADRDPATLSGGQRARVALLRALLAEP 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 1033140466 151 RLLMLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLV 188
Cdd:COG4136 153 RALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLV 190
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
15-214 |
7.42e-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: 96.85 E-value: 7.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 15 RVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSA--GTVELDGEDVTRlaphERVARGMAYVPQGQQCFPHLT 92
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLDK----RSFRKIIGYVPQDDILHPTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 93 AAENLRLVAdarrdgavataealdlfpalrpLLRRraglLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVAEIQE 172
Cdd:cd03213 99 VRETLMFAA----------------------KLRG----LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMS 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1033140466 173 RIVELtRQSGFSVLL-VEQHLGFALRVANRYHVLESGRVTSHG 214
Cdd:cd03213 153 LLRRL-ADTGRTIICsIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
10-197 |
8.14e-25 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 96.53 E-value: 8.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 10 GYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVeldgedvtRLAPHERVArgmaYVPQ---GQQ 86
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV--------RRAGGARVA----YVPQrseVPD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 87 CFPhLTAAE--------NLRLVADARRDGAVATAEALDLFpALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEP 158
Cdd:NF040873 69 SLP-LTVRDlvamgrwaRRGLWRRLTRDDRAAVDDALERV-GLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEP 146
|
170 180 190
....*....|....*....|....*....|....*....
gi 1033140466 159 TEGIQPSVVAEIQERIVELTRQsGFSVLLVEQHLGFALR 197
Cdd:NF040873 147 TTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRR 184
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-214 |
1.15e-24 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 95.84 E-value: 1.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGYGRSR--VLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLapHERVARGMA 79
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL--EKALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 80 YVPQGqqcfPHLTAAenlrlvadarrdgavataealdlfpALRPLLRRRaglLSGGQRQQLAIARALITRPRLLMLDEPT 159
Cdd:cd03247 79 VLNQR----PYLFDT-------------------------TLRNNLGRR---FSGGERQRLALARILLQDAPIVLLDEPT 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1033140466 160 EGIQPSVVAEIQERIVELTRqsGFSVLLVEQHLGfALRVANRYHVLESGRVTSHG 214
Cdd:cd03247 127 VGLDPITERQLLSLIFEVLK--DKTLIWITHHLT-GIEHMDKILFLENGKIIMQG 178
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-210 |
1.19e-24 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 101.28 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVARGMAY 80
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 81 VPQGQQCFPHLTAAENLrLVADARRDGAVATAEALdlfpaLRPL-----LRRRAGLLSGGQRQQLAIARALITRPRLLML 155
Cdd:PRK15439 91 VPQEPLLFPNLSVKENI-LFGLPKRQASMQKMKQL-----LAALgcqldLDSSAGSLEVADRQIVEILRGLMRDSRILIL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1033140466 156 DEPTEGIQPSVVAEIQERIVELtRQSGFSVLLVEQHLGFALRVANRYHVLESGRV 210
Cdd:PRK15439 165 DEPTASLTPAETERLFSRIREL-LAQGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
17-210 |
2.25e-24 |
|
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: 95.94 E-value: 2.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 17 LHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRL----APHERVARGMAYvpQGQQCFPHLT 92
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgraIPYLRRKIGVVF--QDFRLLPDRN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 93 AAEN----LRLVADARRDGAVATAEALDLFpALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVA 168
Cdd:cd03292 95 VYENvafaLEVTGVPPREIRKRVPAALELV-GLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTW 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1033140466 169 EIQeRIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRV 210
Cdd:cd03292 174 EIM-NLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-192 |
2.83e-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: 2.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGY-GRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLaPHERVARGMAY 80
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSL-DQDEVRRRVSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 81 VPQGQQCFpHLTAAENLRLVA-DARRDGAVATAEALDLFPALRPL-------LRRRAGLLSGGQRQQLAIARALITRPRL 152
Cdd:TIGR02868 414 CAQDAHLF-DTTVRENLRLARpDATDEELWAALERVGLADWLRALpdgldtvLGEGGARLSGGERQRLALARALLADAPI 492
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1033140466 153 LMLDEPTEGIQPSVVAEIQERIVELTrqSGFSVLLVEQHL 192
Cdd:TIGR02868 493 LLLDEPTEHLDAETADELLEDLLAAL--SGRTVVLITHHL 530
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
7-214 |
6.03e-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: 95.48 E-value: 6.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 7 VHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDvtrlaPHER----VARGMAYVP 82
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLV-----PWKRrkkfLRRIGVVFG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 83 QGQQCFPHLTAAENLRLVAD----------ARRDGavaTAEALDLFPALRPLLRRraglLSGGQRQQLAIARALITRPRL 152
Cdd:cd03267 102 QKTQLWWDLPVIDSFYLLAAiydlpparfkKRLDE---LSELLDLEELLDTPVRQ----LSLGQRMRAEIAAALLHEPEI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1033140466 153 LMLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHG 214
Cdd:cd03267 175 LFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
4-214 |
1.49e-23 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 95.05 E-value: 1.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 4 LRG--VHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHErVARGMAYV 81
Cdd:PRK10253 8 LRGeqLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKE-VARRIGLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 82 PQGQQCFPHLTAAEnlrLVADA-----------RRDGAVATAEALDLfPALRPLLRRRAGLLSGGQRQQLAIARALITRP 150
Cdd:PRK10253 87 AQNATTPGDITVQE---LVARGryphqplftrwRKEDEEAVTKAMQA-TGITHLADQSVDTLSGGQRQRAWIAMVLAQET 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1033140466 151 RLLMLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHG 214
Cdd:PRK10253 163 AIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG 226
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-187 |
1.72e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 95.56 E-value: 1.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRlapheRVARGMAY 80
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP-----EDRRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 81 VPQGQQCFPHLTAAENL----RL----VADARRdgavATAEALDLFpALRPLLRRRAGLLSGGQRQQLAIARALITRPRL 152
Cdd:COG4152 76 LPEERGLYPKMKVGEQLvylaRLkglsKAEAKR----RADEWLERL-GLGDRANKKVEELSKGNQQKVQLIAALLHDPEL 150
|
170 180 190
....*....|....*....|....*....|....*
gi 1033140466 153 LMLDEPTEGIQPSVVAEIQERIVELtRQSGFSVLL 187
Cdd:COG4152 151 LILDEPFSGLDPVNVELLKDVIREL-AAKGTTVIF 184
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
20-215 |
2.04e-23 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 96.10 E-value: 2.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 20 VDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVEL------DGEDVTRLAPHERvarGMAYVPQGQQCFPHLTA 93
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLngrvlfDAEKGICLPPEKR---RIGYVFQDARLFPHYKV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 94 AENLRL-VADARRDGAVATAEALdlfpALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVAEIQE 172
Cdd:PRK11144 94 RGNLRYgMAKSMVAQFDKIVALL----GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1033140466 173 RIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGD 215
Cdd:PRK11144 170 YLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGP 212
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-201 |
4.34e-23 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 93.56 E-value: 4.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVaagL-----LRPSA---GTVELDGEDVtrLAPHER 73
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRC---LnrmndLIPGArveGEILLDGEDI--YDPDVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 74 VAR-----GMayVPQGQQCFPHlTAAEN----LRLVADARR---DGAVAtaEALdlfpalrpllrRRAGL---------- 131
Cdd:COG1117 87 VVElrrrvGM--VFQKPNPFPK-SIYDNvaygLRLHGIKSKselDEIVE--ESL-----------RKAALwdevkdrlkk 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1033140466 132 ----LSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVAEIQERIVELTRQsgFSVLLVEQHLGFALRVANR 201
Cdd:COG1117 151 salgLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD--YTIVIVTHNMQQAARVSDY 222
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
22-214 |
5.24e-23 |
|
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: 92.61 E-value: 5.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 22 LAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGedvtrlAPHERVARGMAYVPQGQQC---FP----HLTAA 94
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAG------ASPGKGWRHIGYVPQRHEFawdFPisvaHTVMS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 95 ENLRLVADARRDGA---VATAEALDLFpALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVAEIQ 171
Cdd:TIGR03771 75 GRTGHIGWLRRPCVadfAAVRDALRRV-GLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLT 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1033140466 172 ERIVELTrQSGFSVLLVEQHLGFALRVANRYhVLESGRVTSHG 214
Cdd:TIGR03771 154 ELFIELA-GAGTAILMTTHDLAQAMATCDRV-VLLNGRVIADG 194
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
6-228 |
9.42e-23 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 95.88 E-value: 9.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 6 GVHAGyGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPhERVARGMAYVPQGQ 85
Cdd:TIGR01842 324 IVPPG-GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDR-ETFGKHIGYLPQDV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 86 QCFPHlTAAENL-RLVADARRDGAVATAEALDLFPALRPL-------LRRRAGLLSGGQRQQLAIARALITRPRLLMLDE 157
Cdd:TIGR01842 402 ELFPG-TVAENIaRFGENADPEKIIEAAKLAGVHELILRLpdgydtvIGPGGATLSGGQRQRIALARALYGDPKLVVLDE 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1033140466 158 PTEGIQPSVVAEIQERIVELtRQSGFSVLLVEQHLGfALRVANRYHVLESGRVTSHGDGgvtaeREVRAAL 228
Cdd:TIGR01842 481 PNSNLDEEGEQALANAIKAL-KARGITVVVITHRPS-LLGCVDKILVLQDGRIARFGER-----DEVLAKL 544
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
8-201 |
1.19e-22 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 91.76 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 8 HAGYGRSR--VLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERV---ARGMAYVP 82
Cdd:PRK10584 15 SVGQGEHElsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAklrAKHVGFVF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 83 QGQQCFPHLTAAENLRLVADAR-------RDGAVATAEALDLFPALRPLlrrrAGLLSGGQRQQLAIARALITRPRLLML 155
Cdd:PRK10584 95 QSFMLIPTLNALENVELPALLRgessrqsRNGAKALLEQLGLGKRLDHL----PAQLSGGEQQRVALARAFNGRPDVLFA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1033140466 156 DEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANR 201
Cdd:PRK10584 171 DEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRR 216
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
12-210 |
1.24e-22 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 92.56 E-value: 1.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 12 GRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVA--RGMAYVPQG--QQC 87
Cdd:TIGR02769 22 QRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAfrRDVQLVFQDspSAV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 88 FPHLTAAENL--------RLVADARRDGAVATAEALDLFPALrplLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPT 159
Cdd:TIGR02769 102 NPRMTVRQIIgeplrhltSLDESEQKARIAELLDMVGLRSED---ADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAV 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1033140466 160 EGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRV 210
Cdd:TIGR02769 179 SNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-214 |
1.76e-22 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 91.91 E-value: 1.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGE-----DVTRLAPHER-- 73
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAERrr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 74 VARG-MAYVPQG--QQCFPHLTAAENL--RLVADARRDGAVATAEALDLF-----PALRplLRRRAGLLSGGQRQQLAIA 143
Cdd:PRK11701 86 LLRTeWGFVHQHprDGLRMQVSAGGNIgeRLMAVGARHYGDIRATAGDWLerveiDAAR--IDDLPTTFSGGMQQRLQIA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1033140466 144 RALITRPRLLMLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHG 214
Cdd:PRK11701 164 RNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-164 |
1.82e-22 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 95.19 E-value: 1.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 4 LRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVARGMAYVPQ 83
Cdd:NF033858 4 LEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCPRIAYMPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 84 --GQQCFPHLTAAENL----RLVADARRDGAVATAEALDlfpA--LRPLLRRRAGLLSGGQRQQLAIARALITRPRLLML 155
Cdd:NF033858 84 glGKNLYPTLSVFENLdffgRLFGQDAAERRRRIDELLR---AtgLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLIL 160
|
....*....
gi 1033140466 156 DEPTEGIQP 164
Cdd:NF033858 161 DEPTTGVDP 169
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
16-213 |
1.90e-22 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 91.42 E-value: 1.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 16 VLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVA---RGMAYVPQGQQCFPHLT 92
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAElrnQKLGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 93 AAENLR---LVADARRdgAVATAEALDLFPA--LRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVV 167
Cdd:PRK11629 104 ALENVAmplLIGKKKP--AEINSRALEMLAAvgLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1033140466 168 AEIQERIVELTRQSGFSVLLVEQHLGFALRVaNRYHVLESGRVTSH 213
Cdd:PRK11629 182 DSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTAE 226
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-224 |
1.91e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 92.60 E-value: 1.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGR-SRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGE--DVTRLAPHE-RVAR 76
Cdd:PRK13636 5 ILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKlRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 77 GMAYVPQGQQCFPHLT------AAENLRLVADA---RRDGAVATAealdlfpALRPLLRRRAGLLSGGQRQQLAIARALI 147
Cdd:PRK13636 85 GMVFQDPDNQLFSASVyqdvsfGAVNLKLPEDEvrkRVDNALKRT-------GIEHLKDKPTHCLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1033140466 148 TRPRLLMLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGD-GGVTAEREV 224
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNpKEVFAEKEM 235
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
29-214 |
2.30e-22 |
|
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: 95.08 E-value: 2.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 29 VAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVARGMAyvPQGQQCFPHLTAAENLRLVADAR---R 105
Cdd:TIGR01257 958 ITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMC--PQHNILFHHLTVAEHILFYAQLKgrsW 1035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 106 DGAVATAEALDLFPALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVAEIQERIveLTRQSGFSV 185
Cdd:TIGR01257 1036 EEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTI 1113
|
170 180
....*....|....*....|....*....
gi 1033140466 186 LLVEQHLGFALRVANRYHVLESGRVTSHG 214
Cdd:TIGR01257 1114 IMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-215 |
2.69e-22 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 91.57 E-value: 2.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHE--------- 72
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDgqlkvadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 73 --RVARG-MAYVPQGQQCFPHLTAAEN--------LRLVADARRDGAVATAEALDLFPALRpllRRRAGLLSGGQRQQLA 141
Cdd:PRK10619 86 qlRLLRTrLTMVFQHFNLWSHMTVLENvmeapiqvLGLSKQEARERAVKYLAKVGIDERAQ---GKYPVHLSGGQQQRVS 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1033140466 142 IARALITRPRLLMLDEPTEGIQPSVVAEIQeRIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGD 215
Cdd:PRK10619 163 IARALAMEPEVLLFDEPTSALDPELVGEVL-RIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGA 235
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
3-214 |
3.52e-22 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 93.17 E-value: 3.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 3 TLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERvarGMAYVP 82
Cdd:PRK11000 5 TLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAER---GVGMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 83 QGQQCFPHLTAAEN----LRL--VADARRDGAV-ATAEALDLfpalRPLLRRRAGLLSGGQRQQLAIARALITRPRLLML 155
Cdd:PRK11000 82 QSYALYPHLSVAENmsfgLKLagAKKEEINQRVnQVAEVLQL----AHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1033140466 156 DEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHG 214
Cdd:PRK11000 158 DEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-192 |
4.50e-22 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 90.94 E-value: 4.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVEldgedvtrlapHERVARgMAY 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-----------RNGKLR-IGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 81 VPQGQQCFPH--LTAAENLRLVADARRDgavataealDLFPALR-----PLLRRRAGLLSGGQRQQLAIARALITRPRLL 153
Cdd:PRK09544 72 VPQKLYLDTTlpLTVNRFLRLRPGTKKE---------DILPALKrvqagHLIDAPMQKLSGGETQRVLLARALLNRPQLL 142
|
170 180 190
....*....|....*....|....*....|....*....
gi 1033140466 154 MLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHL 192
Cdd:PRK09544 143 VLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDL 181
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
16-193 |
6.19e-22 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 89.47 E-value: 6.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 16 VLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPheRVARGMAYVPQGQQCFPHLTAAE 95
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD--SIARGLLYLGHAPGIKTTLSVLE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 96 NLRLVADARRDGAVAtaEALDLFpALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVAEIQERIV 175
Cdd:cd03231 93 NLRFWHADHSDEQVE--EALARV-GLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMA 169
|
170
....*....|....*...
gi 1033140466 176 ELTRQSGFSVLLVEQHLG 193
Cdd:cd03231 170 GHCARGGMVVLTTHQDLG 187
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
32-211 |
1.25e-21 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 92.37 E-value: 1.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 32 VLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVARGMAYVPQ---GQQCFPHLTAAENLRLVADA----- 103
Cdd:PRK10762 283 VSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIVYISEdrkRDGLVLGMSVKENMSLTALRyfsra 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 104 -----RRDGAVATAEALDLFPALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVAEIQERIVELt 178
Cdd:PRK10762 363 ggslkHADEQQAVSDFIRLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQF- 441
|
170 180 190
....*....|....*....|....*....|...
gi 1033140466 179 RQSGFSVLLVEQHLGFALRVANRYHVLESGRVT 211
Cdd:PRK10762 442 KAEGLSIILVSSEMPEVLGMSDRILVMHEGRIS 474
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
8-214 |
1.61e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 89.86 E-value: 1.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 8 HAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHE-RVARGMAYVPQGQQ 86
Cdd:PRK13652 11 YSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREvRKFVGLVFQNPDDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 87 CFPHLTAAE------NLRLVADARrdgAVATAEALDLFpALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTE 160
Cdd:PRK13652 91 IFSPTVEQDiafgpiNLGLDEETV---AHRVSSALHML-GLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1033140466 161 GIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHG 214
Cdd:PRK13652 167 GLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYG 220
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-201 |
2.46e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 89.06 E-value: 2.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVA--AGLLRPS---AGTVELDGEDVtrLAPHE--- 72
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNI--YSPRTdtv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 73 --RVARGMAYvpQGQQCFPhLTAAEN----LRL--VAD-ARRDGAVATA-EALDLFPALRPLLRRRAGLLSGGQRQQLAI 142
Cdd:PRK14239 83 dlRKEIGMVF--QQPNPFP-MSIYENvvygLRLkgIKDkQVLDEAVEKSlKGASIWDEVKDRLHDSALGLSGGQQQRVCI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1033140466 143 ARALITRPRLLMLDEPTEGIQPSVVAEIQERIVELTRQsgFSVLLVEQHLGFALRVANR 201
Cdd:PRK14239 160 ARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD--YTMLLVTRSMQQASRISDR 216
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-214 |
2.65e-21 |
|
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: 88.31 E-value: 2.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGYG--RSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPhERVARGMA 79
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADP-AWLRRQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 80 YVPQGQQCFpHLTAAENLRLV---ADARRDGAVAT-AEALDLFPALR----PLLRRRAGLLSGGQRQQLAIARALITRPR 151
Cdd:cd03252 80 VVLQENVLF-NRSIRDNIALAdpgMSMERVIEAAKlAGAHDFISELPegydTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1033140466 152 LLMLDEPTEGIQPSVVAEIQERIVELTrqSGFSVLLVEQHLGfALRVANRYHVLESGRVTSHG 214
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDIC--AGRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQG 218
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-188 |
2.82e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 88.60 E-value: 2.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVargmay 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGV------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 81 VPQGQQCFPHLTAAEN----LRLVADARRDGAVATAEALDLFpALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLD 156
Cdd:PRK11248 75 VFQNEGLLPWRNVQDNvafgLQLAGVEKMQRLEIAHQMLKKV-GLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLD 153
|
170 180 190
....*....|....*....|....*....|..
gi 1033140466 157 EPTEGIQPSVVAEIQERIVELTRQSGFSVLLV 188
Cdd:PRK11248 154 EPFGALDAFTREQMQTLLLKLWQETGKQVLLI 185
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-188 |
3.62e-21 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 87.85 E-value: 3.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHervargmAY 80
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPE-------IY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 81 VPQGQQCF--PHL---TAAENLRLVADARRDGAVATAEALDL--FPALRPLLRRRAGLLSGGQRQQLAIARALITRPRLL 153
Cdd:PRK10247 80 RQQVSYCAqtPTLfgdTVYDNLIFPWQIRNQQPDPAIFLDDLerFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVL 159
|
170 180 190
....*....|....*....|....*....|....*
gi 1033140466 154 MLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLV 188
Cdd:PRK10247 160 LLDEITSALDESNKHNVNEIIHRYVREQNIAVLWV 194
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
14-214 |
3.87e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 89.02 E-value: 3.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 14 SRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHER---VARGMAYVPQgqqcFPH 90
Cdd:PRK13643 19 SRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEikpVRKKVGVVFQ----FPE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 91 LTAAEN--LRLVADARRDGAVA-------TAEALDLFPALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEG 161
Cdd:PRK13643 95 SQLFEEtvLKDVAFGPQNFGIPkekaekiAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1033140466 162 IQPSVVAEIQeRIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHG 214
Cdd:PRK13643 175 LDPKARIEMM-QLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCG 226
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
19-159 |
4.30e-21 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 89.41 E-value: 4.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 19 GVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVA--RGMAYVpqgqqcF-------- 88
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPlrRRMQMV------Fqdpyasln 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1033140466 89 PHLTAAENL-------RLVADARRDGAVAtaEALDLFpALRP-LLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPT 159
Cdd:COG4608 110 PRMTVGDIIaeplrihGLASKAERRERVA--ELLELV-GLRPeHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPV 185
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
16-209 |
6.30e-21 |
|
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: 87.10 E-value: 6.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 16 VLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGE----DVTRLAPHERVA---RGMAYVPQGQQCF 88
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQASPREILAlrrRTIGYVSQFLRVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 89 PHLTAaenLRLVADARRDGAVATAEALD----LFPALRpLLRRRAGL----LSGGQRQQLAIARALITRPRLLMLDEPTE 160
Cdd:COG4778 106 PRVSA---LDVVAEPLLERGVDREEARArareLLARLN-LPERLWDLppatFSGGEQQRVNIARGFIADPPLLLLDEPTA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1033140466 161 GIQPSVVAEIQERIVELtRQSGFSVLLVEQHLGFALRVANRYHVLESGR 209
Cdd:COG4778 182 SLDAANRAVVVELIEEA-KARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
16-214 |
9.79e-21 |
|
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: 87.49 E-value: 9.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 16 VLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDV----TRLAPHERVarGMayV---PQGQqcf 88
Cdd:TIGR04520 17 ALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTldeeNLWEIRKKV--GM--VfqnPDNQ--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 89 phLTAA----------ENLRLVAD--ARRdgavaTAEALDLFpALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLD 156
Cdd:TIGR04520 90 --FVGAtveddvafglENLGVPREemRKR-----VDEALKLV-GMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1033140466 157 EPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRvANRYHVLESGRVTSHG 214
Cdd:TIGR04520 162 EATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEG 218
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-217 |
1.10e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 87.76 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGE--DVTR---LAPHERVA 75
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKrglLALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 76 rgMAYVPQGQQCF---PHLTAAENLRLVADARRDGAVATAEALDLFPALRpLLRRRAGLLSGGQRQQLAIARALITRPRL 152
Cdd:PRK13638 81 --TVFQDPEQQIFytdIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQH-FRHQPIQCLSHGQKKRVAIAGALVLQARY 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1033140466 153 LMLDEPTEGIQPSVVAE---IQERIVeltrQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGDGG 217
Cdd:PRK13638 158 LLLDEPTAGLDPAGRTQmiaIIRRIV----AQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPG 221
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
16-214 |
1.70e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 87.07 E-value: 1.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 16 VLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDvTRLAPHE---RVARGMAYV-PQGQqcfphL 91
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLD-TSDEENLwdiRNKAGMVFQnPDNQ-----I 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 92 TAA----------ENLRLVADARRDGAVATAEALDLFPalrplLRRRA-GLLSGGQRQQLAIARALITRPRLLMLDEPTE 160
Cdd:PRK13633 99 VATiveedvafgpENLGIPPEEIRERVDESLKKVGMYE-----YRRHApHLLSGGQKQRVAIAGILAMRPECIIFDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1033140466 161 GIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRvANRYHVLESGRVTSHG 214
Cdd:PRK13633 174 MLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEG 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-159 |
2.07e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 88.97 E-value: 2.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 4 LRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVeldgedvtRLAPHERVargmAYVPQ 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV--------SIPKGLRI----GYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 84 GQQCFPHLTAAENLrLVADARRDGAVAT------------------AEALDLFPAL-------------------RPLLR 126
Cdd:COG0488 69 EPPLDDDLTVLDTV-LDGDAELRALEAEleeleaklaepdedlerlAELQEEFEALggweaearaeeilsglgfpEEDLD 147
|
170 180 190
....*....|....*....|....*....|...
gi 1033140466 127 RRAGLLSGGQRQQLAIARALITRPRLLMLDEPT 159
Cdd:COG0488 148 RPVSELSGGWRRRVALARALLSEPDLLLLDEPT 180
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
12-215 |
2.23e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 86.77 E-value: 2.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 12 GRSrVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLApHERVARGMAYVPQgqqcfpHL 91
Cdd:PRK10575 23 GRT-LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWS-SKAFARKVAYLPQ------QL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 92 TAAENL---RLVADAR--------RDGAV---ATAEALDLFpALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDE 157
Cdd:PRK10575 95 PAAEGMtvrELVAIGRypwhgalgRFGAAdreKVEEAISLV-GLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1033140466 158 PTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGD 215
Cdd:PRK10575 174 PTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGT 231
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-195 |
2.26e-20 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 85.24 E-value: 2.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAphERVARGMAY 80
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQR--DEYHQDLLY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 81 VpqGQQ--CFPHLTAAENLR-LVADARRDGAVATAEALDLFPalrplLRRR----AGLLSGGQRQQLAIARALITRPRLL 153
Cdd:PRK13538 79 L--GHQpgIKTELTALENLRfYQRLHGPGDDEALWEALAQVG-----LAGFedvpVRQLSAGQQRRVALARLWLTRAPLW 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1033140466 154 MLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFA 195
Cdd:PRK13538 152 ILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTHQDLPVA 193
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
15-214 |
2.66e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 86.61 E-value: 2.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 15 RVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELdGEDV-------TRLAP----------------- 70
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVitagkknKKLKPlrkkvgivfqfpehqlf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 71 HERVARGMAYVPQgqqcfpHLTAAEnlrlvADARRdgavATAEALDLFPALRPLLRRRAGLLSGGQRQQLAIARALITRP 150
Cdd:PRK13634 100 EETVEKDICFGPM------NFGVSE-----EDAKQ----KAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1033140466 151 RLLMLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHG 214
Cdd:PRK13634 165 EVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQG 228
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
14-214 |
2.79e-20 |
|
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: 85.16 E-value: 2.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 14 SRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLaPHERVARGMAYVPQGQQCFPHlTA 93
Cdd:cd03369 21 PPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTI-PLEDLRSSLTIIPQDPTLFSG-TI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 94 AENLRlVADARRDgavataeaLDLFPALRPllrRRAGL-LSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVAEIQE 172
Cdd:cd03369 99 RSNLD-PFDEYSD--------EEIYGALRV---SEGGLnLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQK 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1033140466 173 RIVELTrqSGFSVLLVEQHLGFALRVAnRYHVLESGRVTSHG 214
Cdd:cd03369 167 TIREEF--TNSTILTIAHRLRTIIDYD-KILVMDAGEVKEYD 205
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
4-215 |
3.27e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 85.52 E-value: 3.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 4 LRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGedvtRLAPheRVARGMAYVPQ 83
Cdd:COG1134 29 LRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG----RVSA--LLELGAGFHPE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 84 gqqcfphLTAAENLRLVA----------DARRDGAVATAE---ALDLfpalrPLlrrraGLLSGGQRQQLAIARALITRP 150
Cdd:COG1134 103 -------LTGRENIYLNGrllglsrkeiDEKFDEIVEFAElgdFIDQ-----PV-----KTYSSGMRARLAFAVATAVDP 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 151 RLLMLDEPTegiqpSVV-AEIQE----RIVELtRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGD 215
Cdd:COG1134 166 DILLVDEVL-----AVGdAAFQKkclaRIREL-RESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGD 229
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-218 |
3.31e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 88.30 E-value: 3.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVARGMAY 80
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 81 VPQGQQCFPHLTAAENL---RL---------VADARRDGAVatAEALDLFPALRPLLRRRAGLLSGGQRQQLAIARALIT 148
Cdd:PRK09700 85 IYQELSVIDELTVLENLyigRHltkkvcgvnIIDWREMRVR--AAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 149 RPRLLMLDEPTEGIQPSVVAEIQERIVELtRQSGFSVLLVEQHLGFALRVANRYHVLESGrvTSHGDGGV 218
Cdd:PRK09700 163 DAKVIIMDEPTSSLTNKEVDYLFLIMNQL-RKEGTAIVYISHKLAEIRRICDRYTVMKDG--SSVCSGMV 229
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-204 |
3.49e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 84.62 E-value: 3.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRlaphERVARgmay 80
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK----DLCTY---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 81 vpQGQQCF--------PHLTAAENLrLVADARRDGAVATAEALDLFpALRPLLRRRAGLLSGGQRQQLAIARALITRPRL 152
Cdd:PRK13540 73 --QKQLCFvghrsginPYLTLRENC-LYDIHFSPGAVGITELCRLF-SLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1033140466 153 LMLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHV 204
Cdd:PRK13540 149 WLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQDLPLNKADYEEYHL 200
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-179 |
3.83e-20 |
|
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: 85.36 E-value: 3.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGYGRSR-VLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVaagLLR---PSAGTVELDGEDVTRLAPHErVARG 77
Cdd:cd03253 1 IEFENVTFAYDPGRpVLKDVSFTIPAGKKVAIVGPSGSGKSTILRL---LFRfydVSSGSILIDGQDIREVTLDS-LRRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 78 MAYVPQGQQCFpHLTAAENLRL-VADARRDGAVATAEALDL------FP-ALRPLLRRRAGLLSGGQRQQLAIARALITR 149
Cdd:cd03253 77 IGVVPQDTVLF-NDTIGYNIRYgRPDATDEEVIEAAKAAQIhdkimrFPdGYDTIVGERGLKLSGGEKQRVAIARAILKN 155
|
170 180 190
....*....|....*....|....*....|
gi 1033140466 150 PRLLMLDEPTEGIQPSVVAEIQERIVELTR 179
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAALRDVSK 185
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
12-215 |
3.96e-20 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 88.32 E-value: 3.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 12 GRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVEL----DGEDVTRLAPHE--RVARGMAYVPQGQ 85
Cdd:TIGR03269 295 GVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPDGrgRAKRYIGILHQEY 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 86 QCFPHLTAAENL------RLVADARRDGAVATAEALDLF-PALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEP 158
Cdd:TIGR03269 375 DLYPHRTVLDNLteaiglELPDELARMKAVITLKMVGFDeEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEP 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1033140466 159 TEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGD 215
Cdd:TIGR03269 455 TGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGD 511
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
6-210 |
4.89e-20 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 85.89 E-value: 4.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 6 GVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVA--RGMAYVPQ 83
Cdd:PRK10419 17 GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAfrRDIQMVFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 84 GQ--QCFPHLTA----AENLRLVADARRDGAVATAEALDLFPALRP-LLRRRAGLLSGGQRQQLAIARALITRPRLLMLD 156
Cdd:PRK10419 97 DSisAVNPRKTVreiiREPLRHLLSLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1033140466 157 EPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRV 210
Cdd:PRK10419 177 EAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
15-187 |
9.03e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 85.91 E-value: 9.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 15 RVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDvtrlaPHER---VARGMAYV-PQGQQCFPH 90
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV-----PFKRrkeFARRIGVVfGQRSQLWWD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 91 LTAAENLRL------VADARRDGAVAT-AEALDlfpaLRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQ 163
Cdd:COG4586 111 LPAIDSFRLlkaiyrIPDAEYKKRLDElVELLD----LGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLD 186
|
170 180
....*....|....*....|....
gi 1033140466 164 PSVVAEIQERIVELTRQSGFSVLL 187
Cdd:COG4586 187 VVSKEAIREFLKEYNRERGTTILL 210
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
8-214 |
1.29e-19 |
|
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: 83.74 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 8 HAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLApherVARGMAyvpqgqqc 87
Cdd:cd03220 29 KGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLG----LGGGFN-------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 88 fPHLTAAENLRLVA----------DARRDGAVATAE---ALDLfpalrPLLRrraglLSGGQRQQLAIARALITRPRLLM 154
Cdd:cd03220 97 -PELTGRENIYLNGrllglsrkeiDEKIDEIIEFSElgdFIDL-----PVKT-----YSSGMKARLAFAIATALEPDILL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 155 LDEPTEGIQPSVVAEIQERIVELTRQSGfSVLLVEQHLGFALRVANRYHVLESGRVTSHG 214
Cdd:cd03220 166 IDEVLAVGDAAFQEKCQRRLRELLKQGK-TVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-226 |
1.29e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 86.50 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVARGMAYV 81
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGVAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 82 PQGQQCFPHLTAAENLRL--------VADARRDGAVATAE----ALDLFPALRplLRRraglLSGGQRQQLAIARALITR 149
Cdd:PRK11288 85 YQELHLVPEMTVAENLYLgqlphkggIVNRRLLNYEAREQlehlGVDIDPDTP--LKY----LSIGQRQMVEIAKALARN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 150 PRLLMLDEPTEGIQpsvVAEIQE--RIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGR-VTSHGDG-GVTAEREVR 225
Cdd:PRK11288 159 ARVIAFDEPTSSLS---AREIEQlfRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRyVATFDDMaQVDRDQLVQ 235
|
.
gi 1033140466 226 A 226
Cdd:PRK11288 236 A 236
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-214 |
1.47e-19 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 84.49 E-value: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSA--------GTVELDGEDVTRLAPhE 72
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGEPLAAIDA-P 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 73 RVARGMAYVPQGQQ--------------CFPHLTAAEnlrlvADARRDGAVATAeALDLFPAlRPLLRRRAGLLSGGQRQ 138
Cdd:PRK13547 80 RLARLRAVLPQAAQpafafsareivllgRYPHARRAG-----ALTHRDGEIAWQ-ALALAGA-TALVGRDVTTLSGGELA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 139 QLAIARAL---------ITRPRLLMLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGR 209
Cdd:PRK13547 153 RVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGA 232
|
....*
gi 1033140466 210 VTSHG 214
Cdd:PRK13547 233 IVAHG 237
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
15-179 |
2.21e-19 |
|
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: 83.09 E-value: 2.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 15 RVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSA---GTVELDGEDVTRlaphERVARGMAYVPQGQQCFPHL 91
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKP----DQFQKCVAYVRQDDILLPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 92 TAAENL---------RLVADARRDGAVATAEALDLfpALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGI 162
Cdd:cd03234 97 TVRETLtytailrlpRKSSDAIRKKRVEDVLLRDL--ALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170
....*....|....*..
gi 1033140466 163 QPSVVAEIQERIVELTR 179
Cdd:cd03234 175 DSFTALNLVSTLSQLAR 191
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
17-214 |
2.96e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 83.91 E-value: 2.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 17 LHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHE-RVARGMAYV-PQGQqcFPHLTAA 94
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDvRRQVGMVFQnPDNQ--FVGATVQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 95 ENLRLVADAR---RDGAVATA-EALDLFpALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVAEI 170
Cdd:PRK13635 101 DDVAFGLENIgvpREEMVERVdQALRQV-GMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREV 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1033140466 171 QERIVELTRQSGFSVLLVEQHLGFALRvANRYHVLESGRVTSHG 214
Cdd:PRK13635 180 LETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEG 222
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-216 |
3.25e-19 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 82.62 E-value: 3.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGY-GRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRL----APHERVA 75
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLknreVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 76 RGMAYvpQGQQCFPHLTAAEN----LRLVADARRDGAVATAEALDLFpALRPLLRRRAGLLSGGQRQQLAIARALITRPR 151
Cdd:PRK10908 81 IGMIF--QDHHLLMDRTVYDNvaipLIIAGASGDDIRRRVSAALDKV-GLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1033140466 152 LLMLDEPTEGIQPSVVAEIQeRIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGDG 216
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGIL-RLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGVGG 221
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
15-215 |
3.30e-19 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 85.51 E-value: 3.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 15 RVLHGVDLAVPPDGVAAVLGHNGAGKSTLlrvAAGLLR--PSAGTVELDGEDVTRLAPHER------------------- 73
Cdd:COG4172 300 KAVDGVSLTLRRGETLGLVGESGSGKSTL---GLALLRliPSEGEIRFDGQDLDGLSRRALrplrrrmqvvfqdpfgsls 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 74 --------VARGMAYVpqgqqcFPHLTAAENLRLVADARRDgaVA-TAEALDLFPAlrpllrrragLLSGGQRQQLAIAR 144
Cdd:COG4172 377 prmtvgqiIAEGLRVH------GPGLSAAERRARVAEALEE--VGlDPAARHRYPH----------EFSGGQRQRIAIAR 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1033140466 145 ALITRPRLLMLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGD 215
Cdd:COG4172 439 ALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGP 509
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-215 |
3.98e-19 |
|
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: 82.66 E-value: 3.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGYG--RSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHErVARGMA 79
Cdd:cd03251 1 VEFKNVTFRYPgdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLAS-LRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 80 YVPQGQQCFpHLTAAENLRL----VADARRDGAVATAEALDL---FP-ALRPLLRRRAGLLSGGQRQQLAIARALITRPR 151
Cdd:cd03251 80 LVSQDVFLF-NDTVAENIAYgrpgATREEVEEAARAANAHEFimeLPeGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1033140466 152 LLMLDEPTEGIQPSVVAEIQERIVELTRqsGFSVLLVEQHLGfALRVANRYHVLESGRVTSHGD 215
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLS-TIENADRIVVLEDGKIVERGT 219
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-214 |
7.39e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 82.40 E-value: 7.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 16 VLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGE------DVTRL-APHERVARGMAYvpQGQQCF 88
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIdAIKLRKEVGMVF--QQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 89 PHLTAAENLRL------VADARRDGAVA--TAEALDLFPALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTE 160
Cdd:PRK14246 103 PHLSIYDNIAYplkshgIKEKREIKKIVeeCLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1033140466 161 GIQPSVVAEIQERIVELTRQsgFSVLLVEQHLGFALRVANRYHVLESGRVTSHG 214
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWG 234
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-214 |
1.24e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 83.35 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHErVARGMAY 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARA-ASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 81 VPQGQQC--------------FPHLTAAENLRLVADARRDGAVATAEAlDLFpALRPLLRrraglLSGGQRQQLAIARAL 146
Cdd:PRK09536 82 VPQDTSLsfefdvrqvvemgrTPHRSRFDTWTETDRAAVERAMERTGV-AQF-ADRPVTS-----LSGGERQRVLLARAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1033140466 147 ITRPRLLMLDEPTegiqPSVVAEIQERIVELTR---QSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHG 214
Cdd:PRK09536 155 AQATPVLLLDEPT----ASLDINHQVRTLELVRrlvDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
14-210 |
1.27e-18 |
|
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: 80.98 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 14 SRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTrLAPHERVARGMAYVPQGQQCFPHlTA 93
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIS-QYEHKYLHSKVSLVGQEPVLFAR-SL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 94 AEN----LRLVADARRDGAVATAEALDLFPALRPLLRRRAG----LLSGGQRQQLAIARALITRPRLLMLDEPTEgiqpS 165
Cdd:cd03248 105 QDNiaygLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGekgsQLSGGQKQRVAIARALIRNPQVLILDEATS----A 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1033140466 166 VVAEIQERIVELTRQ--SGFSVLLVEQHLGFALRvANRYHVLESGRV 210
Cdd:cd03248 181 LDAESEQQVQQALYDwpERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
11-214 |
1.29e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 81.98 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 11 YGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLL---RPSAGTVELDGEDVT---RLAPHERVARG-MAYVPQ 83
Cdd:PRK09984 14 FNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQregRLARDIRKSRAnTGYIFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 84 GQQCFPHLTAAENLRLvadarrdGAVATA----EALDLFP------ALRPLLR--------RRAGLLSGGQRQQLAIARA 145
Cdd:PRK09984 94 QFNLVNRLSVLENVLI-------GALGSTpfwrTCFSWFTreqkqrALQALTRvgmvhfahQRVSTLSGGQQQRVAIARA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1033140466 146 LITRPRLLMLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHG 214
Cdd:PRK09984 167 LMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDG 235
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
8-215 |
1.51e-18 |
|
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: 83.58 E-value: 1.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 8 HAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKS----TLLRVAAGLLRPSAGTVELDGEDVTRLAPHE-RVARG--MAY 80
Cdd:COG4172 17 GQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERElRRIRGnrIAM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 81 VPQ------------GQQcfphltAAENLRLVADARRdgAVATAEALDLF-----PALRPLLRRRAGLLSGGQRQQLAIA 143
Cdd:COG4172 97 IFQepmtslnplhtiGKQ------IAEVLRLHRGLSG--AAARARALELLervgiPDPERRLDAYPHQLSGGQRQRVMIA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1033140466 144 RALITRPRLLMLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGD 215
Cdd:COG4172 169 MALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGP 240
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-200 |
1.60e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 81.62 E-value: 1.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 11 YGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVaagLLRPSA--------GTVELDGEDV-TRLAPHERVARGMAYV 81
Cdd:PRK14258 17 YDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKC---LNRMNElesevrveGRVEFFNQNIyERRVNLNRLRRQVSMV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 82 PQGQQCFP---HLTAAENLRLVA---DARRDGAVATA-EALDLFPALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLM 154
Cdd:PRK14258 94 HPKPNLFPmsvYDNVAYGVKIVGwrpKLEIDDIVESAlKDADLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1033140466 155 LDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVAN 200
Cdd:PRK14258 174 MDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
5-215 |
1.74e-18 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 82.32 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 5 RGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVA--RGMAYVP 82
Cdd:PRK11308 19 RGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLlrQKIQIVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 83 Q------------GQQCFPHLtaAENLRLVADARRDGAVATAEALdlfpALRP-LLRRRAGLLSGGQRQQLAIARALITR 149
Cdd:PRK11308 99 QnpygslnprkkvGQILEEPL--LINTSLSAAERREKALAMMAKV----GLRPeHYDRYPHMFSGGQRQRIAIARALMLD 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1033140466 150 PRLLMLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGD 215
Cdd:PRK11308 173 PDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGT 238
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
14-214 |
1.92e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 81.71 E-value: 1.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 14 SRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHE---RVARGMAYVPQgqqcFP- 89
Cdd:PRK13649 20 GRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdikQIRKKVGLVFQ----FPe 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 90 -HLTAAENLRLVADARRDGAVATAEA-------LDLFPALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEG 161
Cdd:PRK13649 96 sQLFEETVLKDVAFGPQNFGVSQEEAealarekLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1033140466 162 IQPSVVAEIQERIVELtRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHG 214
Cdd:PRK13649 176 LDPKGRKELMTLFKKL-HQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSG 227
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
12-214 |
2.77e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 82.39 E-value: 2.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 12 GRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHE-RVAR--GMAYVPQGQQCF 88
Cdd:PRK10070 39 GLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElREVRrkKIAMVFQSFALM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 89 PHLTAAENlrlVADARRDGAVATAEALDlfPALRPLlrRRAGL----------LSGGQRQQLAIARALITRPRLLMLDEP 158
Cdd:PRK10070 119 PHMTVLDN---TAFGMELAGINAEERRE--KALDAL--RQVGLenyahsypdeLSGGMRQRVGLARALAINPDILLMDEA 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1033140466 159 TEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHG 214
Cdd:PRK10070 192 FSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVG 247
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
14-210 |
5.65e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 80.48 E-value: 5.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 14 SRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVT----RLA------------PH-----E 72
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkkvKLSdirkkvglvfqyPEyqlfeE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 73 RVARGMAYVPQgqqcfphltaaeNLRLVADARRDGAVATAEALDLfpALRPLLRRRAGLLSGGQRQQLAIARALITRPRL 152
Cdd:PRK13637 100 TIEKDIAFGPI------------NLGLSEEEIENRVKRAMNIVGL--DYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKI 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1033140466 153 LMLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRV 210
Cdd:PRK13637 166 LILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKC 223
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
12-162 |
9.26e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 81.63 E-value: 9.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 12 GRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPS---AGTVELDGEDVTRLAPHERVArgmaYVPQGQQCF 88
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRAISA----YVQQDDLFI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 89 PHLTAAENL------RLVADARRDGAVATAEALDLFPALRPLLRRRAGL------LSGGQRQQLAIARALITRPRLLMLD 156
Cdd:TIGR00955 112 PTLTVREHLmfqahlRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCD 191
|
....*.
gi 1033140466 157 EPTEGI 162
Cdd:TIGR00955 192 EPTSGL 197
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-214 |
1.28e-17 |
|
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: 80.92 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGY-GRSR-VLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHErVARGMA 79
Cdd:TIGR02203 331 VEFRNVTFRYpGRDRpALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLAS-LRRQVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 80 YVPQGQQCFPHlTAAENLRL-----VADARRDGAVATAEALDLFPALrPL-----LRRRAGLLSGGQRQQLAIARALITR 149
Cdd:TIGR02203 410 LVSQDVVLFND-TIANNIAYgrteqADRAEIERALAAAYAQDFVDKL-PLgldtpIGENGVLLSGGQRQRLAIARALLKD 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1033140466 150 PRLLMLDEPTEGIQPSVVAEIQERIVELtrQSGFSVLLVEQHLGfALRVANRYHVLESGRVTSHG 214
Cdd:TIGR02203 488 APILILDEATSALDNESERLVQAALERL--MQGRTTLVIAHRLS-TIEKADRIVVMDDGRIVERG 549
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-179 |
1.80e-17 |
|
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: 80.63 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGYGRSR-VLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHE-RVARGMa 79
Cdd:COG5265 358 VRFENVSFGYDPERpILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASlRAAIGI- 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 80 yVPQGQQCFpHLTAAENLRL-VADARRDGAVATAEA--LDLFPALRP-----LLRRRaGL-LSGGQRQQLAIARALITRP 150
Cdd:COG5265 437 -VPQDTVLF-NDTIAYNIAYgRPDASEEEVEAAARAaqIHDFIESLPdgydtRVGER-GLkLSGGEKQRVAIARTLLKNP 513
|
170 180
....*....|....*....|....*....
gi 1033140466 151 RLLMLDEPTEGIQPSVVAEIQERIVELTR 179
Cdd:COG5265 514 PILIFDEATSALDSRTERAIQAALREVAR 542
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
16-214 |
2.27e-17 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 80.54 E-value: 2.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 16 VLHGVDLAVPPDGVAAVLGHNGAGKSTllrVAAGLLR---PSAGTVELDGEDVTRLApHERVARGMAYVPQGQQCFPHlT 92
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKST---VAALLQNlyqPTGGQVLLDGVPLVQYD-HHYLHRQVALVGQEPVLFSG-S 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 93 AAEN----LRLVADARRDGAVATAEALDLFPALRPLLRRRAG----LLSGGQRQQLAIARALITRPRLLMLDEPTEGIQp 164
Cdd:TIGR00958 571 VRENiaygLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGekgsQLSGGQKQRIAIARALVRKPRVLILDEATSALD- 649
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1033140466 165 svvAEIQERIVELTRQSGFSVLLVEQHLGFALRvANRYHVLESGRVTSHG 214
Cdd:TIGR00958 650 ---AECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMG 695
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-159 |
3.11e-17 |
|
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: 75.18 E-value: 3.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELdGEDVTrlaphervargMAYV 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-GSTVK-----------IGYF 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1033140466 82 PQgqqcfphltaaenlrlvadarrdgavataealdlfpalrpllrrraglLSGGQRQQLAIARALITRPRLLMLDEPT 159
Cdd:cd03221 69 EQ------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPT 98
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-215 |
4.96e-17 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 77.50 E-value: 4.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHE--RVARGM 78
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRlyTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 79 AYVPQGQQCFPHLTAAENL--------RLVADARRDGAVATAEALDLFPA--LRPllrrraGLLSGGQRQQLAIARALIT 148
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVayplrehtQLPAPLLHSTVMMKLEAVGLRGAakLMP------SELSGGMARRAALARAIAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1033140466 149 RPRLLMLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGD 215
Cdd:PRK11831 161 EPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGS 227
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-215 |
6.45e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 79.10 E-value: 6.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGY--GRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLapHERVAR-GM 78
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADY--SEAALRqAI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 79 AYVPQGQQCFPHlTAAENLRLVADARRDGAVAtaEALDLFpALRPLLRRRAGL----------LSGGQRQQLAIARALIT 148
Cdd:PRK11160 417 SVVSQRVHLFSA-TLRDNLLLAAPNASDEALI--EVLQQV-GLEKLLEDDKGLnawlgeggrqLSGGEQRRLGIARALLH 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1033140466 149 RPRLLMLDEPTEGIQpsvvAEIQERIVELTRQ--SGFSVLLVEQHLgFALRVANRYHVLESGRVTSHGD 215
Cdd:PRK11160 493 DAPLLLLDEPTEGLD----AETERQILELLAEhaQNKTVLMITHRL-TGLEQFDRICVMDNGQIIEQGT 556
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-160 |
7.01e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 78.89 E-value: 7.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVARGMAY 80
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGIGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 81 VPQGQQCFPHLTAAENLRL-----VADARRDGAVATAEALDLFPAL--RPLLRRRAGLLSGGQRQQLAIARALITRPRLL 153
Cdd:PRK10762 84 IHQELNLIPQLTIAENIFLgrefvNRFGRIDWKKMYAEADKLLARLnlRFSSDKLVGELSIGEQQMVEIAKVLSFESKVI 163
|
....*..
gi 1033140466 154 MLDEPTE 160
Cdd:PRK10762 164 IMDEPTD 170
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
14-227 |
8.18e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 77.08 E-value: 8.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 14 SRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTrlAPHERVARGM--------------- 78
Cdd:PRK13647 18 TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN--AENEKWVRSKvglvfqdpddqvfss 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 79 ------AYVPQGQQcfphLTAAENLRLVADARRdgAVATAEaldlfpalrplLRRRAGL-LSGGQRQQLAIARALITRPR 151
Cdd:PRK13647 96 tvwddvAFGPVNMG----LDKDEVERRVEEALK--AVRMWD-----------FRDKPPYhLSYGQKKRVAIAGVLAMDPD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1033140466 152 LLMLDEPTEGIQPSVVAEIQERIVELTRQsGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGDGGVTAEREVRAA 227
Cdd:PRK13647 159 VIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIVEQ 233
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
10-214 |
8.29e-17 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 78.63 E-value: 8.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 10 GYGrSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHErVARGMAYVPQGQQCFP 89
Cdd:TIGR01193 484 GYG-SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHT-LRQFINYLPQEPYIFS 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 90 HlTAAENLRL-----VADARRDGAVATAEA---LDLFP-ALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTE 160
Cdd:TIGR01193 562 G-SILENLLLgakenVSQDEIWAACEIAEIkddIENMPlGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTS 640
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1033140466 161 GIQPSVVAEIQERIVELTRQsgfSVLLVEQHLGFALRVaNRYHVLESGRVTSHG 214
Cdd:TIGR01193 641 NLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQS-DKIIVLDHGKIIEQG 690
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
15-214 |
9.16e-17 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 78.61 E-value: 9.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 15 RVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLApHERVARGMAYVPQGqqcfPHLTAA 94
Cdd:PRK10790 355 LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLS-HSVLRQGVAMVQQD----PVVLAD 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 95 ---ENLRLVADARRDGAVATAEALDLFPALRPL-------LRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQP 164
Cdd:PRK10790 430 tflANVTLGRDISEEQVWQALETVQLAELARSLpdglytpLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDS 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1033140466 165 SVVAEIQERIVELTRQsgfSVLLVEQHLGFALRVANRYHVLESGRVTSHG 214
Cdd:PRK10790 510 GTEQAIQQALAAVREH---TTLVVIAHRLSTIVEADTILVLHRGQAVEQG 556
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-214 |
1.07e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 76.65 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGR-SRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDV-----TRLAPHERV 74
Cdd:PRK13639 1 ILETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkydkkSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 75 arGMAYVPQGQQCF-PhlTAAE-------NLRLVAD--ARRdgavaTAEALdlfpalrpllrRRAGL----------LSG 134
Cdd:PRK13639 81 --GIVFQNPDDQLFaP--TVEEdvafgplNLGLSKEevEKR-----VKEAL-----------KAVGMegfenkpphhLSG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 135 GQRQQLAIARALITRPRLLMLDEPTEGIQPSVVAEIQERIVELTRQsGFSVLLVEQHLGFALRVANRYHVLESGRVTSHG 214
Cdd:PRK13639 141 GQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEG 219
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-180 |
2.31e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 75.80 E-value: 2.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSR--VLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLA-PHERVARG 77
Cdd:PRK13632 7 MIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENlKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 78 MAYV-PQGQqcFPHLTAA-------ENLRLVADARRDGAVATAEALDlfpaLRPLLRRRAGLLSGGQRQQLAIARALITR 149
Cdd:PRK13632 87 IIFQnPDNQ--FIGATVEddiafglENKKVPPKKMKDIIDDLAKKVG----MEDYLDKEPQNLSGGQKQRVAIASVLALN 160
|
170 180 190
....*....|....*....|....*....|.
gi 1033140466 150 PRLLMLDEPTEGIQPSVVAEIQERIVELTRQ 180
Cdd:PRK13632 161 PEIIIFDESTSMLDPKGKREIKKIMVDLRKT 191
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
31-213 |
2.84e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 75.64 E-value: 2.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 31 AVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHE---RVARGMAYVPQgqqcFPHLTAAEN--LRLVADARR 105
Cdd:PRK13641 37 ALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnlkKLRKKVSLVFQ----FPEAQLFENtvLKDVEFGPK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 106 DGAVATAEALDlfPALRPLlrRRAGL-----------LSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVAEIQERI 174
Cdd:PRK13641 113 NFGFSEDEAKE--KALKWL--KKVGLsedliskspfeLSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLF 188
|
170 180 190
....*....|....*....|....*....|....*....
gi 1033140466 175 VELTRqSGFSVLLVEQHLGFALRVANRYHVLESGRVTSH 213
Cdd:PRK13641 189 KDYQK-AGHTVILVTHNMDDVAEYADDVLVLEHGKLIKH 226
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
9-186 |
3.80e-16 |
|
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: 73.84 E-value: 3.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 9 AGYGRSR--VLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSA---GTVELDGEDVTRLapHERVARGMAYVPQ 83
Cdd:cd03233 13 TGKGRSKipILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEF--AEKYPGEIIYVSE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 84 GQQCFPHLTAAENLRLVADARRDGAVataealdlfpalrpllrrRAglLSGGQRQQLAIARALITRPRLLMLDEPTEGIQ 163
Cdd:cd03233 91 EDVHFPTLTVRETLDFALRCKGNEFV------------------RG--ISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
170 180
....*....|....*....|...
gi 1033140466 164 PSVVAEIQERIVELTRQSGFSVL 186
Cdd:cd03233 151 SSTALEILKCIRTMADVLKTTTF 173
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
2-215 |
7.93e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 73.72 E-value: 7.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGyGRsrvLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLrPSAGTVELDGEDVTRLAPHErVARGMAYV 81
Cdd:COG4138 1 LQLNDVAVA-GR---LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAE-LARHRAYL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 82 PQGQQCFPHLTAAENLRLVADARRDGAVATAEALDLFPALR--PLLRRRAGLLSGGQRQQLAIARALIT-------RPRL 152
Cdd:COG4138 75 SQQQSPPFAMPVFQYLALHQPAGASSEAVEQLLAQLAEALGleDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1033140466 153 LMLDEPTEGIQPSVVAEIQERIVELTRQsGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGD 215
Cdd:COG4138 155 LLLDEPMNSLDVAQQAALDRLLRELCQQ-GITVVMSSHDLNHTLRHADRVWLLKQGKLVASGE 216
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
16-174 |
8.01e-16 |
|
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: 73.30 E-value: 8.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 16 VLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHeRVARGMAYVPQGqqcfPHL---T 92
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLH-DLRSRISIIPQD----PVLfsgT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 93 AAENL---RLVADARRDGAVATAEALDLFPALRPLLRRRA----GLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPS 165
Cdd:cd03244 94 IRSNLdpfGEYSDEELWQALERVGLKEFVESLPGGLDTVVeeggENLSVGQRQLLCLARALLRKSKILVLDEATASVDPE 173
|
....*....
gi 1033140466 166 VVAEIQERI 174
Cdd:cd03244 174 TDALIQKTI 182
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
37-211 |
9.37e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 75.33 E-value: 9.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 37 GAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVARGMAYVPQGQQ---CFPHLTAAENLRLvaDARR-------- 105
Cdd:PRK11288 289 GAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMLCPEDRKaegIIPVHSVADNINI--SARRhhlragcl 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 106 -DGAVATAEALDLFPALR---PLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVAEIQERIVELTRQs 181
Cdd:PRK11288 367 iNNRWEAENADRFIRSLNiktPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQ- 445
|
170 180 190
....*....|....*....|....*....|
gi 1033140466 182 GFSVLLVEQHLGFALRVANRYHVLESGRVT 211
Cdd:PRK11288 446 GVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
11-200 |
1.17e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 73.66 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 11 YGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGL--LRPSA---GTVELDGEDV--TRLAPHErVARGMAYVPQ 83
Cdd:PRK14243 20 YGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGFrveGKVTFHGKNLyaPDVDPVE-VRRRIGMVFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 84 GQQCFPHlTAAENL--------------RLVADARRDGAvataealdLFPALRPLLRRRAGLLSGGQRQQLAIARALITR 149
Cdd:PRK14243 99 KPNPFPK-SIYDNIaygaringykgdmdELVERSLRQAA--------LWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQ 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1033140466 150 PRLLMLDEPTEGIQPSVVAEIQERIVELTRQsgFSVLLVEQHLGFALRVAN 200
Cdd:PRK14243 170 PEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSD 218
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
5-188 |
1.91e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 74.76 E-value: 1.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 5 RGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVA---RGMAYV 81
Cdd:PRK10535 12 RSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQlrrEHFGFI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 82 PQGQQCFPHLTAAENLRL---VADARRDGAVATAEALDLFPALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEP 158
Cdd:PRK10535 92 FQRYHLLSHLTAAQNVEVpavYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEP 171
|
170 180 190
....*....|....*....|....*....|
gi 1033140466 159 TeGIQPSVVAEIQERIVELTRQSGFSVLLV 188
Cdd:PRK10535 172 T-GALDSHSGEEVMAILHQLRDRGHTVIIV 200
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-214 |
2.33e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 73.21 E-value: 2.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 10 GYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAG-----TVELDGEDVTRLAPHERVARGMAYVPQG 84
Cdd:PRK14271 30 GFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVLEFRRRVGMLFQR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 85 QQCFPH------LTAAENLRLVADARRDG-AVATAEALDLFPALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDE 157
Cdd:PRK14271 110 PNPFPMsimdnvLAGVRAHKLVPRKEFRGvAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDE 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1033140466 158 PTEGIQPSVVAEIQERIVELTRQsgFSVLLVEQHLGFALRVANRYHVLESGRVTSHG 214
Cdd:PRK14271 190 PTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEG 244
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
37-228 |
3.57e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 73.67 E-value: 3.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 37 GAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVARGMAYVPQGQQ---CFPHLTAAENL---RLVADARRDGAVA 110
Cdd:PRK09700 299 GSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYITESRRdngFFPNFSIAQNMaisRSLKDGGYKGAMG 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 111 ---------TAEALDLFPALR-PLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVAEIQERIVELTrQ 180
Cdd:PRK09700 379 lfhevdeqrTAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLA-D 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1033140466 181 SGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGDGG--VTAEREVRAAL 228
Cdd:PRK09700 458 DGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRddMSEEEIMAWAL 507
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
12-214 |
5.04e-15 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 73.46 E-value: 5.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 12 GRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLApHERVARGMAYVPQGQQCFPHl 91
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT-RASLRRNIAVVFQDAGLFNR- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 92 TAAENLRL----VADARRDGAVATAEALDlFPALRP-----LLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGI 162
Cdd:PRK13657 424 SIEDNIRVgrpdATDEEMRAAAERAQAHD-FIERKPdgydtVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSAL 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1033140466 163 QPSVVAEIQERIVELTRqsGFSVLLVEQHLGfALRVANRYHVLESGRVTSHG 214
Cdd:PRK13657 503 DVETEAKVKAALDELMK--GRTTFIIAHRLS-TVRNADRILVFDNGRVVESG 551
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-209 |
6.86e-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: 72.94 E-value: 6.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGlLRPSA---GTVELDGEDVTRLAPHERVARG 77
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHGtwdGEIYWSGSPLKASNIRDTERAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 78 MAYVPQGQQCFPHLTAAENLRLVADARRDGAVATAEALDLfpALRPLLR----------RRAGLLSGGQRQQLAIARALI 147
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIFLGNEITLPGGRMAYNAMYL--RAKNLLRelqldadnvtRPVGDYGGGQQQLVEIAKALN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1033140466 148 TRPRLLMLDEPTEGIQPSVVaEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGR 209
Cdd:TIGR02633 158 KQARLLILDEPSSSLTEKET-EILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
31-221 |
7.64e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 71.36 E-value: 7.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 31 AVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDV--------------------TRLAPHERVARGMAyvpqgqqcFPH 90
Cdd:PRK15112 43 AIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfgdysyrsqrirmifqdpsTSLNPRQRISQILD--------FPL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 91 LTaaeNLRLVADARRDGAVATAEALDLFP---ALRPllrrraGLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVV 167
Cdd:PRK15112 115 RL---NTDLEPEQREKQIIETLRQVGLLPdhaSYYP------HMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMR 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1033140466 168 AEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGDggvTAE 221
Cdd:PRK15112 186 SQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGS---TAD 236
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
12-186 |
8.05e-15 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 69.96 E-value: 8.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 12 GRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGllRPSAGTVE----LDGEDVTrlaphERVARGMAYVPQGQQC 87
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAGVITgeilINGRPLD-----KNFQRSTGYVEQQDVH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 88 FPHLTAAENLRLVADARRdgavataealdlfpalrpllrrraglLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVV 167
Cdd:cd03232 91 SPNLTVREALRFSALLRG--------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAA 144
|
170
....*....|....*....
gi 1033140466 168 AEIQERIVELTRqSGFSVL 186
Cdd:cd03232 145 YNIVRFLKKLAD-SGQAIL 162
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
54-228 |
1.06e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 72.27 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 54 SAGTVELDGEDVTRLAPHERVARGMAYVPQGQQCF---PHLTAAENLRLVADARRDGAVATAEALDLFPALRPLLRRRA- 129
Cdd:PRK13549 316 WEGEIFIDGKPVKIRNPQQAIAQGIAMVPEDRKRDgivPVMGVGKNITLAALDRFTGGSRIDDAAELKTILESIQRLKVk 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 130 --------GLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVAEIQERIVELTRQsGFSVLLVEQHLGFALRVANR 201
Cdd:PRK13549 396 taspelaiARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDR 474
|
170 180 190
....*....|....*....|....*....|
gi 1033140466 202 YHVLESGRVTshGD---GGVTAEREVRAAL 228
Cdd:PRK13549 475 VLVMHEGKLK--GDlinHNLTQEQVMEAAL 502
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
7-213 |
1.50e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 72.32 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 7 VHAGY--GRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHErVARGMAYVPQG 84
Cdd:PLN03232 1240 VHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTD-LRRVLSIIPQS 1318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 85 QQCFphltaAENLRLVADARRDGAVAtaealDLFPAL-----RPLLRRRA-GL----------LSGGQRQQLAIARALIT 148
Cdd:PLN03232 1319 PVLF-----SGTVRFNIDPFSEHNDA-----DLWEALerahiKDVIDRNPfGLdaevseggenFSVGQRQLLSLARALLR 1388
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1033140466 149 RPRLLMLDEPTEGIQPSVVAEIQERIVELTRQsgfSVLLVEQHLGFALRVANRYHVLESGRVTSH 213
Cdd:PLN03232 1389 RSKILVLDEATASVDVRTDSLIQRTIREEFKS---CTMLVIAHRLNTIIDCDKILVLSSGQVLEY 1450
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-159 |
1.64e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.88 E-value: 1.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLrPSA---GTVELDGEDVTRLAPHERVARG 77
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEGEELQASNIRDTERAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 78 MAYVPQGQQCFPHLTAAENLRLVADARRDG----AVATAEA--------LDLFPALrpllrrRAGLLSGGQRQQLAIARA 145
Cdd:PRK13549 84 IAIIHQELALVKELSVLENIFLGNEITPGGimdyDAMYLRAqkllaqlkLDINPAT------PVGNLGLGQQQLVEIAKA 157
|
170
....*....|....
gi 1033140466 146 LITRPRLLMLDEPT 159
Cdd:PRK13549 158 LNKQARLLILDEPT 171
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
15-214 |
2.48e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 70.42 E-value: 2.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 15 RVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAG-TVELDGE---DVTRLAPHERVARGMAYVPQgqqcFPH 90
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqTIVGDYAipaNLKKIKEVKRLRKEIGLVFQ----FPE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 91 LTAAEN----------LRLVADaRRDGAVATAEALDLFPALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTE 160
Cdd:PRK13645 101 YQLFQEtiekdiafgpVNLGEN-KQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTG 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1033140466 161 GIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHG 214
Cdd:PRK13645 180 GLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIG 233
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
33-182 |
2.53e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 71.69 E-value: 2.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 33 LGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTrlaphervARGMA------YVPQGQQCFPHLTAAENLRL------V 100
Cdd:NF033858 298 LGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD--------AGDIAtrrrvgYMSQAFSLYGELTVRQNLELharlfhL 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 101 ADARRDGAVAtaEALDLFpALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPsvVAEIQ--ERIVELT 178
Cdd:NF033858 370 PAAEIAARVA--EMLERF-DLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDP--VARDMfwRLLIELS 444
|
....
gi 1033140466 179 RQSG 182
Cdd:NF033858 445 REDG 448
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
16-159 |
4.19e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 70.61 E-value: 4.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 16 VLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVEL-DGEDVTRLAphERvargmAYVPQG----QQCFPH 90
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLFLP--QR-----PYLPLGtlreALLYPA 450
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1033140466 91 LtaaenlrlvADARRDGAVATA-EALDLfPALRPLL---RRRAGLLSGGQRQQLAIARALITRPRLLMLDEPT 159
Cdd:COG4178 451 T---------AEAFSDAELREAlEAVGL-GHLAERLdeeADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEAT 513
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
18-215 |
4.80e-14 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 68.96 E-value: 4.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 18 HGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRP----SAGTVELDGEdvtRLAPHERVARGMAYVPQG-QQCF-PHL 91
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGK---PVAPCALRGRKIATIMQNpRSAFnPLH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 92 T----AAENLRLVADARRDGAVATA-EALDLFPALRpLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSV 166
Cdd:PRK10418 97 TmhthARETCLALGKPADDATLTAAlEAVGLENAAR-VLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1033140466 167 VAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGD 215
Cdd:PRK10418 176 QARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGD 224
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
31-159 |
6.31e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 70.26 E-value: 6.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 31 AVLGHNGAGKSTLLRVAAGLLrPSAGTVELDGEDVTRLAPhERVARGMAYVPQGQQcFPHLTAAENLRL----VADARRD 106
Cdd:PRK11174 380 ALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDP-ESWRKHLSWVGQNPQ-LPHGTLRDNVLLgnpdASDEQLQ 456
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1033140466 107 GAVATAEALDLFPALRPLL----RRRAGLLSGGQRQQLAIARALITRPRLLMLDEPT 159
Cdd:PRK11174 457 QALENAWVSEFLPLLPQGLdtpiGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPT 513
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
4-214 |
7.20e-14 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 69.76 E-value: 7.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 4 LRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLlRVAAGLLRPSAGtvELDGEDVTRLAPHERVARGMAY--- 80
Cdd:NF000106 16 VRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAG--RRPWRF*TWCANRRALRRTIG*hrp 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 81 VPQGQQcfPHLTAAENLRLVAD----ARRDGAVATAEALDLFpALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLD 156
Cdd:NF000106 93 VR*GRR--ESFSGRENLYMIGR*ldlSRKDARARADELLERF-SLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1033140466 157 EPTEGIQPSVVAEIQERIVELTRqSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHG 214
Cdd:NF000106 170 EPTTGLDPRTRNEVWDEVRSMVR-DGATVLLTTQYMEEAEQLAHELTVIDRGRVIADG 226
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
32-209 |
9.43e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 68.96 E-value: 9.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 32 VLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHE-RVARGmayvpQGQQCF--------PHLTA----AENLR 98
Cdd:PRK15079 52 VVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEwRAVRS-----DIQMIFqdplaslnPRMTIgeiiAEPLR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 99 -----LVADARRDGAVATAEALDLFPALrplLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVAEIQER 173
Cdd:PRK15079 127 tyhpkLSRQEVKDRVKAMMLKVGLLPNL---INRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNL 203
|
170 180 190
....*....|....*....|....*....|....*.
gi 1033140466 174 IVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGR 209
Cdd:PRK15079 204 LQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGH 239
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
17-210 |
9.66e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 68.58 E-value: 9.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 17 LHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVT-RLAPHERVARGMAYVPQGQQcFPHLTAAE 95
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTaENVWNLRRKIGMVFQNPDNQ-FVGATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 96 NLRLVADAR---RDGAVATAEALDLFPALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVAEIQE 172
Cdd:PRK13642 102 DVAFGMENQgipREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMR 181
|
170 180 190
....*....|....*....|....*....|....*...
gi 1033140466 173 RIVELTRQSGFSVLLVEQHLGFALRvANRYHVLESGRV 210
Cdd:PRK13642 182 VIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEI 218
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
16-216 |
1.21e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 69.52 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 16 VLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPS--AGTVELDGEDVTRlapheRVARGMAYVPQGQQCFPHLTA 93
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTK-----QILKRTGFVTQDDILYPHLTV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 94 AENLRLVADARRDGAVATAEALDLFPALRPLLrrraGL---------------LSGGQRQQLAIARALITRPRLLMLDEP 158
Cdd:PLN03211 158 RETLVFCSLLRLPKSLTKQEKILVAESVISEL----GLtkcentiignsfirgISGGERKRVSIAHEMLINPSLLILDEP 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1033140466 159 TEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGDG 216
Cdd:PLN03211 234 TSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKG 291
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
12-215 |
1.27e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 69.35 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 12 GRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTllrVAAGLLR--PSAGTVELDGEDVTRLAPHER--VARGMAYVPQ--GQ 85
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKST---TGLALLRliNSQGEIWFDGQPLHNLNRRQLlpVRHRIQVVFQdpNS 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 86 QCFPHLTA----AENLR-----LVADARRDGAVATAEALDLFPALRpllRRRAGLLSGGQRQQLAIARALITRPRLLMLD 156
Cdd:PRK15134 374 SLNPRLNVlqiiEEGLRvhqptLSAAQREQQVIAVMEEVGLDPETR---HRYPAEFSGGQRQRIAIARALILKPSLIILD 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1033140466 157 EPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGD 215
Cdd:PRK15134 451 EPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGD 509
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
28-228 |
1.27e-13 |
|
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: 69.08 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 28 GVAAVLGhngAGKSTLLRVAAGLLRPS-AGTVELDGEDVTRLAPHERVARGMAYVPQGQQ---CFPHLTAAENLRLVADA 103
Cdd:TIGR02633 290 GVAGLVG---AGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKrhgIVPILGVGKNITLSVLK 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 104 RRDGAVATAEALDLFPALRPLLRRRA---------GLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVAEIQERI 174
Cdd:TIGR02633 367 SFCFKMRIDAAAELQIIGSAIQRLKVktaspflpiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLI 446
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1033140466 175 VELTRQsGFSVLLVEQHLGFALRVANRYHVLESGRV-TSHGDGGVTAEREVRAAL 228
Cdd:TIGR02633 447 NQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLkGDFVNHALTQEQVLAAAL 500
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
31-212 |
2.18e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 67.45 E-value: 2.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 31 AVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHE-RVARGMAYV-PQGQqcFPHLTA----AENLRLVADAR 104
Cdd:PRK13650 37 SIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDiRHKIGMVFQnPDNQ--FVGATVeddvAFGLENKGIPH 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 105 RDGAVATAEALDLFpALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVAEIQERIVELTRQSGFS 184
Cdd:PRK13650 115 EEMKERVNEALELV-GMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMT 193
|
170 180
....*....|....*....|....*...
gi 1033140466 185 VLLVEQHLGfALRVANRYHVLESGRVTS 212
Cdd:PRK13650 194 VISITHDLD-EVALSDRVLVMKNGQVES 220
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
17-214 |
2.29e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 67.50 E-value: 2.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 17 LHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVT-----RLAPHERVARGMAYVPQGQQCFPHL 91
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkdKYIRPVRKRIGMVFQFPESQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 92 TAAENLRLVADARRDGAVATAEALDLFPAL---RPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVA 168
Cdd:PRK13646 103 VEREIIFGPKNFKMNLDEVKNYAHRLLMDLgfsRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKR 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1033140466 169 EIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHG 214
Cdd:PRK13646 183 QVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQT 228
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
15-215 |
2.52e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 67.80 E-value: 2.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 15 RVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVARGMAYVPQGQQCFPHLTAA 94
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEKVLEKLVIQKTRFKKIKKI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 95 ENLRlvadaRRDGAV----------ATAEALDLFPAL-----RPLLRRRA-------GL-----------LSGGQRQQLA 141
Cdd:PRK13651 101 KEIR-----RRVGVVfqfaeyqlfeQTIEKDIIFGPVsmgvsKEEAKKRAakyielvGLdesylqrspfeLSGGQKRRVA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1033140466 142 IARALITRPRLLMLDEPTEGIQPSVVAEIQERIVELtRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGD 215
Cdd:PRK13651 176 LAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNL-NKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGD 248
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-215 |
2.76e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 66.97 E-value: 2.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGllRPS----AGTVELDGEDVTRLAPHERVAR 76
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDLEPEERAHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 77 GMAYVPQGQQCFPHLTAAENLRLVADARRDG-AVATAEALDLFPALRPLL-----------RRRAGLLSGGQRQQLAIAR 144
Cdd:CHL00131 85 GIFLAFQYPIEIPGVSNADFLRLAYNSKRKFqGLPELDPLEFLEIINEKLklvgmdpsflsRNVNEGFSGGEKKRNEILQ 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1033140466 145 ALITRPRLLMLDEPTEGIQPSVVAEIQERIVELTRQSGfSVLLVE--QHLgFALRVANRYHVLESGRVTSHGD 215
Cdd:CHL00131 165 MALLDSELAILDETDSGLDIDALKIIAEGINKLMTSEN-SIILIThyQRL-LDYIKPDYVHVMQNGKIIKTGD 235
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-159 |
5.17e-13 |
|
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: 67.65 E-value: 5.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 5 RGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELdGEDVTrlaphervargMAYVPQG 84
Cdd:TIGR03719 326 ENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK-----------LAYVDQS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 85 QQcfpHLTAAENlrlVADARRDGavatAEALDL----FPAlRPLLRR----------RAGLLSGGQRQQLAIARALITRP 150
Cdd:TIGR03719 394 RD---ALDPNKT---VWEEISGG----LDIIKLgkreIPS-RAYVGRfnfkgsdqqkKVGQLSGGERNRVHLAKTLKSGG 462
|
....*....
gi 1033140466 151 RLLMLDEPT 159
Cdd:TIGR03719 463 NVLLLDEPT 471
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-159 |
6.24e-13 |
|
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: 67.27 E-value: 6.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 3 TLRGVHAGYGRSR-VLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGL-------LRPSAG-TV-------ELDGEDVT 66
Cdd:TIGR03719 6 TMNRVSKVVPPKKeILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdkdfngeARPQPGiKVgylpqepQLDPTKTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 67 RlaphERVARGMAYVPQGQQCFPHLTA------AENLRLVAD-ARRDGAVATAEALDL-------FPALR-PLLRRRAGL 131
Cdd:TIGR03719 86 R----ENVEEGVAEIKDALDRFNEISAkyaepdADFDKLAAEqAELQEIIDAADAWDLdsqleiaMDALRcPPWDADVTK 161
|
170 180
....*....|....*....|....*...
gi 1033140466 132 LSGGQRQQLAIARALITRPRLLMLDEPT 159
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPT 189
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-215 |
8.65e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 65.78 E-value: 8.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGY-GRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVARGMA 79
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 80 YVPQGQQC-FPHLTAAENLRL--------VADARRDGAVATAEAldlfpALRPLLRRRAGLLSGGQRQQLAIARALITRP 150
Cdd:PRK13644 81 IVFQNPETqFVGRTVEEDLAFgpenlclpPIEIRKRVDRALAEI-----GLEKYRHRSPKTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1033140466 151 RLLMLDEPTEGIQPSVVAEIQERIVELTRQsGFSVLLVEQHLGfALRVANRYHVLESGRVTSHGD 215
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGE 218
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
22-192 |
1.01e-12 |
|
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: 66.96 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 22 LAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVtrLAPHERVARGMAYVPQGQQCFPHLTAAENLRLVA 101
Cdd:TIGR01257 1960 VGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI--LTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYA 2037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 102 DARRDGA-----VATAEALDLfpALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVAEIQERIVE 176
Cdd:TIGR01257 2038 RLRGVPAeeiekVANWSIQSL--GLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVS 2115
|
170
....*....|....*.
gi 1033140466 177 LTRQsGFSVLLVEQHL 192
Cdd:TIGR01257 2116 IIRE-GRAVVLTSHSM 2130
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-206 |
1.49e-12 |
|
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: 64.74 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 29 VAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVtrlaphervargmAYVPQGQQCFPHLTAAENLRLVADARRDGA 108
Cdd:cd03237 27 VIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-------------SYKPQYIKADYEGTVRDLLSSITKDFYTHP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 109 VATAEALDlfP-ALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGI---QPSVVAEIQERIVELTRQSGFs 184
Cdd:cd03237 94 YFKTEIAK--PlQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLdveQRLMASKVIRRFAENNEKTAF- 170
|
170 180
....*....|....*....|..
gi 1033140466 185 vlLVEQHLGFALRVANRYHVLE 206
Cdd:cd03237 171 --VVEHDIIMIDYLADRLIVFE 190
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
17-214 |
1.51e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 65.29 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 17 LHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVargmAYVPQGQQC---FPHLTa 93
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLV----AYVPQSEEVdwsFPVLV- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 94 aENLRLVADARRDGAVATAEALDLFPALRPLLR--------RRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPS 165
Cdd:PRK15056 98 -EDVVMMGRYGHMGWLRRAKKRDRQIVTAALARvdmvefrhRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVK 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1033140466 166 VVAEIQERIVELtRQSGFSVLLVEQHLGFALRVANrYHVLESGRVTSHG 214
Cdd:PRK15056 177 TEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASG 223
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
28-211 |
1.63e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.84 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 28 GVAAVLGhngAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVARGMAYVPQGQQcfphltaAENLRLVADARRDG 107
Cdd:PRK15439 293 GLAGVVG---AGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVYLPEDRQ-------SSGLYLDAPLAWNV 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 108 AVATAEALDLFpaLRP------LLRRRAGL-------------LSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVA 168
Cdd:PRK15439 363 CALTHNRRGFW--IKParenavLERYRRALnikfnhaeqaartLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARN 440
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1033140466 169 EIQERIVELTRQsGFSVLLVEQHLGFALRVANRYHVLESGRVT 211
Cdd:PRK15439 441 DIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEIS 482
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
15-191 |
1.67e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 64.21 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 15 RVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLL--RPSAGTVELDGEDVTRLAPH-ERVARGMayvpqgqqcfPHL 91
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGREASLiDAIGRKG----------DFK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 92 TAAENLrlvadarrdGAVATAEAldlfpalrPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVAEIQ 171
Cdd:COG2401 114 DAVELL---------NAVGLSDA--------VLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVA 176
|
170 180
....*....|....*....|
gi 1033140466 172 ERIVELTRQSGFSVLLVEQH 191
Cdd:COG2401 177 RNLQKLARRAGITLVVATHH 196
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
32-215 |
1.86e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 65.52 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 32 VLGHNGAGKSTLLRVAAGLLRPS---AGTVELDGEDVTRLAPHE--RV-ARGMAYVPQGQQCF--PHLTAAENLR--LVA 101
Cdd:PRK09473 47 IVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKElnKLrAEQISMIFQDPMTSlnPYMRVGEQLMevLML 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 102 DARRDGAVATAEALDLFPALR-PLLRRRAGL----LSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVAEIQERIVE 176
Cdd:PRK09473 127 HKGMSKAEAFEESVRMLDAVKmPEARKRMKMypheFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNE 206
|
170 180 190
....*....|....*....|....*....|....*....
gi 1033140466 177 LTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGD 215
Cdd:PRK09473 207 LKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGN 245
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
32-188 |
2.11e-12 |
|
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: 62.94 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 32 VLGHNGAGKSTLLRVAAGLLRPSAGTVELdgedvtrlapHERvaRGMAYVPQGqqcfPHLTAAeNLRlvadarrdgavat 111
Cdd:cd03223 32 ITGPSGTGKSSLFRALAGLWPWGSGRIGM----------PEG--EDLLFLPQR----PYLPLG-TLR------------- 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1033140466 112 aEALdlfpaLRPLLRRraglLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPsvvaEIQERIVELTRQSGFSVLLV 188
Cdd:cd03223 82 -EQL-----IYPWDDV----LSGGEQQRLAFARLLLHKPKFVFLDEATSALDE----ESEDRLYQLLKELGITVISV 144
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-175 |
2.76e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 65.74 E-value: 2.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 17 LHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEdvtrlaphervargMAYVPQgQQCFPHLTAAEN 96
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--------------VAYVPQ-QAWIQNDSLREN 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 97 LRLVADARRDGAVATAEALDLFPALRPL-------LRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVAE 169
Cdd:TIGR00957 719 ILFGKALNEKYYQQVLEACALLPDLEILpsgdrteIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKH 798
|
....*.
gi 1033140466 170 IQERIV 175
Cdd:TIGR00957 799 IFEHVI 804
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
132-213 |
3.35e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 65.11 E-value: 3.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 132 LSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVT 211
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCV 236
|
..
gi 1033140466 212 SH 213
Cdd:PRK15134 237 EQ 238
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
15-162 |
3.96e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 65.13 E-value: 3.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 15 RVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGllRPSAGTVELDGEDVTRLAPHERVARGMAYVPQGQQCFPHLTAA 94
Cdd:TIGR00956 777 VILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTGVITGGDRLVNGRPLDSSFQRSIGYVQQQDLHLPTSTVR 854
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1033140466 95 ENLRLVADARRDGAVATAEALDLFPALRPLLRRRA------GL----LSGGQRQQLAIARALITRPRLLM-LDEPTEGI 162
Cdd:TIGR00956 855 ESLRFSAYLRQPKSVSKSEKMEYVEEVIKLLEMESyadavvGVpgegLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGL 933
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-215 |
4.02e-12 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 63.66 E-value: 4.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGL--LRPSAGTVELDGEDVTRLAPHERVARG- 77
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEGi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 78 -MAY-----VPQGQQCFPHLTAAENLRLVADA----RRDGAVATAEALDLFPALRPLLRRRAGL-LSGGQRQQLAIARAL 146
Cdd:PRK09580 81 fMAFqypveIPGVSNQFFLQTALNAVRSYRGQepldRFDFQDLMEEKIALLKMPEDLLTRSVNVgFSGGEKKRNDILQMA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 147 ITRPRLLMLDEPTEGIQPSVVAEIQERIVELtRQSGFSVLLVEQHLGFALRVANRY-HVLESGRVTSHGD 215
Cdd:PRK09580 161 VLEPELCILDESDSGLDIDALKIVADGVNSL-RDGKRSFIIVTHYQRILDYIKPDYvHVLYQGRIVKSGD 229
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
16-164 |
4.82e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 62.94 E-value: 4.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 16 VLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRlapHERvARGMAYVPQGQQCFPHLTAAE 95
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR---GDR-SRFMAYLGHLPGLKADLSTLE 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1033140466 96 NLRLVA-----DARRDGAVATAeALDLFPALRPLLRRraglLSGGQRQQLAIARALITRPRLLMLDEPTEGIQP 164
Cdd:PRK13543 102 NLHFLCglhgrRAKQMPGSALA-IVGLAGYEDTLVRQ----LSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
28-211 |
6.00e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 64.37 E-value: 6.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 28 GVAAVLGhngAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVARGMAYVPQGQQC---FPHLTAAEN-------- 96
Cdd:PRK10982 278 GIAGLVG---AKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHGFALVTEERRStgiYAYLDIGFNslisnirn 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 97 ----LRLVADARRDGAvaTAEALDLFPALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVAEIQE 172
Cdd:PRK10982 355 yknkVGLLDNSRMKSD--TQWVIDSMRVKTPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQ 432
|
170 180 190
....*....|....*....|....*....|....*....
gi 1033140466 173 RIVELTRQsGFSVLLVEQHLGFALRVANRYHVLESGRVT 211
Cdd:PRK10982 433 LIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLVA 470
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
13-209 |
6.67e-12 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 62.49 E-value: 6.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 13 RSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGedvtrlaphervarGMAYVPQgQQCFPHLT 92
Cdd:cd03250 17 TSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--------------SIAYVSQ-EPWIQNGT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 93 AAENLRLVA--DARRDGAVATAEALD----LFPalrpllrrrAGL----------LSGGQRQQLAIARALITRPRLLMLD 156
Cdd:cd03250 82 IRENILFGKpfDEERYEKVIKACALEpdleILP---------DGDlteigekginLSGGQKQRISLARAVYSDADIYLLD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1033140466 157 EPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRvANRYHVLESGR 209
Cdd:cd03250 153 DPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
6-225 |
7.44e-12 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 64.04 E-value: 7.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 6 GVHAgygrsrvLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLrPSA---GTVELDGEDVTRLAPHERVARGMAYVP 82
Cdd:NF040905 13 GVKA-------LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHGsyeGEILFDGEVCRFKDIRDSEALGIVIIH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 83 QGQQCFPHLTAAENLRLVADARRDGAV----ATAEALDLFpalrpllrRRAGL----------LSGGQRQQLAIARALIT 148
Cdd:NF040905 85 QELALIPYLSIAENIFLGNERAKRGVIdwneTNRRARELL--------AKVGLdespdtlvtdIGVGKQQLVEIAKALSK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 149 RPRLLMLDEPTEGIQPSVVAEIQERIVELTRQsGFSVLLVEQHLGFALRVANRYHVLESGRVTSH---GDGGVTAEREVR 225
Cdd:NF040905 157 DVKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGRTIETldcRADEVTEDRIIR 235
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
16-215 |
1.54e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 62.56 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 16 VLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELdgEDVtRLAPHERVARGMAYVPQGQqcfphLTAAE 95
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQV--GDI-YIGDKKNNHELITNPYSKK-----IKNFK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 96 NLR-------------LVADA-RRD---GAVA-----------TAEALDLFPALRPLLRRRAGLLSGGQRQQLAIARALI 147
Cdd:PRK13631 113 ELRrrvsmvfqfpeyqLFKDTiEKDimfGPVAlgvkkseakklAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILA 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1033140466 148 TRPRLLMLDEPTEGIQPSVVAEIQERIVElTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGD 215
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGT 259
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
32-214 |
1.76e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 61.87 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 32 VLGHNGAGKSTLLRVAAGLLrPSAGTVELDGEDVTRLAPHErVARGMAYVPQGQQ------CFPHLTaaenLRLVADARR 105
Cdd:PRK03695 27 LVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAE-LARHRAYLSQQQTppfampVFQYLT----LHQPDKTRT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 106 DGAVATAEALDLFPALRPLLRRRAGLLSGG--QRQQLA-----IARALITRPRLLMLDEPTEGIQPSVVAEIQERIVELT 178
Cdd:PRK03695 101 EAVASALNEVAEALGLDDKLGRSVNQLSGGewQRVRLAavvlqVWPDINPAGQLLLLDEPMNSLDVAQQAALDRLLSELC 180
|
170 180 190
....*....|....*....|....*....|....*.
gi 1033140466 179 RQsGFSVLLVEQHLGFALRVANRYHVLESGRVTSHG 214
Cdd:PRK03695 181 QQ-GIAVVMSSHDLNHTLRHADRVWLLKQGKLLASG 215
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-185 |
1.92e-11 |
|
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: 62.88 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 29 VAAVLGHNGAGKSTLLRVAAGLLRPSAGTVEldgEDVTrlaphervargMAYVPQGQQCFPHLTAAENLRLVADARRDGA 108
Cdd:COG1245 368 VLGIVGPNGIGKTTFAKILAGVLKPDEGEVD---EDLK-----------ISYKPQYISPDYDGTVEEFLRSANTDDFGSS 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 109 VATAEALDLFpALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPT-----EgiQPSVVAEIQERIVELTRQSGF 183
Cdd:COG1245 434 YYKTEIIKPL-GLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSahldvE--QRLAVAKAIRRFAENRGKTAM 510
|
..
gi 1033140466 184 SV 185
Cdd:COG1245 511 VV 512
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-159 |
2.21e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 62.88 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELdgedvtrlaphervARG--M 78
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL--------------AKGikL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 79 AYVPQGQQCFphLTAAEN--LRLVADARRDGAVATAEALDLFPALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLD 156
Cdd:PRK10636 378 GYFAQHQLEF--LRADESplQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLD 455
|
...
gi 1033140466 157 EPT 159
Cdd:PRK10636 456 EPT 458
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-159 |
5.02e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 61.67 E-value: 5.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 6 GVHAGYGrSRVL-HGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELdGEDVTrlaphervargMAYVPQG 84
Cdd:PRK11819 329 NLSKSFG-DRLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVK-----------LAYVDQS 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 85 QQcfpHLTAAENlrlVADARRDGA----VATAEaldlFPAlRPLLRR----------RAGLLSGGQRQQLAIARALITRP 150
Cdd:PRK11819 396 RD---ALDPNKT---VWEEISGGLdiikVGNRE----IPS-RAYVGRfnfkggdqqkKVGVLSGGERNRLHLAKTLKQGG 464
|
....*....
gi 1033140466 151 RLLMLDEPT 159
Cdd:PRK11819 465 NVLLLDEPT 473
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-185 |
8.86e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.98 E-value: 8.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 29 VAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDgedvtrlaphERVArgmaYVPQGQQCFPHLTAAENLRLVADARRDGA 108
Cdd:PRK13409 367 VIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE----------LKIS----YKPQYIKPDYDGTVEDLLRSITDDLGSSY 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 109 VAT--AEALdlfpALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPT-----EgiQPSVVAEIQERIVELTRQS 181
Cdd:PRK13409 433 YKSeiIKPL----QLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSahldvE--QRLAVAKAIRRIAEEREAT 506
|
....
gi 1033140466 182 GFSV 185
Cdd:PRK13409 507 ALVV 510
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
16-214 |
1.10e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 59.81 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 16 VLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSA---GTVELDGEDVTRLAP---HERVarGMAYV-PQGQqcF 88
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVwdiREKV--GIVFQnPDNQ--F 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 89 PHLTAA-------EN--------LRLVADARRDgaVATAEALDLFPALrpllrrraglLSGGQRQQLAIARALITRPRLL 153
Cdd:PRK13640 98 VGATVGddvafglENravprpemIKIVRDVLAD--VGMLDYIDSEPAN----------LSGGQKQRVAIAGILAVEPKII 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1033140466 154 MLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFAlRVANRYHVLESGRVTSHG 214
Cdd:PRK13640 166 ILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQG 225
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
29-214 |
1.36e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 59.76 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 29 VAAVLGHNGAGKSTLLRVAAGLL----RPSAGTVELDGEDVTRLAPHER---VARGMAYVPQGQQCF--PHLTAAENLRL 99
Cdd:PRK11022 35 VVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDLQRISEKERrnlVGAEVAMIFQDPMTSlnPCYTVGFQIME 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 100 VADARRDGAVAT--AEALDLF-----PALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVAEIQE 172
Cdd:PRK11022 115 AIKVHQGGNKKTrrQRAIDLLnqvgiPDPASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIE 194
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1033140466 173 RIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHG 214
Cdd:PRK11022 195 LLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETG 236
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
16-214 |
1.45e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 60.52 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 16 VLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHErVARGMAYVPQGQQCFphltaAE 95
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMD-LRKVLGIIPQAPVLF-----SG 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 96 NLRLVADARRDGAVAtaealDLFPAL-----RPLLRRRA-GL----------LSGGQRQQLAIARALITRPRLLMLDEPT 159
Cdd:PLN03130 1328 TVRFNLDPFNEHNDA-----DLWESLerahlKDVIRRNSlGLdaevseagenFSVGQRQLLSLARALLRRSKILVLDEAT 1402
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1033140466 160 EGIQPSVVAEIQERIVELTRQsgfSVLLVEQHLGFALRVANRYHVLESGRVTSHG 214
Cdd:PLN03130 1403 AAVDVRTDALIQKTIREEFKS---CTMLIIAHRLNTIIDCDRILVLDAGRVVEFD 1454
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
13-186 |
2.15e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 60.24 E-value: 2.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 13 RSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGllRPSAGTVELDGEDVTRLAPHERVARGMAYVPQGQQCFPHLT 92
Cdd:PLN03140 892 RLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEGDIRISGFPKKQETFARISGYCEQNDIHSPQVT 969
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 93 AAENLRLVADARRDGAVATAEALDLFPALRPLLR----RRA--GL-----LSGGQRQQLAIARALITRPRLLMLDEPTEG 161
Cdd:PLN03140 970 VRESLIYSAFLRLPKEVSKEEKMMFVDEVMELVEldnlKDAivGLpgvtgLSTEQRKRLTIAVELVANPSIIFMDEPTSG 1049
|
170 180
....*....|....*....|....*
gi 1033140466 162 IQPSVVAeIQERIVELTRQSGFSVL 186
Cdd:PLN03140 1050 LDARAAA-IVMRTVRNTVDTGRTVV 1073
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
17-214 |
3.81e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 58.88 E-value: 3.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 17 LHGVDLAVPPDGVAAVLGHNGAGKSTLlrvaAGLLRP----SAGTVELDGEDVT--RLApheRVARGMAYVPQGQQCFpH 90
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTI----ANLLTRfydiDEGEILLDGHDLRdyTLA---SLRNQVALVSQNVHLF-N 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 91 LTAAENlrlVADARRD--------GAVATAEALDLFPALRPLLRRRAG----LLSGGQRQQLAIARALITRPRLLMLDEP 158
Cdd:PRK11176 431 DTIANN---IAYARTEqysreqieEAARMAYAMDFINKMDNGLDTVIGengvLLSGGQRQRIAIARALLRDSPILILDEA 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1033140466 159 TEGIQPSVVAEIQERIVELtrQSGFSVLLVEQHLGfALRVANRYHVLESGRVTSHG 214
Cdd:PRK11176 508 TSALDTESERAIQAALDEL--QKNRTSLVIAHRLS-TIEKADEILVVEDGEIVERG 560
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-159 |
3.90e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.98 E-value: 3.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 3 TLRGVHAGYGRSR-VLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSagtvelDGEdvTRLAPHERVargmAYV 81
Cdd:PRK11819 8 TMNRVSKVVPPKKqILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEF------EGE--ARPAPGIKV----GYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 82 PQGQQCFPHLTAAENLRL-VAD-----ARRDG-AVATAEALDLFPAlrpLLRRRAGL----------------------- 131
Cdd:PRK11819 76 PQEPQLDPEKTVRENVEEgVAEvkaalDRFNEiYAAYAEPDADFDA---LAAEQGELqeiidaadawdldsqleiamdal 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 1033140466 132 -----------LSGGQRQQLAIARALITRPRLLMLDEPT 159
Cdd:PRK11819 153 rcppwdakvtkLSGGERRRVALCRLLLEKPDMLLLDEPT 191
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
31-215 |
7.72e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 58.33 E-value: 7.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 31 AVLGHNGAGKSTLLRVAAGLLRPSAGTVELDG-------EDVTRL----APHERVARG--MAYVPQ------------GQ 85
Cdd:PRK10261 46 AIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsRQVIELseqsAAQMRHVRGadMAMIFQepmtslnpvftvGE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 86 QCfphltaAENLRLVADARRDGAVATAE-ALDL--FPALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGI 162
Cdd:PRK10261 126 QI------AESIRLHQGASREEAMVEAKrMLDQvrIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTAL 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1033140466 163 QPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHGD 215
Cdd:PRK10261 200 DVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGS 252
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
17-194 |
1.31e-09 |
|
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: 56.19 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 17 LHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVARG---MAYVPQgQQCFPHLTA 93
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNrysVAYAAQ-KPWLLNATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 94 AENLRLVADARRDGAVATAEALDLFPALRPL-------LRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSV 166
Cdd:cd03290 96 EENITFGSPFNKQRYKAVTDACSLQPDIDLLpfgdqteIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHL 175
|
170 180
....*....|....*....|....*....
gi 1033140466 167 VAEI-QERIVELTRQSGFSVLLVEQHLGF 194
Cdd:cd03290 176 SDHLmQEGILKFLQDDKRTLVLVTHKLQY 204
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
15-170 |
4.57e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 56.27 E-value: 4.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 15 RVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAA----GLLRPSAGTVELDGEDVTRLAPHERVArgMAYVPQGQQCFPH 90
Cdd:TIGR00956 75 DILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYRGD--VVYNAETDVHFPH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 91 LTAAENLRLVADARRdgavataealdlfPALRPLLRRRA--------------GL---------------LSGGQRQQLA 141
Cdd:TIGR00956 153 LTVGETLDFAARCKT-------------PQNRPDGVSREeyakhiadvymatyGLshtrntkvgndfvrgVSGGERKRVS 219
|
170 180
....*....|....*....|....*....
gi 1033140466 142 IARALITRPRLLMLDEPTEGIQPSVVAEI 170
Cdd:TIGR00956 220 IAEASLGGAKIQCWDNATRGLDSATALEF 248
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
11-192 |
5.28e-09 |
|
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: 54.68 E-value: 5.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 11 YGRSR-VLHGvdLAVPPDG-VAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGE--DV-------------TRLAPHE- 72
Cdd:cd03236 10 YGPNSfKLHR--LPVPREGqVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDwdEIldefrgselqnyfTKLLEGDv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 73 RVARGMAYVPQGQQCFPHlTAAENLRLVADarRDGAVATAEALDLfpalRPLLRRRAGLLSGGQRQQLAIARALITRPRL 152
Cdd:cd03236 88 KVIVKPQYVDLIPKAVKG-KVGELLKKKDE--RGKLDELVDQLEL----RHVLDRNIDQLSGGELQRVAIAAALARDADF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1033140466 153 LMLDEPTEGI---QPSVVAEIQERIVELTRqsgfSVLLVEQHL 192
Cdd:cd03236 161 YFFDEPSSYLdikQRLNAARLIRELAEDDN----YVLVVEHDL 199
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
15-157 |
6.37e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 54.11 E-value: 6.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 15 RVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLA-PHervargMAYVPQGQQCFPHLTA 93
Cdd:PRK13541 14 KNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAkPY------CTYIGHNLGLKLEMTV 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1033140466 94 AENLRLVADARrdGAVATAEALDLFPALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDE 157
Cdd:PRK13541 88 FENLKFWSEIY--NSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDE 149
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
15-159 |
6.61e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.12 E-value: 6.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 15 RVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVARGMAYVPQGQQCFPHLTAA 94
Cdd:PRK10982 12 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQELNLVLQRSVM 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1033140466 95 ENLRLVADARRDGAV----------ATAEALDLfpALRPllRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPT 159
Cdd:PRK10982 92 DNMWLGRYPTKGMFVdqdkmyrdtkAIFDELDI--DIDP--RAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
7-192 |
1.23e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.43 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 7 VHAgYGRSR-VLHGvdLAVPPDG-VAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDG--EDV-------------TRLA 69
Cdd:PRK13409 80 VHR-YGVNGfKLYG--LPIPKEGkVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPswDEVlkrfrgtelqnyfKKLY 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 70 PHE-RVARGMAYVPQGQQCFPHlTAAENLRLVADARRDGAVatAEALDlfpaLRPLLRRRAGLLSGGQRQQLAIARALIT 148
Cdd:PRK13409 157 NGEiKVVHKPQYVDLIPKVFKG-KVRELLKKVDERGKLDEV--VERLG----LENILDRDISELSGGELQRVAIAAALLR 229
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1033140466 149 RPRLLMLDEPTEGIqpsvvaEIQER------IVELTRqsGFSVLLVEQHL 192
Cdd:PRK13409 230 DADFYFFDEPTSYL------DIRQRlnvarlIRELAE--GKYVLVVEHDL 271
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
22-159 |
1.25e-08 |
|
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: 54.41 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 22 LAVPPDG-VAAVLGHNGAGKSTLLRVAAGLLRPSAGTV--ELDGEDV------TRLAPH-ERVARG---MAYVPQGQQCF 88
Cdd:COG1245 93 LPVPKKGkVTGILGPNGIGKSTALKILSGELKPNLGDYdeEPSWDEVlkrfrgTELQDYfKKLANGeikVAHKPQYVDLI 172
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1033140466 89 PHL---TAAENLRLVaDARrdGAVAT-AEALDlfpaLRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPT 159
Cdd:COG1245 173 PKVfkgTVRELLEKV-DER--GKLDElAEKLG----LENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPS 240
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-210 |
1.31e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 54.92 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGY---GRSrVLHGVDLAVPPDGVAAVLGHNGAGKSTLLrvaAGLLR--PSAGTVELDGEDVTRLAPHE-RVA 75
Cdd:TIGR01271 1218 MDVQGLTAKYteaGRA-VLQDLSFSVEGGQRVGLLGRTGSGKSTLL---SALLRllSTEGEIQIDGVSWNSVTLQTwRKA 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 76 RGMayVPQGQQCF---------PHLT-AAENLRLVADArrdgaVATAEALDLFP-ALRPLLRRRAGLLSGGQRQQLAIAR 144
Cdd:TIGR01271 1294 FGV--IPQKVFIFsgtfrknldPYEQwSDEEIWKVAEE-----VGLKSVIEQFPdKLDFVLVDGGYVLSNGHKQLMCLAR 1366
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1033140466 145 ALITRPRLLMLDEPTEGIQPsvvaeIQERIVELTRQSGFS---VLLVEqHLGFALRVANRYHVLESGRV 210
Cdd:TIGR01271 1367 SILSKAKILLLDEPSAHLDP-----VTLQIIRKTLKQSFSnctVILSE-HRVEALLECQQFLVIEGSSV 1429
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
19-159 |
1.80e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.10 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 19 GVDLavppDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTV--------------ELDGEDVTRlAPHERVARGMAYVPQg 84
Cdd:PLN03073 531 GIDL----DSRIAMVGPNGIGKSTILKLISGELQPSSGTVfrsakvrmavfsqhHVDGLDLSS-NPLLYMMRCFPGVPE- 604
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1033140466 85 QQCFPHLtaaenlrlvadarrdGAVATAEALdlfpALRPLLRrraglLSGGQRQQLAIARALITRPRLLMLDEPT 159
Cdd:PLN03073 605 QKLRAHL---------------GSFGVTGNL----ALQPMYT-----LSGGQKSRVAFAKITFKKPHILLLDEPS 655
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-175 |
1.96e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 54.15 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 16 VLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEdvtrlaphervargMAYVPQGQQCFPHlTAAE 95
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR--------------ISFSPQTSWIMPG-TIKD 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 96 NL--RLVADARRDGAVATA----EALDLFPALRPLLRRRAGL-LSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVA 168
Cdd:TIGR01271 506 NIifGLSYDEYRYTSVIKAcqleEDIALFPEKDKTVLGEGGItLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEK 585
|
....*..
gi 1033140466 169 EIQERIV 175
Cdd:TIGR01271 586 EIFESCL 592
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-214 |
2.09e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.21 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 17 LHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTveldgedvtrlaphERVARG-MAYVPQGQQCFpHLTAAE 95
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETS--------------SVVIRGsVAYVPQVSWIF-NATVRE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 96 NLRLVAD------ARRDGAVATAEALDLFPAL-RPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVA 168
Cdd:PLN03232 698 NILFGSDfeseryWRAIDVTALQHDLDLLPGRdLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAH 777
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1033140466 169 EIQERIVELTRQsGFSVLLVEQHLGFaLRVANRYHVLESGRVTSHG 214
Cdd:PLN03232 778 QVFDSCMKDELK-GKTRVLVTNQLHF-LPLMDRIILVSEGMIKEEG 821
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
12-209 |
2.33e-08 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 53.37 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 12 GRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPS----AGTVELDGEDVTRLAPHER---VARGMAYVPQG 84
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtADRFRWNGIDLLKLSPRERrkiIGREIAMIFQE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 85 -QQCF-PHLTAAENLRLV-------------ADARRDGAVAtaealdlfpalrplLRRRAGL-------------LSGGQ 136
Cdd:COG4170 98 pSSCLdPSAKIGDQLIEAipswtfkgkwwqrFKWRKKRAIE--------------LLHRVGIkdhkdimnsypheLTEGE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1033140466 137 RQQLAIARALITRPRLLMLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVL------ESGR 209
Cdd:COG4170 164 CQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLycgqtvESGP 242
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
26-214 |
2.80e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 53.71 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 26 PDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPH--ERVARGMAYVPQGQQCF--PHLTAA----ENL 97
Cdd:PRK10261 349 PGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGklQALRRDIQFIFQDPYASldPRQTVGdsimEPL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 98 RLVADARRDGAVATAEALDLFPALRP-LLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVAEIQERIVE 176
Cdd:PRK10261 429 RVHGLLPGKAAAARVAWLLERVGLLPeHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLD 508
|
170 180 190
....*....|....*....|....*....|....*...
gi 1033140466 177 LTRQSGFSVLLVEQHLGFALRVANRYHVLESGRVTSHG 214
Cdd:PRK10261 509 LQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-215 |
3.03e-08 |
|
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: 53.27 E-value: 3.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGL--LRPSAGTV--------------------- 58
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 59 -------ELDGEDVTRLAPHE----RVARGMAYVPQ------GQQcfphlTAAEN-LRLVADARRDGAVATAEALDLFPA 120
Cdd:TIGR03269 81 pcpvcggTLEPEEVDFWNLSDklrrRIRKRIAIMLQrtfalyGDD-----TVLDNvLEALEEIGYEGKEAVGRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 121 LRplLRRR----AGLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFAL 196
Cdd:TIGR03269 156 VQ--LSHRithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIE 233
|
250
....*....|....*....
gi 1033140466 197 RVANRYHVLESGRVTSHGD 215
Cdd:TIGR03269 234 DLSDKAIWLENGEIKEEGT 252
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
132-209 |
1.25e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 51.34 E-value: 1.25e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1033140466 132 LSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLESGR 209
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQ 236
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
32-159 |
1.26e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 51.71 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 32 VLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVARGMA---YVPQGQQCFPHLTAAENlrlVADARRDG- 107
Cdd:PRK10636 32 LVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPQPaleYVIDGDREYRQLEAQLH---DANERNDGh 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1033140466 108 AVAT--------------AEALDLFPAL---RPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPT 159
Cdd:PRK10636 109 AIATihgkldaidawtirSRAASLLHGLgfsNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPT 177
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
32-190 |
1.86e-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: 51.29 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 32 VLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDvtrlaphervarGMAYVPQGqqcfPHLTAAeNLR---LVADA----- 103
Cdd:TIGR00954 483 ICGPNGCGKSSLFRILGELWPVYGGRLTKPAKG------------KLFYVPQR----PYMTLG-TLRdqiIYPDSsedmk 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 104 RRDGAVATAEALDLFPALRPLLRRRAG---------LLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPsvvaEIQERI 174
Cdd:TIGR00954 546 RRGLSDKDLEQILDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSV----DVEGYM 621
|
170
....*....|....*.
gi 1033140466 175 VELTRQSGFSVLLVEQ 190
Cdd:TIGR00954 622 YRLCREFGITLFSVSH 637
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
31-188 |
1.87e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.78 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 31 AVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAphervargmayVPQGQQcfphLTAAE----NLRLVADARRD 106
Cdd:PRK10938 33 AFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLS-----------FEQLQK----LVSDEwqrnNTDMLSPGEDD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 107 GAVATAE---------ALDLFPA----LRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVAEIQER 173
Cdd:PRK10938 98 TGRTTAEiiqdevkdpARCEQLAqqfgITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAEL 177
|
170
....*....|....*
gi 1033140466 174 IVELTRQsGFSVLLV 188
Cdd:PRK10938 178 LASLHQS-GITLVLV 191
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-210 |
2.67e-07 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 49.85 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGY--GRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRpSAGTVELDGEDVTRLaPHERVARGMA 79
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSV-PLQKWRKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 80 YVPQGQQCF---------PHLT-AAENLRLVADArrdgaVATAEALDLFPA-LRPLLRRRAGLLSGGQRQQLAIARALIT 148
Cdd:cd03289 81 VIPQKVFIFsgtfrknldPYGKwSDEEIWKVAEE-----VGLKSVIEQFPGqLDFVLVDGGCVLSHGHKQLMCLARSVLS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1033140466 149 RPRLLMLDEPTEGIQPsvvaeIQERIVELTRQSGFS---VLLVEQHLGfALRVANRYHVLESGRV 210
Cdd:cd03289 156 KAKILLLDEPSAHLDP-----ITYQVIRKTLKQAFAdctVILSEHRIE-AMLECQRFLVIEENKV 214
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
132-192 |
3.12e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.80 E-value: 3.12e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1033140466 132 LSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHL 192
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI 1419
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
17-216 |
3.30e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 49.75 E-value: 3.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 17 LHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTV-----ELDGEDVTRLAPH----------ERVARGMAY- 80
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqAITDDNFEKLRKHigivfqnpdnQFVGSIVKYd 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 81 VPQGQQcfPHLTAAENL-RLVADARRDgaVATAEALDLFPALrpllrrraglLSGGQRQQLAIARALITRPRLLMLDEPT 159
Cdd:PRK13648 105 VAFGLE--NHAVPYDEMhRRVSEALKQ--VDMLERADYEPNA----------LSGGQKQRVAIAGVLALNPSVIILDEAT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1033140466 160 EGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGFALR-----VANRYHVLESGR---VTSHGDG 216
Cdd:PRK13648 171 SMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEadhviVMNKGTVYKEGTpteIFDHAEE 235
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
31-159 |
6.50e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.56 E-value: 6.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 31 AVLGHNGAGKSTLLRVAAGLLRPSAGTVELDgedvTRLAphervargMAYVPQGQQCF-PHLTAAENLrlvADARRDGAV 109
Cdd:PRK11147 349 ALIGPNGCGKTTLLKLMLGQLQADSGRIHCG----TKLE--------VAYFDQHRAELdPEKTVMDNL---AEGKQEVMV 413
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1033140466 110 ATAE--ALD-----LFPALRPLLRRRAglLSGGQRQQLAIARALITRPRLLMLDEPT 159
Cdd:PRK11147 414 NGRPrhVLGylqdfLFHPKRAMTPVKA--LSGGERNRLLLARLFLKPSNLLILDEPT 468
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
124-221 |
6.51e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 49.64 E-value: 6.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 124 LLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVAEIQERIVELTRQSGFSVLLVEQHLGfALRVANRYH 203
Cdd:PTZ00265 572 LVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLS-TIRYANTIF 650
|
90
....*....|....*...
gi 1033140466 204 VLESGRVTSHGDGGVTAE 221
Cdd:PTZ00265 651 VLSNRERGSTVDVDIIGE 668
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-67 |
6.91e-07 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 49.41 E-value: 6.91e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1033140466 2 LTLRGVHAGYGRSRVLHG-----VDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTR 67
Cdd:COG4615 328 LELRGVTYRYPGEDGDEGftlgpIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTA 398
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-158 |
8.50e-07 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 48.70 E-value: 8.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 16 VLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEdvtrlaphervargMAYVPQGQQCFPHlTAAE 95
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--------------ISFSSQFSWIMPG-TIKE 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 96 NL--RLVADARRDGAVATA----EALDLFPALRPLLRRRAGL-LSGGQRQQLAIARALITRPRLLMLDEP 158
Cdd:cd03291 117 NIifGVSYDEYRYKSVVKAcqleEDITKFPEKDNTVLGEGGItLSGGQRARISLARAVYKDADLYLLDSP 186
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
34-159 |
9.53e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 48.73 E-value: 9.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 34 GHNGAGKSTLLRVAAGLLRPSAGTVELDgedvtrlaPHERvargMAYVPQGQQCF------------------------- 88
Cdd:PRK15064 34 GANGCGKSTFMKILGGDLEPSAGNVSLD--------PNER----LGKLRQDQFAFeeftvldtvimghtelwevkqerdr 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 89 ----PHLTAAENLRlVAD-----ARRDGavATAEAldlfpalrpllrrRAG-LLSG---------GQRQQLA-------- 141
Cdd:PRK15064 102 iyalPEMSEEDGMK-VADlevkfAEMDG--YTAEA-------------RAGeLLLGvgipeeqhyGLMSEVApgwklrvl 165
|
170
....*....|....*...
gi 1033140466 142 IARALITRPRLLMLDEPT 159
Cdd:PRK15064 166 LAQALFSNPDILLLDEPT 183
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-58 |
1.24e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 48.35 E-value: 1.24e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1033140466 2 LTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTV 58
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
11-206 |
2.08e-06 |
|
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: 46.41 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 11 YGRSRVLhgVDLAVPPDG-VAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVtrlaphervargmAYVPQGQQcfp 89
Cdd:cd03222 10 YGVFFLL--VELGVVKEGeVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITP-------------VYKPQYID--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 90 hltaaenlrlvadarrdgavataealdlfpalrpllrrraglLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVAE 169
Cdd:cd03222 72 ------------------------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLN 109
|
170 180 190
....*....|....*....|....*....|....*..
gi 1033140466 170 IQERIVELTRQSGFSVLLVEQHLGFALRVANRYHVLE 206
Cdd:cd03222 110 AARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
16-215 |
2.33e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 47.78 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 16 VLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVARgMAYVPQGQQCFPHlTAAE 95
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSR-LAVVSQTPFLFSD-TVAN 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 96 NLRLvadARRDgavATAEALDLFPAL----RPLLR----------RRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEg 161
Cdd:PRK10789 408 NIAL---GRPD---ATQQEIEHVARLasvhDDILRlpqgydtevgERGVMLSGGQKQRISIARALLLNAEILILDDALS- 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1033140466 162 iqpSVVAEIQERIVELTRQSGFS-VLLVEQHLGFALRVANRYHVLESGRVTSHGD 215
Cdd:PRK10789 481 ---AVDGRTEHQILHNLRQWGEGrTVIISAHRLSALTEASEILVMQHGHIAQRGN 532
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
55-211 |
2.97e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.48 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 55 AGTVELDGEDVTRLAPHERVARGMAYVPQGQQcfpHL-----------TAAENLRLVA-----DARRDGAVATaealDLF 118
Cdd:NF040905 316 SGTVFKDGKEVDVSTVSDAIDAGLAYVTEDRK---GYglnliddikrnITLANLGKVSrrgviDENEEIKVAE----EYR 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 119 PALR---PLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGIqpSVVA--EIQERIVELTRQsGFSVLLVEQHLG 193
Cdd:NF040905 389 KKMNiktPSVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGI--DVGAkyEIYTIINELAAE-GKGVIVISSELP 465
|
170
....*....|....*...
gi 1033140466 194 FALRVANRYHVLESGRVT 211
Cdd:NF040905 466 ELLGMCDRIYVMNEGRIT 483
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
115-208 |
3.25e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.52 E-value: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 115 LDLFPALRPLLRrraglLSGGQRQQLAIARALIT---RPRLLMLDEPTEGIQPSVVAEIQERIVELTRQsGFSVLLVEQH 191
Cdd:PRK00635 798 LDYLPLGRPLSS-----LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQ-GHTVVIIEHN 871
|
90
....*....|....*..
gi 1033140466 192 LgFALRVANryHVLESG 208
Cdd:PRK00635 872 M-HVVKVAD--YVLELG 885
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
17-158 |
3.72e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 47.43 E-value: 3.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 17 LHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTveldgedvtrlaphERVARG-MAYVPQGQQCFpHLTAAE 95
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDA--------------SVVIRGtVAYVPQVSWIF-NATVRD 697
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1033140466 96 NLRLVAD---ARRDGAV---ATAEALDLFPA--LRPLLRRRAGlLSGGQRQQLAIARALITRPRLLMLDEP 158
Cdd:PLN03130 698 NILFGSPfdpERYERAIdvtALQHDLDLLPGgdLTEIGERGVN-ISGGQKQRVSMARAVYSNSDVYIFDDP 767
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
27-201 |
4.69e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 45.68 E-value: 4.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 27 DGVAAVLGHNGAGKSTL---LRVA-AGLLRPSA----------------GTVEL-----DGEDVT---RLApherVARGM 78
Cdd:cd03240 22 SPLTLIVGQNGAGKTTIieaLKYAlTGELPPNSkggahdpkliregevrAQVKLafenaNGKKYTitrSLA----ILENV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 79 AYVPQGQQCfphltaaenlrlvadarrdgavataealdlfpalRPLLRRRaGLLSGGQRQ------QLAIARALITRPRL 152
Cdd:cd03240 98 IFCHQGESN----------------------------------WPLLDMR-GRCSGGEKVlasliiRLALAETFGSNCGI 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1033140466 153 LMLDEPTEGIQPSVVAEIQERIVELTR-QSGFSVLLV------EQHLGFALRVANR 201
Cdd:cd03240 143 LALDEPTTNLDEENIEESLAEIIEERKsQKNFQLIVIthdeelVDAADHIYRVEKD 198
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-229 |
5.85e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 46.70 E-value: 5.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 16 VLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVeldgedvtrlapheRVARGMAYVPQgQQCFPHLTAAE 95
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV--------------WAERSIAYVPQ-QAWIMNATVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 96 NL---------RLvADARRdgaVATAEA-LDLFPA-LRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQp 164
Cdd:PTZ00243 740 NIlffdeedaaRL-ADAVR---VSQLEAdLAQLGGgLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALD- 814
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 165 svvAEIQERIVE---LTRQSGFS-VLLVEQ-HLgfaLRVANRYHVLESGRVTSHGDGGVTAEREVRAALA 229
Cdd:PTZ00243 815 ---AHVGERVVEecfLGALAGKTrVLATHQvHV---VPRADYVVALGDGRVEFSGSSADFMRTSLYATLA 878
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-159 |
1.27e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 45.71 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 1 MLTLRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGE-DVTRLA---P-HER-- 73
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDlIVARLQqdpPrNVEgt 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 74 ----VARGMAYVPQGQQCFPHLtaaenLRLVADARRDGAVA-----------------------TAEALDLfPALRPLLR 126
Cdd:PRK11147 83 vydfVAEGIEEQAEYLKRYHDI-----SHLVETDPSEKNLNelaklqeqldhhnlwqlenrineVLAQLGL-DPDAALSS 156
|
170 180 190
....*....|....*....|....*....|...
gi 1033140466 127 rraglLSGGQRQQLAIARALITRPRLLMLDEPT 159
Cdd:PRK11147 157 -----LSGGWLRKAALGRALVSNPDVLLLDEPT 184
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-214 |
1.54e-05 |
|
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: 45.32 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 16 VLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVARgMAYVPQGQQCFphltaAE 95
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFK-ITIIPQDPVLF-----SG 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 96 NLRLVAD---ARRDGAVATAEAL----DLFPALRPLLRRRAGL----LSGGQRQQLAIARALITRPRLLMLDEPTEGIQP 164
Cdd:TIGR00957 1375 SLRMNLDpfsQYSDEEVWWALELahlkTFVSALPDKLDHECAEggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDL 1454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1033140466 165 SVVAEIQERIveLTRQSGFSVLLVEQHLGFALRVaNRYHVLESGRVTSHG 214
Cdd:TIGR00957 1455 ETDNLIQSTI--RTQFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEVAEFG 1501
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
4-164 |
1.72e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.01 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 4 LRGVHAGYGRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLlRPSAGTVEL--------DGEDVTRLAPHerva 75
Cdd:PRK10938 263 LNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGD-HPQGYSNDLtlfgrrrgSGETIWDIKKH---- 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 76 rgMAYVPQGQqcfpHL-----TAAENLRL------------VADARRDGAvatAEALDLFPALRPLLRRRAGLLSGGQRQ 138
Cdd:PRK10938 338 --IGYVSSSL----HLdyrvsTSVRNVILsgffdsigiyqaVSDRQQKLA---QQWLDILGIDKRTADAPFHSLSWGQQR 408
|
170 180
....*....|....*....|....*.
gi 1033140466 139 QLAIARALITRPRLLMLDEPTEGIQP 164
Cdd:PRK10938 409 LALIVRALVKHPTLLILDEPLQGLDP 434
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-157 |
5.97e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 43.42 E-value: 5.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGYGRSRVLHG-VDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHERVARGMAY 80
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGpINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 81 V-----------PQGQQCFPHLTAA--ENLRLVADAR-RDGAVATAEaldlfpalrpllrrraglLSGGQRQQLAIARAL 146
Cdd:PRK10522 403 FtdfhlfdqllgPEGKPANPALVEKwlERLKMAHKLElEDGRISNLK------------------LSKGQKKRLALLLAL 464
|
170
....*....|.
gi 1033140466 147 ITRPRLLMLDE 157
Cdd:PRK10522 465 AEERDILLLDE 475
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
125-192 |
7.42e-05 |
|
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: 41.92 E-value: 7.42e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 125 LRRRAGLLSGGQRQQLAIARALITRPR--LLMLDEPTEGIQPSVVAEIQERIVELtRQSGFSVLLVEQHL 192
Cdd:cd03238 81 LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGL-IDLGNTVILIEHNL 149
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
2-203 |
1.53e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 42.46 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 2 LTLRGVHAGY--GRSRVLHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEDVTRLAPHErVARGMA 79
Cdd:PTZ00243 1309 LVFEGVQMRYreGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRE-LRRQFS 1387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 80 YVPQGQQCF---------PHLTA--AE---NLRLVadARRDGAVATAEALDlfpalrpllrrrAGLLSG------GQRQQ 139
Cdd:PTZ00243 1388 MIPQDPVLFdgtvrqnvdPFLEAssAEvwaALELV--GLRERVASESEGID------------SRVLEGgsnysvGQRQL 1453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1033140466 140 LAIARALITRPR-LLMLDEPTEGIQPSVVAEIQErivelTRQSGFSVLLVeqhlgfaLRVANRYH 203
Cdd:PTZ00243 1454 MCMARALLKKGSgFILMDEATANIDPALDRQIQA-----TVMSAFSAYTV-------ITIAHRLH 1506
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
126-159 |
1.69e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.15 E-value: 1.69e-04
10 20 30
....*....|....*....|....*....|....
gi 1033140466 126 RRRAGLLSGGQRQQLAIARALITRPRLLMLDEPT 159
Cdd:PLN03073 339 VKATKTFSGGWRMRIALARALFIEPDLLLLDEPT 372
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
17-62 |
2.45e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 41.80 E-value: 2.45e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1033140466 17 LHGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDG 62
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG 85
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
27-146 |
3.59e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 40.38 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 27 DGVAAVLGHNGAGKSTLLR-VAAGLLRPSAGTVELDGEDVTRLAPHERV-----ARGMAYV---PQGQQCFP-------- 89
Cdd:COG0419 23 DGLNLIVGPNGAGKSTILEaIRYALYGKARSRSKLRSDLINVGSEEASVelefeHGGKRYRierRQGEFAEFleakpser 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1033140466 90 --------HLTAAENLRLVADARRDGAVATAEALDLFPALR-PLLRRRAGL-----LSGGQRQQLAIARAL 146
Cdd:COG0419 103 kealkrllGLEIYEELKERLKELEEALESALEELAELQKLKqEILAQLSGLdpietLSGGERLRLALADLL 173
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
29-215 |
1.18e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 39.03 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 29 VAAVLGHNGAGKSTLLRVAAGLLRPSAGTVELDGEdVTRLApherVARGMayvpQGQqcfphLTAAENLR----LVADAR 104
Cdd:PRK13546 52 VIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-VSVIA----ISAGL----SGQ-----LTGIENIEfkmlCMGFKR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 105 RDGAVATAEALDlFPALRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVAEIQERIVELTRQsGFS 184
Cdd:PRK13546 118 KEIKAMTPKIIE-FSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQ-NKT 195
|
170 180 190
....*....|....*....|....*....|.
gi 1033140466 185 VLLVEQHLGFALRVANRYHVLESGRVTSHGD 215
Cdd:PRK13546 196 IFFVSHNLGQVRQFCTKIAWIEGGKLKDYGE 226
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
127-198 |
1.32e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.43 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 127 RRAGLLSGGQRQQLAIARAL------ITrprlLMLDEPTEGIQPSVVAEIQERIVELtRQSGFSVLLVE---QHLGFALR 197
Cdd:PRK00635 472 RALATLSGGEQERTALAKHLgaeligIT----YILDEPSIGLHPQDTHKLINVIKKL-RDQGNTVLLVEhdeQMISLADR 546
|
.
gi 1033140466 198 V 198
Cdd:PRK00635 547 I 547
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
26-177 |
2.59e-03 |
|
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: 37.35 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033140466 26 PDGVAAVLGHNGAGKSTLLRVAAGLL-RPSAGTVELDGEDVTRLAPHERvargmayvpqgqqcfphltaaenlrlvadar 104
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELgPPGGGVIYIDGEDILEEVLDQL------------------------------- 49
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1033140466 105 rdgavataealdlfpaLRPLLRRRAGLLSGGQRQQLAIARALITRPRLLMLDEPTEGIQPSVVAEIQERIVEL 177
Cdd:smart00382 50 ----------------LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELR 106
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
18-55 |
2.69e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 35.27 E-value: 2.69e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1033140466 18 HGVDLAVPPDGVAAVLGHNGAGKSTLLRVAAGLLRPSA 55
Cdd:pfam13555 13 DGHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVPAK 50
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| CYP77_89 |
cd11075 |
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ... |
86-154 |
3.31e-03 |
|
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes cytochrome P450 families 73 (CYP77) and 89 (CYP89), which are sister families that share a common ancestor. CYP89, present only in angiosperms, is younger than CYP77, which is already found in lycopods; thus, CYP89 may have evolved from CYP77 after duplication and divergence. Also included in this group is ent-kaurene oxidase, called CYP701A3 in Arabidopsis thaliana and CYP701B1 in Physcomitrella patens, that catalyzes the oxidation of ent-kaurene to form ent-kaurenoic acid. CYP701A3 is sensitive to inhibitor uniconazole-P while CYP701B1 is not. This CYP77/89 group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.
Pssm-ID: 410698 [Multi-domain] Cd Length: 433 Bit Score: 37.99 E-value: 3.31e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1033140466 86 QCFPHLTAAENLRLVADARRDGAVATAEA--LDLFPALRPLL-RRRAGLLSGGQRQQLAIARALITRPRLLM 154
Cdd:cd11075 127 MCFGERLDEETVRELERVQRELLLSFTDFdvRDFFPALTWLLnRRRWKKVLELRRRQEEVLLPLIRARRKRR 198
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