|
Name |
Accession |
Description |
Interval |
E-value |
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
2-232 |
3.52e-139 |
|
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: 389.19 E-value: 3.52e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVREGLAYV 81
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 82 PQGRDIFSTLTVEENILIGMAKFKGAKtRKVPEHLYEIFPILDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDEPT 161
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTGLAALPRRS-RKIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1832152097 162 EGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREMPEKGIRELVAI 232
Cdd:TIGR03410 160 EGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDKVRRYLAV 230
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-221 |
3.62e-113 |
|
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: 323.47 E-value: 3.62e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVREGLAY 80
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 81 VPQGRDIFSTLTVEENILIGMAKFKG-AKTRKVPEHLYEIFPILDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDE 159
Cdd:COG0410 83 VPEGRRIFPSLTVEENLLLGAYARRDrAEVRADLERVYELFPRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1832152097 160 PTEGIQPSIIKDIGRVIRKLADSGeMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREM 221
Cdd:COG0410 163 PSLGLAPLIVEEIFEIIRRLNREG-VTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-221 |
1.27e-109 |
|
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: 313.99 E-value: 1.27e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVREGLAYV 81
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 82 PQGRDIFSTLTVEENILIGMAKFKGAKTRKVPEHLYEIFPILDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDEPT 161
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 162 EGIQPSIIKDIGRVIRKLADSGeMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREM 221
Cdd:cd03224 161 EGLAPKIVEEIFEAIRELRDEG-VTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-216 |
6.96e-57 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 180.64 E-value: 6.96e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEqrVREGLAYV 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE--VRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 82 PQGRDIFSTLTVEENILIgMAKFKGAKTRKVPEHLYEIFPI--LDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDE 159
Cdd:COG1131 79 PQEPALYPDLTVRENLRF-FARLYGLPRKEARERIDELLELfgLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1832152097 160 PTEGIQPSIIKDIGRVIRKLADSGeMAIVLVEQFYDFAEELADGYTVMARGQVIAQG 216
Cdd:COG1131 158 PTSGLDPEARRELWELLRELAAEG-KTVLLSTHYLEEAERLCDRVAIIDKGRIVADG 213
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-216 |
1.65e-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: 179.56 E-value: 1.65e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVREGLAYV 81
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 82 PQGRDIFSTLTVEENILIGMAKFKG------AKTRKVPEHLYEIFPILDEMK-----QRRGGDLSGGQQQQLAIARALAS 150
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAQARTGsglllaRARREEREARERAEELLERVGladlaDRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1832152097 151 EPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGeMAIVLVEQFYDFAEELADGYTVMARGQVIAQG 216
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRERG-ITVLLVEHDMDVVMSLADRVTVLDQGRVIAEG 225
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-216 |
1.06e-55 |
|
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: 178.31 E-value: 1.06e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVREGLAY 80
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLGIAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 81 ---VPQgrdIFSTLTVEENILIGM-----------------AKFKGAKTRKVPEHLYEIFPiLDEMKQRRGGDLSGGQQQ 140
Cdd:COG0411 84 tfqNPR---LFPELTVLENVLVAAharlgrgllaallrlprARREEREARERAEELLERVG-LADRADEPAGNLSYGQQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1832152097 141 QLAIARALASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQG 216
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEG 235
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-216 |
4.57e-53 |
|
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: 171.19 E-value: 4.57e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEqrVREGLAY 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE--ARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 81 VPQGRDIFSTLTVEENILIgMAKFKGAKTRKVPEHLYEIFP--ILDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILD 158
Cdd:COG4555 79 LPDERGLYDRLTVRENIRY-FAELYGLFDEELKKRIEELIEllGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1832152097 159 EPTEGIQPSIIKDIGRVIRKLADSGEMaIVLVEQFYDFAEELADGYTVMARGQVIAQG 216
Cdd:COG4555 158 EPTNGLDVMARRLLREILRALKKEGKT-VLFSSHIMQEVEALCDRVVILHKGKVVAQG 214
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-217 |
2.91e-52 |
|
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: 169.45 E-value: 2.91e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVREgLAY 80
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARR-IAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 81 VPQGRDIFSTLTVEENILIGMAKFKGAkTRKVPEHLYEIfpI--------LDEMKQRRGGDLSGGQQQQLAIARALASEP 152
Cdd:COG1120 80 VPQEPPAPFGLTVRELVALGRYPHLGL-FGRPSAEDREA--VeealertgLEHLADRPVDELSGGERQRVLIARALAQEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1832152097 153 KVLILDEPTEGIqpsiikDIG------RVIRKLADSGEMAIVLV----EQFYDFAEELAdgytVMARGQVIAQGA 217
Cdd:COG1120 157 PLLLLDEPTSHL------DLAhqlevlELLRRLARERGRTVVMVlhdlNLAARYADRLV----LLKDGRIVAQGP 221
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-218 |
3.40e-48 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 158.50 E-value: 3.40e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVREGLAY 80
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 81 VPQGRDIFSTLTVEENILIGMAKFKGAKTRKVPEHLYEIFPILDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDEP 160
Cdd:PRK11614 85 VPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1832152097 161 TEGIQPSIIKDIGRVIRKLADSGeMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAG 218
Cdd:PRK11614 165 SLGLAPIIIQQIFDTIEQLREQG-MTIFLVEQNANQALKLADRGYVLENGHVVLEDTG 221
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-212 |
3.67e-48 |
|
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: 156.02 E-value: 3.67e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEqrVREGLAYV 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE--VKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 82 PQGRDIFSTLTVEENIligmakfkgaktrkvpehlyeifpildemkqrrggDLSGGQQQQLAIARALASEPKVLILDEPT 161
Cdd:cd03230 79 PEEPSLYENLTVRENL-----------------------------------KLSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1832152097 162 EGIQPSIIKDIGRVIRKLADSGeMAIVLVEQFYDFAEELADGYTVMARGQV 212
Cdd:cd03230 124 SGLDPESRREFWELLRELKKEG-KTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-216 |
3.52e-47 |
|
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: 154.98 E-value: 3.52e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRvreGLAYV 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERR---NIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 82 PQGRDIFSTLTVEENILIGMAKFKGAK---TRKVPEHLYEIfpILDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILD 158
Cdd:cd03259 78 FQDYALFPHLTVAENIAFGLKLRGVPKaeiRARVRELLELV--GLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1832152097 159 EPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQG 216
Cdd:cd03259 156 EPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-217 |
8.58e-47 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 154.86 E-value: 8.58e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDIsrlspeQRVREGLAY 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP------RRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 81 VPQGRDIFST--LTVEENILIGMAKFKGAKTRKVPEHLYEIFPILDEM-----KQRRGGDLSGGQQQQLAIARALASEPK 153
Cdd:COG1121 80 VPQRAEVDWDfpITVRDVVLMGRYGRRGLFRRPSRADREAVDEALERVgledlADRPIGELSGGQQQRVLLARALAQDPD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1832152097 154 VLILDEPTEGIQPSIIKDIGRVIRKLADSGeMAIVLVEQFYDFAEELADGYTVMARGqVIAQGA 217
Cdd:COG1121 160 LLLLDEPFAGVDAATEEALYELLRELRREG-KTILVVTHDLGAVREYFDRVLLLNRG-LVAHGP 221
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-221 |
3.63e-46 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 153.23 E-value: 3.63e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPE-QRVREGLA 79
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDiNKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 80 YVPQGRDIFSTLTVEENILIGMAKFKG---AKTRKVPEHLYEIFPILDEMkQRRGGDLSGGQQQQLAIARALASEPKVLI 156
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPIKVKKmskAEAEERAMELLERVGLADKA-DAYPAQLSGGQQQRVAIARALAMEPKVML 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1832152097 157 LDEPTEGIQPSIIKDIGRVIRKLADSGeMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREM 221
Cdd:COG1126 160 FDEPTSALDPELVGEVLDVMRDLAKEG-MTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEF 223
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-216 |
7.31e-46 |
|
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: 150.66 E-value: 7.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 3 EVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVREgLAYVP 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARK-IAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 83 QgrdifstltveeniliGMAKFKgaktrkvpehlyeifpiLDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDEPTE 162
Cdd:cd03214 80 Q----------------ALELLG-----------------LAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1832152097 163 GIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQG 216
Cdd:cd03214 127 HLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-183 |
2.00e-45 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 151.34 E-value: 2.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSHILRDVSFQapVGACSVV--LGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVREGL 78
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLE--VNQGEIVglLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 79 AYVPQGRDIFSTLTVEENILI--GMAKFKGAKTRKVPEHLYEIFPIlDEMKQRRGGDLSGGQQQQLAIARALASEPKVLI 156
Cdd:COG1137 81 GYLPQEASIFRKLTVEDNILAvlELRKLSKKEREERLEELLEEFGI-THLRKSKAYSLSGGERRRVEIARALATNPKFIL 159
|
170 180
....*....|....*....|....*..
gi 1832152097 157 LDEPTEGIQPSIIKDIGRVIRKLADSG 183
Cdd:COG1137 160 LDEPFAGVDPIAVADIQKIIRHLKERG 186
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-220 |
3.92e-45 |
|
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: 150.18 E-value: 3.92e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFY-GGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPeQRVREGLAY 80
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNL-RELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 81 VPQGRD--IFSTlTVEENILIGMA--KFKGAKTRKVPEHLYEIFPiLDEMKQRRGGDLSGGQQQQLAIARALASEPKVLI 156
Cdd:COG1122 80 VFQNPDdqLFAP-TVEEDVAFGPEnlGLPREEIRERVEEALELVG-LEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1832152097 157 LDEPTEGIQPSIIKDIGRVIRKLADSGeMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGRE 220
Cdd:COG1122 158 LDEPTAGLDPRGRRELLELLKRLNKEG-KTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPRE 220
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-216 |
8.85e-45 |
|
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: 148.84 E-value: 8.85e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 3 EVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKdisrlsPEQRVREGLAYVP 82
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK------PLEKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 83 QGRDIFST--LTVEENILIGMAKFKG------AKTRKVPEHLYEiFPILDEMKQRRGGDLSGGQQQQLAIARALASEPKV 154
Cdd:cd03235 75 QRRSIDRDfpISVRDVVLMGLYGHKGlfrrlsKADKAKVDEALE-RVGLSELADRQIGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1832152097 155 LILDEPTEGIQPSIIKDIGRVIRKLADSGeMAIVLVEQFYDFAEELADGYTVMARGqVIAQG 216
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLRELRREG-MTILVVTHDLGLVLEYFDRVLLLNRT-VVASG 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-221 |
4.12e-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: 148.03 E-value: 4.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPE--QRVREGLA 79
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 80 YVPQGRDIFSTLTVEENILIGM----AKFKGAKTRKVPEHLYEIFpiLDEMKQRRGGDLSGGQQQQLAIARALASEPKVL 155
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLrehtRLSEEEIREIVLEKLEAVG--LRGAEDLYPAELSGGMKKRVALARALALDPELL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1832152097 156 ILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREM 221
Cdd:cd03261 159 LYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-211 |
6.67e-44 |
|
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: 146.46 E-value: 6.67e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 3 EVKDVNQFYGGSH--ILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRvREGLAY 80
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKEL-RRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 81 VPQG-RDIFSTLTVEENILIGM--AKFKGAKTRKVPEHLYEIFpILDEMKQRRGGDLSGGQQQQLAIARALASEPKVLIL 157
Cdd:cd03225 80 VFQNpDDQFFGPTVEEEVAFGLenLGLPEEEIEERVEEALELV-GLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1832152097 158 DEPTEGIQPSIIKDIGRVIRKLADSGeMAIVLVEQFYDFAEELADGYTVMARGQ 211
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKAEG-KTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-212 |
7.78e-44 |
|
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: 146.52 E-value: 7.78e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPE-QRVREGLAY 80
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNiNELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 81 VPQGRDIFSTLTVEENILIGMAKFKGAKTRKVPEHLYEIFPI--LDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILD 158
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKvgLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1832152097 159 EPTEGIQPSIIKDIGRVIRKLADSGeMAIVLVEQFYDFAEELADGYTVMARGQV 212
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEEG-MTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-216 |
1.23e-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: 146.66 E-value: 1.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQR--VREGL 78
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELyeLRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 79 AYVPQGRDIFSTLTVEENILIGMAKFkgaktRKVPEHlyEIFPI---------LDEMKQRRGGDLSGGQQQQLAIARALA 149
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVAFPLREH-----TDLSEA--EIRELvleklelvgLPGAADKMPSELSGGMRKRVALARALA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1832152097 150 SEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQG 216
Cdd:COG1127 158 LDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEG 224
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-216 |
1.91e-43 |
|
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: 145.73 E-value: 1.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGS--HILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDIsrLSPEQRVREGLA 79
Cdd:cd03263 1 LQIRNLTKTYKKGtkPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI--RTDRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 80 YVPQGRDIFSTLTVEENILIgMAKFKG---AKTRKVPEHLYEIFPILDEMKqRRGGDLSGGQQQQLAIARALASEPKVLI 156
Cdd:cd03263 79 YCPQFDALFDELTVREHLRF-YARLKGlpkSEIKEEVELLLRVLGLTDKAN-KRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 157 LDEPTEGIQPSIIKDIGRVIRKLadSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQG 216
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-221 |
3.62e-43 |
|
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: 145.38 E-value: 3.62e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHILRDVSFQapVGACSVV--LGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVREGLA 79
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLS--VKQGEIVglLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 80 YVPQGRDIFSTLTVEENILIGM--AKFKGAKTRKVPEHLYEIFPIlDEMKQRRGGDLSGGQQQQLAIARALASEPKVLIL 157
Cdd:cd03218 79 YLPQEASIFRKLTVEENILAVLeiRGLSKKEREEKLEELLEEFHI-THLRKSKASSLSGGERRRVEIARALATNPKFLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1832152097 158 DEPTEGIQPSIIKDIGRVIRKLADSGeMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREM 221
Cdd:cd03218 158 DEPFAGVDPIAVQDIQKIIKILKDRG-IGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEI 220
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-211 |
4.44e-43 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 143.48 E-value: 4.44e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRV-REGLAY 80
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPlRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 81 VPQGRDIFSTLTVEENILIGmakfkgaktrkvpehlyeifpildemkqrrggdLSGGQQQQLAIARALASEPKVLILDEP 160
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG---------------------------------LSGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1832152097 161 TEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQ 211
Cdd:cd03229 128 TSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-188 |
2.25e-42 |
|
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: 142.62 E-value: 2.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEqrVREGLAY 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED--YRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 81 VPQGRDIFSTLTVEENiLIGMAKFKGAK-TRKVPEHLYEIFpILDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDE 159
Cdd:COG4133 80 LGHADGLKPELTVREN-LRFWAALYGLRaDREAIDEALEAV-GLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180
....*....|....*....|....*....
gi 1832152097 160 PTEGIQPSIIKDIGRVIRKLADSGEMAIV 188
Cdd:COG4133 158 PFTALDAAGVALLAELIAAHLARGGAVLL 186
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-229 |
5.36e-42 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 142.89 E-value: 5.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVN-QFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPE--QRVREG 77
Cdd:COG3638 2 MLELRNLSkRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRalRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 78 LAYVPQGRDIFSTLTVEENILIG----MAKFKGAkTRKVPEHLYEI-FPILD-----EMKQRRGGDLSGGQQQQLAIARA 147
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVLAGrlgrTSTWRSL-LGLFPPEDRERaLEALErvglaDKAYQRADQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 148 LASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREMPEKGIR 227
Cdd:COG3638 161 LVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAELTDAVLR 240
|
..
gi 1832152097 228 EL 229
Cdd:COG3638 241 EI 242
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-226 |
9.18e-42 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 147.86 E-value: 9.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVREGLAY 80
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAGIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 81 VPQGRDIFSTLTVEENILIGMAKFKG---------AKTRKvpehlyeifpILDEMK-----QRRGGDLSGGQQQQLAIAR 146
Cdd:COG1129 84 IHQELNLVPNLSVAENIFLGREPRRGglidwramrRRARE----------LLARLGldidpDTPVGDLSVAQQQLVEIAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 147 ALASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGeMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREMPEKGI 226
Cdd:COG1129 154 ALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQG-VAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDEL 232
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-231 |
1.43e-41 |
|
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: 141.32 E-value: 1.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHiLRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRvreGLAYV 81
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKR---DISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 82 PQGRDIFSTLTVEENILIGMAKFKGAKtRKVPEHLYEIFPIL--DEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDE 159
Cdd:cd03299 77 PQNYALFPHMTVYKNIAYGLKKRKVDK-KEIERKVLEIAEMLgiDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1832152097 160 PTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREMPEKGIRELVA 231
Cdd:cd03299 156 PFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVA 227
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-160 |
1.92e-41 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 144.09 E-value: 1.92e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRvreGLAY 80
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKR---NVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 81 VPQGRDIFSTLTVEENILIG--MAKF-KGAKTRKVPEHLyEIFPiLDEMKQRRGGDLSGGQQQQLAIARALASEPKVLIL 157
Cdd:COG3842 82 VFQDYALFPHLTVAENVAFGlrMRGVpKAEIRARVAELL-ELVG-LEGLADRYPHQLSGGQQQRVALARALAPEPRVLLL 159
|
...
gi 1832152097 158 DEP 160
Cdd:COG3842 160 DEP 162
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-220 |
3.57e-41 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 146.59 E-value: 3.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGS-----HILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQR-- 73
Cdd:COG1123 260 LLEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLre 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 74 VREGLAYVPQgrDIFSTL----TVEENILIGMAKFKGAKTRKVPEHLYEIfpiLD------EMKQRRGGDLSGGQQQQLA 143
Cdd:COG1123 340 LRRRVQMVFQ--DPYSSLnprmTVGDIIAEPLRLHGLLSRAERRERVAEL---LErvglppDLADRYPHELSGGQRQRVA 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1832152097 144 IARALASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGRE 220
Cdd:COG1123 415 IARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEE 491
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-221 |
4.41e-41 |
|
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: 139.81 E-value: 4.41e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEqrVREGLAYV 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE--VRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 82 PQGRDIFSTLTVEENILIgMAKFKGAKTRKVPEHLYEIFPILD--EMKQRRGGDLSGGQQQQLAIARALASEPKVLILDE 159
Cdd:cd03265 79 FQDLSVDDELTGWENLYI-HARLYGVPGAERRERIDELLDFVGllEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1832152097 160 PTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREM 221
Cdd:cd03265 158 PTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-190 |
6.09e-41 |
|
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: 139.16 E-value: 6.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGG----SHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRV--- 74
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 75 REGLAYVPQGRDIFSTLTVEENILIGM--AKFKGAKTRKVPEHLYEIFPILDEMKqRRGGDLSGGQQQQLAIARALASEP 152
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLllAGVPKKERRERAEELLERVGLGDRLN-HYPSELSGGQQQRVAIARALANDP 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 1832152097 153 KVLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLV 190
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVV 197
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-216 |
1.47e-40 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 138.47 E-value: 1.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIK-----SGQILLDGKDISRLSPE-QRVR 75
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGKDIYDLDVDvLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 76 EGLAYVPQGRDIFStLTVEENILIGmAKFKGAKTRKVP----EHLYEIFPILDEMKQR-RGGDLSGGQQQQLAIARALAS 150
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYG-LRLHGIKLKEELdervEEALRKAALWDEVKDRlHALGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 151 EPKVLILDEPTEGIQPSIIKDIGRVIRKLADsgEMAIVLV----EQfydfAEELADGYTVMARGQVIAQG 216
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKK--EYTIVIVthnmQQ----AARVADRTAFLLNGRLVEFG 222
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-216 |
3.21e-40 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 137.64 E-value: 3.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGS----HILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQR--V 74
Cdd:cd03257 1 LLEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkiR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 75 REGLAYVPQgrDIFSTL----TVEENI-----LIGMAKFKGAKTRKVPEHLyEIFPILDEMKQRRGGDLSGGQQQQLAIA 145
Cdd:cd03257 81 RKEIQMVFQ--DPMSSLnprmTIGEQIaeplrIHGKLSKKEARKEAVLLLL-VGVGLPEEVLNRYPHELSGGQRQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1832152097 146 RALASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQG 216
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-220 |
4.70e-40 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 140.28 E-value: 4.70e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDI-SRLSPEQRvreGLAY 80
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRER---RVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 81 VPQGRDIFSTLTVEENILIGMAK---FKGAKTRKVPEHLYEIFpiLDEMKQRRGGDLSGGQQQQLAIARALASEPKVLIL 157
Cdd:COG1118 80 VFQHYALFPHMTVAENIAFGLRVrppSKAEIRARVEELLELVQ--LEGLADRYPSQLSGGQRQRVALARALAVEPEVLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1832152097 158 DEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLV----EQFYDFAEELAdgytVMARGQVIAQGAGRE 220
Cdd:COG1118 158 DEPFGALDAKVRKELRRWLRRLHDELGGTTVFVthdqEEALELADRVV----VMNQGRIEQVGTPDE 220
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-221 |
1.19e-39 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 142.73 E-value: 1.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFY--GGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIK---SGQILLDGKDISRLSPEQRVR 75
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 76 EgLAYVPQGRDI-FSTLTVEENILIGMAKFKGAKT---RKVPEHLYEIFpiLDEMKQRRGGDLSGGQQQQLAIARALASE 151
Cdd:COG1123 84 R-IGMVFQDPMTqLNPVTVGDQIAEALENLGLSRAearARVLELLEAVG--LERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 152 PKVLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREM 221
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-211 |
2.51e-39 |
|
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: 133.14 E-value: 2.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 3 EVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQrVREGLAYVP 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEE-LRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 83 QgrdifstltveeniligmakfkgaktrkvpehlyeifpildemkqrrggdLSGGQQQQLAIARALASEPKVLILDEPTE 162
Cdd:cd00267 80 Q--------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1832152097 163 GIQPSIIKDIGRVIRKLADSGeMAIVLVEQFYDFAEELADGYTVMARGQ 211
Cdd:cd00267 110 GLDPASRERLLELLRELAEEG-RTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-161 |
2.88e-39 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 132.77 E-value: 2.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 17 LRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRvREGLAYVPQGRDIFSTLTVEEN 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSL-RKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1832152097 97 ILIGmAKFKGAKTRKVPEHLYEI---FPILDEMKQR---RGGDLSGGQQQQLAIARALASEPKVLILDEPT 161
Cdd:pfam00005 80 LRLG-LLLKGLSKREKDARAEEAlekLGLGDLADRPvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-190 |
3.09e-39 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 135.17 E-value: 3.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGS----HILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRV-- 74
Cdd:COG1136 4 LLELRNLTKSYGTGegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELArl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 75 -REGLAYVPQGRDIFSTLTVEENILIGMaKFKGAKTRKVPEHLYEIFPI--LDEMKQRRGGDLSGGQQQQLAIARALASE 151
Cdd:COG1136 84 rRRHIGFVFQFFNLLPELTALENVALPL-LLAGVSRKERRERARELLERvgLGDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1832152097 152 PKVLILDEPT------EGiqpsiiKDIGRVIRKLADSGEMAIVLV 190
Cdd:COG1136 163 PKLILADEPTgnldskTG------EEVLELLRELNRELGTTIVMV 201
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-190 |
8.51e-38 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 130.71 E-value: 8.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQrVREGLAYV 81
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPE-WRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 82 PQGRDIFSTlTVEENILIGMAKFKGAKTRKVPEHLYEIFPILDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDEPT 161
Cdd:COG4619 80 PQEPALWGG-TVRDNLPFPFQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180
....*....|....*....|....*....
gi 1832152097 162 EGIQPSIIKDIGRVIRKLADSGEMAIVLV 190
Cdd:COG4619 159 SALDPENTRRVEELLREYLAEEGRAVLWV 187
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-229 |
1.41e-37 |
|
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: 131.15 E-value: 1.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGS-HILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSP--EQRVREGL 78
Cdd:cd03256 1 IEVENLSKTYPNGkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGkaLRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 79 AYVPQGRDIFSTLTVEENILIG----MAKFKGAKTRKVPEHLYEIFPILD-----EMKQRRGGDLSGGQQQQLAIARALA 149
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGrlgrRSTWRSLFGLFPKEEKQRALAALErvgllDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 150 SEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREMPEKGIREL 229
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEVLDEI 240
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-224 |
2.27e-37 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 130.54 E-value: 2.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRvreGLAYV 81
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER---NVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 82 PQGRDIFSTLTVEENILIGMaKFKGAKTR--------KVPEHLYeiFPILDEMKQRRGGDLSGGQQQQLAIARALASEPK 153
Cdd:cd03296 80 FQHYALFRHMTVFDNVAFGL-RVKPRSERppeaeiraKVHELLK--LVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1832152097 154 VLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREMPEK 224
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDH 227
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-160 |
2.83e-37 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 133.27 E-value: 2.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRvreGLAY 80
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDR---NIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 81 VPQGRDIFSTLTVEENILIG--MAKFKGA----KTRKVPEHLyEIFPILDemkqRRGGDLSGGQQQQLAIARALASEPKV 154
Cdd:COG3839 80 VFQSYALYPHMTVYENIAFPlkLRKVPKAeidrRVREAAELL-GLEDLLD----RKPKQLSGGQRQRVALGRALVREPKV 154
|
....*.
gi 1832152097 155 LILDEP 160
Cdd:COG3839 155 FLLDEP 160
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-213 |
2.97e-37 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 129.30 E-value: 2.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 3 EVKDVN-QFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRlspEQRVREGlAYV 81
Cdd:cd03226 1 RIENISfSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSI-GYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 82 PQG-RDIFSTLTVEENILIGM--AKFKGAKTRKVPEHLYeifpiLDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILD 158
Cdd:cd03226 77 MQDvDYQLFTDSVREELLLGLkeLDAGNEQAETVLKDLD-----LYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1832152097 159 EPTEGIQPSIIKDIGRVIRKLADSGEmAIVLVEQFYDFAEELADGYTVMARGQVI 213
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRELAAQGK-AVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-215 |
6.43e-37 |
|
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: 127.16 E-value: 6.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVREGLAYV 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 82 PQgrdifstltveeniligmakfkgaktrkvpehlyeifpildemkqrrggdLSGGQQQQLAIARALASEPKVLILDEPT 161
Cdd:cd03216 81 YQ--------------------------------------------------LSVGERQMVEIARALARNARLLILDEPT 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1832152097 162 EGIQPSIIKDIGRVIRKLADSGeMAIVLVEQFYDFAEELADGYTVMARGQVIAQ 215
Cdd:cd03216 111 AALTPAEVERLFKVIRRLRAQG-VAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-229 |
6.92e-37 |
|
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: 129.34 E-value: 6.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYG-GSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPE--QRVREG 77
Cdd:TIGR02315 1 MLEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKklRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 78 LAYVPQGRDIFSTLTVEENILIG-----------MAKFKGAKTRKVPEHLYEIFpiLDEMKQRRGGDLSGGQQQQLAIAR 146
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHGrlgykptwrslLGRFSEEDKERALSALERVG--LADKAYQRADQLSGGQQQRVAIAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 147 ALASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREMPEKGI 226
Cdd:TIGR02315 159 ALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDEVL 238
|
...
gi 1832152097 227 REL 229
Cdd:TIGR02315 239 RHI 241
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-216 |
7.63e-37 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 131.00 E-value: 7.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRlspeqRVREGLAY 80
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP-----EDRRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 81 VPQGRDIFSTLTVEEnILIGMAKFKG---AKTRKVPEHLYEIFpildEMKQRRG---GDLSGGQQQQLAIARALASEPKV 154
Cdd:COG4152 76 LPEERGLYPKMKVGE-QLVYLARLKGlskAEAKRRADEWLERL----GLGDRANkkvEELSKGNQQKVQLIAALLHDPEL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1832152097 155 LILDEPTEGIQP---SIIKDigrVIRKLADSGemAIVLveqF----YDFAEELADGYTVMARGQVIAQG 216
Cdd:COG4152 151 LILDEPFSGLDPvnvELLKD---VIRELAAKG--TTVI---FsshqMELVEELCDRIVIINKGRKVLSG 211
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-216 |
1.72e-36 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 127.33 E-value: 1.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVREGLAYV 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 82 PQgrdIFSTLTVEENILIGmAKFKGAKTRKVPEHLYEIFpiLDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDEPT 161
Cdd:cd03268 81 PG---FYPNLTARENLRLL-ARLLGIRKKRIDEVLDVVG--LKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1832152097 162 EGIQPSIIKDIGRVIRKLADSGeMAIVLVEQFYDFAEELADGYTVMARGQVIAQG 216
Cdd:cd03268 155 NGLDPDGIKELRELILSLRDQG-ITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-216 |
2.97e-36 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 127.10 E-value: 2.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFY----GGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRlSPEQrVRE 76
Cdd:cd03266 1 MITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAE-ARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 77 GLAYVPQGRDIFSTLTVEENILIgMAKFKGAKTRKVPEHLYEIFPILD--EMKQRRGGDLSGGQQQQLAIARALASEPKV 154
Cdd:cd03266 79 RLGFVSDSTGLYDRLTARENLEY-FAGLYGLKGDELTARLEELADRLGmeELLDRRVGGFSTGMRQKVAIARALVHDPPV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1832152097 155 LILDEPTEGIQPSIIKDIGRVIRKLADSGEmAIVLVEQFYDFAEELADGYTVMARGQVIAQG 216
Cdd:cd03266 158 LLLDEPTTGLDVMATRALREFIRQLRALGK-CILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-212 |
3.04e-36 |
|
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: 126.01 E-value: 3.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVnqfyGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVREGLAY 80
Cdd:cd03215 4 VLEVRGL----SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 81 VP---QGRDIFSTLTVEENILIgmakfkgaktrkvpehlyeifPILdemkqrrggdLSGGQQQQLAIARALASEPKVLIL 157
Cdd:cd03215 80 VPedrKREGLVLDLSVAENIAL---------------------SSL----------LSGGNQQKVVLARWLARDPRVLIL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1832152097 158 DEPTEGIQPSIIKDIGRVIRKLADSGeMAIVLVEqfYDFAE--ELADGYTVMARGQV 212
Cdd:cd03215 129 DEPTRGVDVGAKAEIYRLIRELADAG-KAVLLIS--SELDEllGLCDRILVMYEGRI 182
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-220 |
8.19e-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: 126.54 E-value: 8.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGS----HILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRV-- 74
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 75 REGLAYVPQGRDIFSTLTVEENILIGMaKFKGAKTRKVPEHLYEIFPI--LDEMKQRRGGDLSGGQQQQLAIARALASEP 152
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPL-EIAGVPKAEIEERVLELLELvgLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1832152097 153 KVLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGRE 220
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEE 227
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-231 |
3.74e-35 |
|
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: 124.66 E-value: 3.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRvreGLAYV 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKR---PVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 82 PQGRDIFSTLTVEENILIG--MAKFKGAKTR-KVPEHLYEIfpILDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILD 158
Cdd:cd03300 78 FQNYALFPHLTVFENIAFGlrLKKLPKAEIKeRVAEALDLV--QLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1832152097 159 EPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREMPEKGIRELVA 231
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVA 228
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-190 |
6.71e-35 |
|
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: 122.11 E-value: 6.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSH--ILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQrVREGLA 79
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLES-LRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 80 YVPQGRDIFSTlTVEENILigmakfkgaktrkvpehlyeifpildemkqrrggdlSGGQQQQLAIARALASEPKVLILDE 159
Cdd:cd03228 80 YVPQDPFLFSG-TIRENIL------------------------------------SGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190
....*....|....*....|....*....|.
gi 1832152097 160 PTEGIQPSIIKDIGRVIRKLADsgEMAIVLV 190
Cdd:cd03228 123 ATSALDPETEALILEALRALAK--GKTVIVI 151
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-226 |
1.15e-34 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 125.30 E-value: 1.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVREGLayV 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGV--V 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 82 PQGRDIFSTLTVEENILIGMAKF--KGAKTRKVPEHLYEiFPILDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDE 159
Cdd:PRK13537 86 PQFDNLDPDFTVRENLLVFGRYFglSAAAARALVPPLLE-FAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1832152097 160 PTEGIQPSIIKDIGRVIRKLADSGEmAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREMPEKGI 226
Cdd:PRK13537 165 PTTGLDPQARHLMWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEI 230
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-220 |
1.25e-34 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 129.50 E-value: 1.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSH--ILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQrVREGLA 79
Cdd:COG4987 334 LELEDVSFRYPGAGrpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDD-LRRRIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 80 YVPQGRDIFSTlTVEENILIGmakfKGAKT--------RKVP-EHLYEIFPI-LDEMKQRRGGDLSGGQQQQLAIARALA 149
Cdd:COG4987 413 VVPQRPHLFDT-TLRENLRLA----RPDATdeelwaalERVGlGDWLAALPDgLDTWLGEGGRRLSGGERRRLALARALL 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1832152097 150 SEPKVLILDEPTEGIQPSIIKDIGRVIRKLAdsGEMAIVLV---EQfydfAEELADGYTVMARGQVIAQGAGRE 220
Cdd:COG4987 488 RDAPILLLDEPTEGLDAATEQALLADLLEAL--AGRTVLLIthrLA----GLERMDRILVLEDGRIVEQGTHEE 555
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-216 |
1.34e-34 |
|
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: 122.69 E-value: 1.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHILRDVSFQAPVGAcSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRlsPEQRVREGLAYV 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK--QPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 82 PQGRDIFSTLTVEEnILIGMAKFKGAKTRKVPEHLYEIFPILD--EMKQRRGGDLSGGQQQQLAIARALASEPKVLILDE 159
Cdd:cd03264 78 PQEFGVYPNFTVRE-FLDYIAWLKGIPSKEVKARVDEVLELVNlgDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1832152097 160 PTEGIQPsiiKDIGRVIRKLADSGEMAIVL-----VEQFYDFAEELAdgytVMARGQVIAQG 216
Cdd:cd03264 157 PTAGLDP---EERIRFRNLLSELGEDRIVIlsthiVEDVESLCNQVA----VLNKGKLVFEG 211
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-216 |
1.63e-34 |
|
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: 123.37 E-value: 1.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYG----GSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVRE 76
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 77 gLAYVPQgrDIFSTL----TVEENILIGMAKFKGAKTRKVPEHLYEIFPILDEMKQRRGGDLSGGQQQQLAIARALASEP 152
Cdd:COG1124 81 -VQMVFQ--DPYASLhprhTVDRILAEPLRIHGLPDREERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARALILEP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1832152097 153 KVLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQG 216
Cdd:COG1124 158 ELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEEL 221
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-221 |
2.54e-34 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 122.89 E-value: 2.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGkdISRLSPEQRVRE---- 76
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG--LKVNDPKVDERLirqe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 77 -GLayVPQGRDIFSTLTVEENILIGMAKFKGAKTRKVPEHLYEIFPI--LDEMKQRRGGDLSGGQQQQLAIARALASEPK 153
Cdd:PRK09493 79 aGM--VFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKvgLAERAHHYPSELSGGQQQRVAIARALAVKPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1832152097 154 VLILDEPTEGIQPSIIKDIGRVIRKLADSGeMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREM 221
Cdd:PRK09493 157 LMLFDEPTSALDPELRHEVLKVMQDLAEEG-MTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVL 223
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-225 |
4.24e-34 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 127.95 E-value: 4.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFY-GGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRvREGLAY 80
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW-RRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 81 VPQGRDIFSTlTVEENILIGMAKFKGAKTRKVPE--HLYEIFP----ILDEMKQRRGGDLSGGQQQQLAIARALASEPKV 154
Cdd:COG4988 416 VPQNPYLFAG-TIRENLRLGRPDASDEELEAALEaaGLDEFVAalpdGLDTPLGEGGRGLSGGQAQRLALARALLRDAPL 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1832152097 155 LILDEPTEGIQPSIIKDIGRVIRKLADsGEMAIV------LVEQfydfaeelADGYTVMARGQVIAQGAGREMPEKG 225
Cdd:COG4988 495 LLLDEPTAHLDAETEAEILQALRRLAK-GRTVILithrlaLLAQ--------ADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
2-224 |
6.42e-34 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 122.02 E-value: 6.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCL--MGIL-PIK--SGQILLDGKDI--SRLSPEQrV 74
Cdd:TIGR00972 2 IEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLnrMNDLvPGVriEGKVLFDGQDIydKKIDVVE-L 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 75 REGLAYVPQGRDIFStLTVEENILIGMaKFKGAKTRK----VPEHLYEIFPILDEMKQR---RGGDLSGGQQQQLAIARA 147
Cdd:TIGR00972 81 RRRVGMVFQKPNPFP-MSIYDNIAYGP-RLHGIKDKKeldeIVEESLKKAALWDEVKDRlhdSALGLSGGQQQRLCIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1832152097 148 LASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSgeMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREMPEK 224
Cdd:TIGR00972 159 LAVEPEVLLLDEPTSALDPIATGKIEELIQELKKK--YTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTN 233
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-160 |
6.58e-34 |
|
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: 121.04 E-value: 6.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGS----HILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEqrvreg 77
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 78 LAYVPQGRDIFSTLTVEENILIG--MAKFKGAKTRKVPEHLYEIFPiLDEMKQRRGGDLSGGQQQQLAIARALASEPKVL 155
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALGleLQGVPKAEARERAEELLELVG-LSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
....*
gi 1832152097 156 ILDEP 160
Cdd:cd03293 154 LLDEP 158
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-231 |
1.01e-33 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 126.29 E-value: 1.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNqfygGSHILRDVSFQAP----VGacsvVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVRE 76
Cdd:COG1129 256 VLEVEGLS----VGGVVRDVSFSVRageiLG----IAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRA 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 77 GLAYVPQGRD---IFSTLTVEENILIG-MAKFKGaktrkvpehlyeiFPILDEMKQRRG-------------------GD 133
Cdd:COG1129 328 GIAYVPEDRKgegLVLDLSIRENITLAsLDRLSR-------------GGLLDRRRERALaeeyikrlriktpspeqpvGN 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 134 LSGGQQQQLAIARALASEPKVLILDEPTEGIqpsiikDIG------RVIRKLADSGeMAIVLVEQfyDFAE--ELADGYT 205
Cdd:COG1129 395 LSGGNQQKVVLAKWLATDPKVLILDEPTRGI------DVGakaeiyRLIRELAAEG-KAVIVISS--ELPEllGLSDRIL 465
|
250 260
....*....|....*....|....*.
gi 1832152097 206 VMARGQVIAQGAGREMPEKGIRELVA 231
Cdd:COG1129 466 VMREGRIVGELDREEATEEAIMAAAT 491
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-183 |
1.61e-33 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 120.16 E-value: 1.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSH-ILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQ--RVREG 77
Cdd:COG2884 1 MIRFENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 78 LAYVPQGRDIFSTLTVEENILIGMaKFKGAKTRKVPEHLYEIFPI--LDEMKQRRGGDLSGGQQQQLAIARALASEPKVL 155
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPL-RVTGKSRKEIRRRVREVLDLvgLSDKAKALPHELSGGEQQRVAIARALVNRPELL 159
|
170 180
....*....|....*....|....*...
gi 1832152097 156 ILDEPTEGIQPSIIKDIGRVIRKLADSG 183
Cdd:COG2884 160 LADEPTGNLDPETSWEIMELLEEINRRG 187
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-161 |
1.72e-33 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 126.87 E-value: 1.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSH--ILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQrVREGLA 79
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPAS-LRRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 80 YVPQGRDIFSTlTVEENILIGMAKFKgaktrkvPEHLYE------IFPILDEMKQR-------RGGDLSGGQQQQLAIAR 146
Cdd:COG2274 553 VVLQDVFLFSG-TIRENITLGDPDAT-------DEEIIEaarlagLHDFIEALPMGydtvvgeGGSNLSGGQRQRLAIAR 624
|
170
....*....|....*
gi 1832152097 147 ALASEPKVLILDEPT 161
Cdd:COG2274 625 ALLRNPRILILDEAT 639
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-212 |
2.03e-33 |
|
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: 119.67 E-value: 2.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRvreGLAYV 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDR---DIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 82 PQGRDIFSTLTVEENILIGMaKFKGAKTRKVPEHLYEIFPIL--DEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDE 159
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGL-KLRKVPKDEIDERVREVAELLqiEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1832152097 160 PTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQV 212
Cdd:cd03301 157 PLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-160 |
2.96e-33 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 120.58 E-value: 2.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFY----GGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEqrvre 76
Cdd:COG1116 7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 77 gLAYVPQGRDIFSTLTVEENILIGMaKFKGAKTRKVPEHLYEIFPI--LDEMKQRRGGDLSGGQQQQLAIARALASEPKV 154
Cdd:COG1116 82 -RGVVFQEPALLPWLTVLDNVALGL-ELRGVPKAERRERARELLELvgLAGFEDAYPHQLSGGMRQRVAIARALANDPEV 159
|
....*.
gi 1832152097 155 LILDEP 160
Cdd:COG1116 160 LLMDEP 165
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-221 |
5.37e-33 |
|
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: 119.33 E-value: 5.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSH-ILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEqRVREGLAY 80
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPV-ELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 81 VPQGRDIFSTLTVEENILIgMAKFKGAKTRKVPEHLYEIFPILD----EMKQRRGGDLSGGQQQQLAIARALASEPKVLI 156
Cdd:cd03295 80 VIQQIGLFPHMTVEENIAL-VPKLLKWPKEKIRERADELLALVGldpaEFADRYPHELSGGQQQRVGVARALAADPPLLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1832152097 157 LDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREM 221
Cdd:cd03295 159 MDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-216 |
8.11e-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: 8.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKcLMGILPI-KSGQILLDGK--DISRLSPEQRVRE-- 76
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLR-VLNLLETpDSGQLNIAGHqfDFSQKPSEKAIRLlr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 77 -GLAYVPQGRDIFSTLTVEENIL------IGMAKFKG-AKTRKVPEHLYeifpiLDEMKQRRGGDLSGGQQQQLAIARAL 148
Cdd:COG4161 82 qKVGMVFQQYNLWPHLTVMENLIeapckvLGLSKEQArEKAMKLLARLR-----LTDKADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1832152097 149 ASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGeMAIVLVEQFYDFAEELADGYTVMARGQVIAQG 216
Cdd:COG4161 157 MMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTG-ITQVIVTHEVEFARKVASQVVYMEKGRIIEQG 223
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
2-220 |
1.01e-32 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 121.30 E-value: 1.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRvreGLAYV 81
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKR---DYGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 82 PQGRDIFSTLTVEENILIGMaKFKGAKTRKVPEHLYEIFPI--LDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDE 159
Cdd:TIGR03265 82 FQSYALFPNLTVADNIAYGL-KNRGMGRAEVAERVAELLDLvgLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1832152097 160 PTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGRE 220
Cdd:TIGR03265 161 PLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQE 221
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-216 |
1.17e-32 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 117.77 E-value: 1.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLspeqrVREGLAYV 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIA-----ARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 82 PQGRDIFSTLTVEENiLIGMAKFKGAKTRKVPEHLYEIFPILD--EMKQRRGGDLSGGQQQQLAIARALASEPKVLILDE 159
Cdd:cd03269 76 PEERGLYPKMKVIDQ-LVYLAQLKGLKKEEARRRIDEWLERLElsEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1832152097 160 PTEGIQPSIIKDIGRVIRKLADSGEmAIVLVEQFYDFAEELADGYTVMARGQVIAQG 216
Cdd:cd03269 155 PFSGLDPVNVELLKDVIRELARAGK-TVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
3-225 |
1.72e-32 |
|
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: 117.71 E-value: 1.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 3 EVKDVNQFY-GGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLsPEQRVREGLAYV 81
Cdd:cd03254 4 EFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDI-SRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 82 PQGRDIFSTlTVEENILIG-----------MAKFKGAKT--RKVPEHLYEifpILDEmkqrRGGDLSGGQQQQLAIARAL 148
Cdd:cd03254 83 LQDTFLFSG-TIMENIRLGrpnatdeevieAAKEAGAHDfiMKLPNGYDT---VLGE----NGGNLSQGERQLLAIARAM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 149 ASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADsGEMAIVLveqfydfAEEL-----ADGYTVMARGQVIAQGAGREMPE 223
Cdd:cd03254 155 LRDPKILILDEATSNIDTETEKLIQEALEKLMK-GRTSIII-------AHRLstiknADKILVLDDGKIIEEGTHDELLA 226
|
..
gi 1832152097 224 KG 225
Cdd:cd03254 227 KK 228
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-221 |
1.97e-32 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 118.07 E-value: 1.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVREGLAYV 81
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 82 PQGRDIFSTLTVEENIL--IGMAKFKGAKTRKV-PEHLYEIFPIlDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILD 158
Cdd:PRK10895 84 PQEASIFRRLSVYDNLMavLQIRDDLSAEQREDrANELMEEFHI-EHLRDSMGQSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1832152097 159 EPTEGIQPSIIKDIGRVIRKLADSGeMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREM 221
Cdd:PRK10895 163 EPFAGVDPISVIDIKRIIEHLRDSG-LGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-217 |
2.01e-32 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 117.55 E-value: 2.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSHIlrDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRvreGLAY 80
Cdd:COG3840 1 MLRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAER---PVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 81 VPQGRDIFSTLTVEENILIGMA---KFKGAKTRKVPEHLYEIFpiLDEMKQRRGGDLSGGQQQQLAIARALASEPKVLIL 157
Cdd:COG3840 76 LFQENNLFPHLTVAQNIGLGLRpglKLTAEQRAQVEQALERVG--LAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 158 DEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQGA 217
Cdd:COG3840 154 DEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGP 213
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-220 |
2.55e-32 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 117.81 E-value: 2.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVREgLAY 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARR-LAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 81 VPQGRDIFSTLTVEENILIGMAKFK------GAKTRKVPEHLYEIFPIlDEMKQRRGGDLSGGQQQQLAIARALASEPKV 154
Cdd:PRK11231 81 LPQHHLTPEGITVRELVAYGRSPWLslwgrlSAEDNARVNQAMEQTRI-NHLADRRLTDLSGGQRQRAFLAMVLAQDTPV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1832152097 155 LILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVeqfYDF--AEELADGYTVMARGQVIAQGAGRE 220
Cdd:PRK11231 160 VLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVL---HDLnqASRYCDHLVVLANGHVMAQGTPEE 224
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
16-216 |
4.21e-32 |
|
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: 115.73 E-value: 4.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 16 ILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMG--ILPIKSGQILLDGKDISRLSPEQRVreglAYVPQGRDIFSTLTV 93
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDKRSFRKII----GYVPQDDILHPTLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 94 EENILIGmAKFKGaktrkvpehlyeifpildemkqrrggdLSGGQQQQLAIARALASEPKVLILDEPTEGIQPSIIKDIG 173
Cdd:cd03213 100 RETLMFA-AKLRG---------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVM 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1832152097 174 RVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQG 216
Cdd:cd03213 152 SLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-221 |
4.64e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 117.98 E-value: 4.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGS-HILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQrVREGLA 79
Cdd:PRK13652 3 LIETRDLCYSYSGSkEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIRE-VRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 80 YVPQGRD--IFSTlTVEENILIGMAKFkGAKTRKVPEHLYEIFPIL--DEMKQRRGGDLSGGQQQQLAIARALASEPKVL 155
Cdd:PRK13652 82 LVFQNPDdqIFSP-TVEQDIAFGPINL-GLDEETVAHRVSSALHMLglEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1832152097 156 ILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREM 221
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
13-221 |
1.22e-31 |
|
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: 118.29 E-value: 1.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 13 GSHILrDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDI--SR----LSPEQRvreGLAYVPQGRD 86
Cdd:TIGR02142 10 GDFSL-DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdSRkgifLPPEKR---RIGYVFQEAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 87 IFSTLTVEENILIGMAKFKGAKTRKVPEHLYEIFPIlDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDEPTEGIQP 166
Cdd:TIGR02142 86 LFPHLSVRGNLRYGMKRARPSERRISFERVIELLGI-GHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1832152097 167 SIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREM 221
Cdd:TIGR02142 165 PRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-220 |
1.36e-31 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 116.02 E-value: 1.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVREgLAY 80
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARR-RAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 81 VPQgrdiFSTL----TVEENILIGMAKFKGAKTRK--VPEHLYEIFPiLDEMKQRRGGDLSGGQQQQLAIARALA----- 149
Cdd:PRK13548 81 LPQ----HSSLsfpfTVEEVVAMGRAPHGLSRAEDdaLVAAALAQVD-LAHLAGRDYPQLSGGEQQRVQLARVLAqlwep 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1832152097 150 -SEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGRE 220
Cdd:PRK13548 156 dGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-212 |
1.49e-31 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 118.26 E-value: 1.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRvREGlaYV 81
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDR-KVG--FV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 82 PQGRDIFSTLTVEENILIGMA------KFKGAKTRKVPEHLYEIFPiLDEMKQRRGGDLSGGQQQQLAIARALASEPKVL 155
Cdd:PRK10851 80 FQHYALFRHMTVFDNIAFGLTvlprreRPNAAAIKAKVTQLLEMVQ-LAHLADRYPAQLSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1832152097 156 ILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQV 212
Cdd:PRK10851 159 LLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
13-216 |
2.48e-31 |
|
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: 114.31 E-value: 2.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 13 GSHILrDVSFQAPvGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGK--DISR----LSPEQRvreGLAYVPQGRD 86
Cdd:cd03297 11 PDFTL-KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlFDSRkkinLPPQQR---KIGLVFQQYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 87 IFSTLTVEENILIGMAKFKGAKTRKVPEHLYEIFPiLDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDEPTEGIQP 166
Cdd:cd03297 86 LFPHLNVRENLAFGLKRKRNREDRISVDELLDLLG-LDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1832152097 167 SIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQG 216
Cdd:cd03297 165 ALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-216 |
2.63e-31 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 115.11 E-value: 2.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLmGILPI-KSGQILLDGK--DISRLSPEQRVRE-- 76
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVL-NLLEMpRSGTLNIAGNhfDFSKTPSDKAIRElr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 77 -GLAYVPQGRDIFSTLTVEENIL------IGMAKfKGAKTR--KVPEHLYeifpiLDEMKQRRGGDLSGGQQQQLAIARA 147
Cdd:PRK11124 82 rNVGMVFQQYNLWPHLTVQQNLIeapcrvLGLSK-DQALARaeKLLERLR-----LKPYADRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1832152097 148 LASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGeMAIVLVEQFYDFAEELADGYTVMARGQVIAQG 216
Cdd:PRK11124 156 LMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETG-ITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-216 |
1.05e-30 |
|
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: 112.68 E-value: 1.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHI--LRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPeQRVREGLA 79
Cdd:cd03245 3 IEFRNVSFSYPNQEIpaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDP-ADLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 80 YVPQGRDIFSTlTVEENILIGM-----------AKFKGAK--TRKVPEHlyeifpiLDEMKQRRGGDLSGGQQQQLAIAR 146
Cdd:cd03245 82 YVPQDVTLFYG-TLRDNITLGApladderilraAELAGVTdfVNKHPNG-------LDLQIGERGRGLSGGQRQAVALAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1832152097 147 ALASEPKVLILDEPTEGIqpsiikDIG---RVIRKLADS-GEMAIVLVEQFYDFAeELADGYTVMARGQVIAQG 216
Cdd:cd03245 154 ALLNDPPILLLDEPTSAM------DMNseeRLKERLRQLlGDKTLIIITHRPSLL-DLVDRIIVMDSGRIVADG 220
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-216 |
1.05e-30 |
|
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: 113.13 E-value: 1.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 16 ILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILP---IKSGQILLDGKDISRlspeQRVREGLAYVPQGRDIFSTLT 92
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQPRKP----DQFQKCVAYVRQDDILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 93 VEENILIgMAKFKGA--KTRKVPEHLYEIFPILDEMKQRRGGD----LSGGQQQQLAIARALASEPKVLILDEPTEGIQP 166
Cdd:cd03234 98 VRETLTY-TAILRLPrkSSDAIRKKRVEDVLLRDLALTRIGGNlvkgISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1832152097 167 SIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQG 216
Cdd:cd03234 177 FTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-229 |
1.28e-30 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 117.82 E-value: 1.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVREGLAY 80
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALGIGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 81 VPQGRDIFSTLTVEENILIGMAKFKGAK--TRKVPEHLYEI-----FPI-LDemkqRRGGDLSGGQQQQLAIARALASEP 152
Cdd:COG3845 85 VHQHFMLVPNLTVAENIVLGLEPTKGGRldRKAARARIRELserygLDVdPD----AKVEDLSVGEQQRVEILKALYRGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 153 KVLILDEPTEGIQPSIIKDIGRVIRKLADSGeMAIVLV-----EqfydfAEELADGYTVMARGQVIAQGAGREMPEKGIR 227
Cdd:COG3845 161 RILILDEPTAVLTPQEADELFEILRRLAAEG-KSIIFIthklrE-----VMAIADRVTVLRRGKVVGTVDTAETSEEELA 234
|
..
gi 1832152097 228 EL 229
Cdd:COG3845 235 EL 236
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-161 |
1.49e-30 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 118.34 E-value: 1.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNqF-YGGSH-ILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQrVREGLA 79
Cdd:COG1132 340 IEFENVS-FsYPGDRpVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLES-LRRQIG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 80 YVPQGRDIFSTlTVEENILIG-----MAKFKGAkTRKVpeHLYEI---FPI-LDEMKQRRGGDLSGGQQQQLAIARALAS 150
Cdd:COG1132 418 VVPQDTFLFSG-TIRENIRYGrpdatDEEVEEA-AKAA--QAHEFieaLPDgYDTVVGERGVNLSGGQRQRIAIARALLK 493
|
170
....*....|.
gi 1832152097 151 EPKVLILDEPT 161
Cdd:COG1132 494 DPPILILDEAT 504
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-221 |
2.74e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 112.70 E-value: 2.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGIL-----PIKSGQILLDGKDISRLsPEQRVRE 76
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIFKM-DVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 77 GLAYVPQGRDIFSTLTVEENILIGMAKFKGAKTRK-----VPEHLyEIFPILDEMKQRRG---GDLSGGQQQQLAIARAL 148
Cdd:PRK14247 83 RVQMVFQIPNPIPNLSIFENVALGLKLNRLVKSKKelqerVRWAL-EKAQLWDEVKDRLDapaGKLSGGQQQRLCIARAL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1832152097 149 ASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADsgEMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREM 221
Cdd:PRK14247 162 AFQPEVLLADEPTANLDPENTAKIESLFLELKK--DMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-217 |
2.99e-30 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 114.81 E-value: 2.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVkDVNQFYGGSHIlrDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGK---DISR---LSPEQRv 74
Cdd:COG4148 2 MLEV-DFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqDSARgifLPPHRR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 75 reGLAYVPQGRDIFSTLTVEENILIGMaKFKGAKTRKV-PEH---LYEIFPILDemkqRRGGDLSGGQQQQLAIARALAS 150
Cdd:COG4148 78 --RIGYVFQEARLFPHLSVRGNLLYGR-KRAPRAERRIsFDEvveLLGIGHLLD----RRPATLSGGERQRVAIGRALLS 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1832152097 151 EPKVLILDEPTEGIqpsiikDIGR------VIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQGA 217
Cdd:COG4148 151 SPRLLLMDEPLAAL------DLARkaeilpYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGP 217
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-190 |
5.26e-30 |
|
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: 116.31 E-value: 5.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHI-LRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSpEQRVREGLAY 80
Cdd:TIGR02868 335 LELRDLSAGYPGAPPvLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLD-QDEVRRRVSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 81 VPQGRDIFSTlTVEENILIGMAKFKGAKTRKVPE------HLYEIFPILDEMKQRRGGDLSGGQQQQLAIARALASEPKV 154
Cdd:TIGR02868 414 CAQDAHLFDT-TVRENLRLARPDATDEELWAALErvgladWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPI 492
|
170 180 190
....*....|....*....|....*....|....*.
gi 1832152097 155 LILDEPTEGIQPsiiKDIGRVIRKLADSGEMAIVLV 190
Cdd:TIGR02868 493 LLLDEPTEHLDA---ETADELLEDLLAALSGRTVVL 525
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-216 |
7.56e-30 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 113.39 E-value: 7.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVREGLayV 81
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGV--V 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 82 PQGRDIFSTLTVEENILIgMAKFKGAKTRKVPEHLYEI--FPILDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDE 159
Cdd:PRK13536 120 PQFDNLDLEFTVRENLLV-FGRYFGMSTREIEAVIPSLleFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDE 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1832152097 160 PTEGIQPSIIKDIGRVIRKLADSGeMAIVLVEQFYDFAEELADGYTVMARGQVIAQG 216
Cdd:PRK13536 199 PTTGLDPHARHLIWERLRSLLARG-KTILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-226 |
7.73e-30 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 115.92 E-value: 7.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVREGLAY 80
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 81 VPQGRDIFSTLTVEENILIGMAKFKGAKtRKVPEHLYEIFPILD-EMKqrrGGDLSGGQQQQLAIARALASEPKVLILDE 159
Cdd:PRK15439 91 VPQEPLLFPNLSVKENILFGLPKRQASM-QKMKQLLAALGCQLDlDSS---AGSLEVADRQIVEILRGLMRDSRILILDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1832152097 160 PTEGIQPSIIKDIGRVIRKLADSGeMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREMPEKGI 226
Cdd:PRK15439 167 PTASLTPAETERLFSRIRELLAQG-VGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDI 232
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-160 |
1.38e-29 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 113.50 E-value: 1.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRvreGLAYV 81
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENR---HVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 82 PQGRDIFSTLTVEENILIGMakfkgaKTRKVPEHlyEIFPI---------LDEMKQRRGGDLSGGQQQQLAIARALASEP 152
Cdd:PRK09452 92 FQSYALFPHMTVFENVAFGL------RMQKTPAA--EITPRvmealrmvqLEEFAQRKPHQLSGGQQQRVAIARAVVNKP 163
|
....*...
gi 1832152097 153 KVLILDEP 160
Cdd:PRK09452 164 KVLLLDES 171
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-190 |
2.21e-29 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 110.13 E-value: 2.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCL--MGILpIK----SGQILLDGKDIsrLSPEQ--- 72
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMNDL-IPgarvEGEILLDGEDI--YDPDVdvv 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 73 RVREGLAYVPQGRDIFSTlTVEENILIGmAKFKGAKTRKVPEHLYE-------IFpilDEMKQR---RGGDLSGGQQQQL 142
Cdd:COG1117 89 ELRRRVGMVFQKPNPFPK-SIYDNVAYG-LRLHGIKSKSELDEIVEeslrkaaLW---DEVKDRlkkSALGLSGGQQQRL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1832152097 143 AIARALASEPKVLILDEPTEGIQP---SIIKDigrVIRKLADsgEMAIVLV 190
Cdd:COG1117 164 CIARALAVEPEVLLMDEPTSALDPistAKIEE---LILELKK--DYTIVIV 209
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
2-216 |
2.30e-29 |
|
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: 115.35 E-value: 2.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGS--HILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQrVREGLA 79
Cdd:TIGR03375 464 IEFRNVSFAYPGQetPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPAD-LRRNIG 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 80 YVPQGRDIFSTlTVEENILIGM-----------AKFKGAkTRKVPEHlyeifPI-LDEMKQRRGGDLSGGQQQQLAIARA 147
Cdd:TIGR03375 543 YVPQDPRLFYG-TLRDNIALGApyaddeeilraAELAGV-TEFVRRH-----PDgLDMQIGERGRSLSGGQRQAVALARA 615
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1832152097 148 LASEPKVLILDEPTEGIqpsiikDIG---RVIRKLAD-SGEMAIVLVEQFYDFAeELADGYTVMARGQVIAQG 216
Cdd:TIGR03375 616 LLRDPPILLLDEPTSAM------DNRseeRFKDRLKRwLAGKTLVLVTHRTSLL-DLVDRIIVMDNGRIVADG 681
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-160 |
2.39e-29 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 110.34 E-value: 2.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGS----HILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVre 76
Cdd:COG4525 3 MLTVRHVSVRYPGGgqpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRGV-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 77 glayVPQGRDIFSTLTVEENILIGMaKFKG---AKTRKVPEHLYEIFPiLDEMKQRRGGDLSGGQQQQLAIARALASEPK 153
Cdd:COG4525 81 ----VFQKDALLPWLNVLDNVAFGL-RLRGvpkAERRARAEELLALVG-LADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
....*..
gi 1832152097 154 VLILDEP 160
Cdd:COG4525 155 FLLMDEP 161
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-216 |
4.42e-29 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 109.67 E-value: 4.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPE---------- 71
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 72 --QRVREGLAYVPQGRDIFSTLTVEENIL------IGMAKFKgAKTRKVpEHLYEIfPILDEMKQRRGGDLSGGQQQQLA 143
Cdd:PRK10619 86 qlRLLRTRLTMVFQHFNLWSHMTVLENVMeapiqvLGLSKQE-ARERAV-KYLAKV-GIDERAQGKYPVHLSGGQQQRVS 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1832152097 144 IARALASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFyDFAEELADGYTVMARGQVIAQG 216
Cdd:PRK10619 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEM-GFARHVSSHVIFLHQGKIEEEG 234
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-221 |
5.73e-29 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 109.12 E-value: 5.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKClMGILPI-KSGQILLDGKDIS-------RLSPE- 71
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRC-INLLETpDSGEIRVGGEEIRlkpdrdgELVPAd 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 72 ----QRVREGLAYVPQGRDIFSTLTVEENIL------IGMAKfkgAKTRKVPEHLYEIFPILDemkqRRG---GDLSGGQ 138
Cdd:COG4598 87 rrqlQRIRTRLGMVFQSFNLWSHMTVLENVIeapvhvLGRPK---AEAIERAEALLAKVGLAD----KRDaypAHLSGGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 139 QQQLAIARALASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGE-MAIVLVEQfyDFAEELADGYTVMARGQVIAQGA 217
Cdd:COG4598 160 QQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRtMLVVTHEM--GFARDVSSHVVFLHQGRIEEQGP 237
|
....
gi 1832152097 218 GREM 221
Cdd:COG4598 238 PAEV 241
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-188 |
6.27e-29 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 107.65 E-value: 6.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDIsrlsPEQRVREGLAY 80
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI----DDPDVAEACHY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 81 VPQGRDIFSTLTVEENiLIGMAKFKGAKTRKVPEHL--YEIFPILDemkqRRGGDLSGGQQQQLAIARALASEPKVLILD 158
Cdd:PRK13539 78 LGHRNAMKPALTVAEN-LEFWAAFLGGEELDIAAALeaVGLAPLAH----LPFGYLSAGQKRRVALARLLVSNRPIWILD 152
|
170 180 190
....*....|....*....|....*....|
gi 1832152097 159 EPTEGIQPSIIKDIGRVIRKLADSGEMAIV 188
Cdd:PRK13539 153 EPTAALDAAAVALFAELIRAHLAQGGIVIA 182
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-190 |
7.91e-29 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 110.14 E-value: 7.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFY----GGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILP---IKSGQILLDGKDISRLSPEQ- 72
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 73 ---RVREgLAYVPQgrDIFSTL----TVEENILIGMAKFKGAKTRKVPEHLYEIfpiLDEMK----QRRGGD----LSGG 137
Cdd:COG0444 81 rkiRGRE-IQMIFQ--DPMTSLnpvmTVGDQIAEPLRIHGGLSKAEARERAIEL---LERVGlpdpERRLDRypheLSGG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1832152097 138 QQQQLAIARALASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLV 190
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFI 207
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-216 |
1.01e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 108.92 E-value: 1.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSH--ILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQrVREGL 78
Cdd:PRK13632 7 MIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKE-IRKKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 79 AYVPQGRD-IFSTLTVEENILIGMakfkgaKTRKVPEHlyEIFPILDEMKQRRGGD---------LSGGQQQQLAIARAL 148
Cdd:PRK13632 86 GIIFQNPDnQFIGATVEDDIAFGL------ENKKVPPK--KMKDIIDDLAKKVGMEdyldkepqnLSGGQKQRVAIASVL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1832152097 149 ASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEqfYDFAEE-LADGYTVMARGQVIAQG 216
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISIT--HDMDEAiLADKVIVFSEGKLIAQG 224
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-223 |
1.36e-28 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 110.70 E-value: 1.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRvreGLAY 80
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQR---PINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 81 VPQGRDIFSTLTVEENILIGMAKFKGAK---TRKVPEHLYEIFpiLDEMKQRRGGDLSGGQQQQLAIARALASEPKVLIL 157
Cdd:PRK11607 96 MFQSYALFPHMTVEQNIAFGLKQDKLPKaeiASRVNEMLGLVH--MQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1832152097 158 DEPtegiqpsiikdIGRVIRKLADSGEMAI-----------VLVEQFYDFAEELADGYTVMARGQVIAQGAGREMPE 223
Cdd:PRK11607 174 DEP-----------MGALDKKLRDRMQLEVvdilervgvtcVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYE 239
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-221 |
1.91e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 108.40 E-value: 1.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYG-GSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGK--DISRlSPEQRVREG 77
Cdd:PRK13636 5 ILKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSR-KGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 78 LAYVPQGRD--IFSTlTVEENILIGMAKFKGAK--TRKVPEHLYEIFPIlDEMKQRRGGDLSGGQQQQLAIARALASEPK 153
Cdd:PRK13636 84 VGMVFQDPDnqLFSA-SVYQDVSFGAVNLKLPEdeVRKRVDNALKRTGI-EHLKDKPTHCLSFGQKKRVAIAGVLVMEPK 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1832152097 154 VLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREM 221
Cdd:PRK13636 162 VLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-216 |
2.17e-28 |
|
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: 107.48 E-value: 2.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQ-ILLDGKDISRLS-PEQRVREGL 78
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDvWELRKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 79 AYVPQGRDIFSTLTVEENIL------IGMAKFKGAKTRKVPEHLYEIFPIlDEMKQRRGGDLSGGQQQQLAIARALASEP 152
Cdd:COG1119 83 VSPALQLRFPRDETVLDVVLsgffdsIGLYREPTDEQRERARELLELLGL-AHLADRPFGTLSQGEQRRVLIARALVKDP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1832152097 153 KVLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQfydFAEELADGYT---VMARGQVIAQG 216
Cdd:COG1119 162 ELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTH---HVEEIPPGIThvlLLKDGRVVAAG 225
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-216 |
9.97e-28 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 107.86 E-value: 9.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGS----HILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQ--RV 74
Cdd:COG1135 1 MIELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElrAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 75 REGLAYVPQGRDIFSTLTVEENI-----LIGMAKfkGAKTRKVPEhlyeifpILD-----EMKQRRGGDLSGGQQQQLAI 144
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENValpleIAGVPK--AEIRKRVAE-------LLElvglsDKADAYPSQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1832152097 145 ARALASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQG 216
Cdd:COG1135 152 ARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQG 223
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-160 |
1.50e-27 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 109.45 E-value: 1.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSH--ILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRvREGLA 79
Cdd:COG4618 331 LSVENLTVVPPGSKrpILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREEL-GRHIG 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 80 YVPQGRDIFSTlTVEENIligmAKFKGAKTRKVPE-------HlyeifpildEMKQR-----------RGGDLSGGQQQQ 141
Cdd:COG4618 410 YLPQDVELFDG-TIAENI----ARFGDADPEKVVAaaklagvH---------EMILRlpdgydtrigeGGARLSGGQRQR 475
|
170
....*....|....*....
gi 1832152097 142 LAIARALASEPKVLILDEP 160
Cdd:COG4618 476 IGLARALYGDPRLVVLDEP 494
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-161 |
1.71e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 105.55 E-value: 1.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVN-QFYGGS----HILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVR 75
Cdd:COG1101 1 MLELKNLSkTFNPGTvnekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 76 eglaYVpqGRdIF--------STLTVEENILIGMAK-----FKGAKTRKVPEHLYEIFPIL-----DEMKQRRGgDLSGG 137
Cdd:COG1101 81 ----YI--GR-VFqdpmmgtaPSMTIEENLALAYRRgkrrgLRRGLTKKRRELFRELLATLglgleNRLDTKVG-LLSGG 152
|
170 180
....*....|....*....|....
gi 1832152097 138 QQQQLAIARALASEPKVLILDEPT 161
Cdd:COG1101 153 QRQALSLLMATLTKPKLLLLDEHT 176
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-229 |
1.89e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 105.31 E-value: 1.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIK-----SGQILLDGKDIsrLSPEQ---R 73
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNI--YSPDVdpiE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 74 VREGLAYVPQGRDIFSTLTVEENILIGMAKFKGAKTRK----VPEHLYEIFPILDEMKQR---RGGDLSGGQQQQLAIAR 146
Cdd:PRK14267 83 VRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKKeldeRVEWALKKAALWDEVKDRlndYPSNLSGGQRQRLVIAR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 147 ALASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADsgEMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREMPEKGI 226
Cdd:PRK14267 163 ALAMKPKILLMDEPTANIDPVGTAKIEELLFELKK--EYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPE 240
|
...
gi 1832152097 227 REL 229
Cdd:PRK14267 241 HEL 243
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
18-221 |
1.98e-27 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 108.98 E-value: 1.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 18 RDVSFQAPVGAcsvVLGRNGV---GKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVREGLAYVPQGRDIF------ 88
Cdd:PRK15439 280 RNISLEVRAGE---ILGLAGVvgaGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVYLPEDRQSSglylda 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 89 ------STLTVEENILIgmakFKGAKTRKVPEHLYEIFPILDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDEPTE 162
Cdd:PRK15439 357 plawnvCALTHNRRGFW----IKPARENAVLERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTR 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1832152097 163 GIQPSIIKDIGRVIRKLADSGeMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREM 221
Cdd:PRK15439 433 GVDVSARNDIYQLIRSIAAQN-VAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAI 490
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-160 |
2.08e-27 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 106.33 E-value: 2.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSHI-LRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQrVREGLA 79
Cdd:COG1125 1 MIEFENVTKRYPDGTVaVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVE-LRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 80 YVPQGRDIFSTLTVEENILI--GMAKFKGAKTRKVPEHLYEIF---PilDEMKQRRGGDLSGGQQQQLAIARALASEPKV 154
Cdd:COG1125 80 YVIQQIGLFPHMTVAENIATvpRLLGWDKERIRARVDELLELVgldP--EEYRDRYPHELSGGQQQRVGVARALAADPPI 157
|
....*.
gi 1832152097 155 LILDEP 160
Cdd:COG1125 158 LLMDEP 163
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-160 |
3.73e-27 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 103.33 E-value: 3.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILP---IKSGQILLDGKDISRLSPEQRvreG 77
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGRRLTALPAEQR---R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 78 LAYVPQGRDIFSTLTVEENILIGMAKFKGAKTRK--VPEHLYEIFpiLDEMKQRRGGDLSGGQQQQLAIARALASEPKVL 155
Cdd:COG4136 78 IGILFQDDLLFPHLSVGENLAFALPPTIGRAQRRarVEQALEEAG--LAGFADRDPATLSGGQRARVALLRALLAEPRAL 155
|
....*
gi 1832152097 156 ILDEP 160
Cdd:COG4136 156 LLDEP 160
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-221 |
4.17e-27 |
|
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: 108.67 E-value: 4.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYG-GSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQrVREGLAY 80
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHT-LRQFINY 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 81 VPQGRDIFSTlTVEENILIGmAKfKGAKTRKVPEHLyEIFPILDEMKQ----------RRGGDLSGGQQQQLAIARALAS 150
Cdd:TIGR01193 553 LPQEPYIFSG-SILENLLLG-AK-ENVSQDEIWAAC-EIAEIKDDIENmplgyqtelsEEGSSISGGQKQRIALARALLT 628
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1832152097 151 EPKVLILDEPTEGIQPSIIKdigRVIRKLADSGEMAIVLVEQFYDFAEElADGYTVMARGQVIAQGAGREM 221
Cdd:TIGR01193 629 DSKVLILDESTSNLDTITEK---KIVNNLLNLQDKTIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDEL 695
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-216 |
4.38e-27 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 104.30 E-value: 4.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVREGLAY 80
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 81 VPQGRDIFSTLTVEENILI------------GMAK---FKGAKTRKVPEHLYEIFPI-LDEMKQRRGGDLSGGQQQQLAI 144
Cdd:PRK11300 85 TFQHVRLFREMTVIENLLVaqhqqlktglfsGLLKtpaFRRAESEALDRAATWLERVgLLEHANRQAGNLAYGQQRRLEI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1832152097 145 ARALASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQG 216
Cdd:PRK11300 165 ARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANG 236
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-161 |
5.85e-27 |
|
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: 101.52 E-value: 5.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSH--ILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRvREGLA 79
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNEL-GDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 80 YVPQGRDIFSTlTVEENIligmakfkgaktrkvpehlyeifpildemkqrrggdLSGGQQQQLAIARALASEPKVLILDE 159
Cdd:cd03246 80 YLPQDDELFSG-SIAENI------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
..
gi 1832152097 160 PT 161
Cdd:cd03246 123 PN 124
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-221 |
6.41e-27 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 103.62 E-value: 6.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVREgLAY 80
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKR-LAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 81 VPQGRDIFSTLTVEEniLIGMAKF---KGAKT----RKVPEHLYeiFPILDEMKQRRGGDLSGGQQQQLAIARALASEPK 153
Cdd:COG4604 80 LRQENHINSRLTVRE--LVAFGRFpysKGRLTaedrEIIDEAIA--YLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTD 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 154 VLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVeqFYD--FAEELADGYTVMARGQVIAQGAGREM 221
Cdd:COG4604 156 YVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIV--LHDinFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-217 |
1.12e-26 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 106.79 E-value: 1.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGShiLRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVREGLAY 80
Cdd:PRK09700 265 VFEVRNVTSRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAY 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 81 VPQGR---DIFSTLTVEENILIG----MAKFKGA-------KTRKVPEHLYEIFPILDEMKQRRGGDLSGGQQQQLAIAR 146
Cdd:PRK09700 343 ITESRrdnGFFPNFSIAQNMAISrslkDGGYKGAmglfhevDEQRTAENQRELLALKCHSVNQNITELSGGNQQKVLISK 422
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1832152097 147 ALASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGEmAIVLVeqfydfAEELADGYTVMARGQVIAQGA 217
Cdd:PRK09700 423 WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGK-VILMV------SSELPEIITVCDRIAVFCEGR 486
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-181 |
1.95e-26 |
|
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: 106.22 E-value: 1.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGS-HILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRvREGLAY 80
Cdd:TIGR02857 322 LEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW-RDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 81 VPQGRDIFSTlTVEENILIGMAKFKGAKTRKVPEH--LYEIFPILDEMKQRRGGD----LSGGQQQQLAIARALASEPKV 154
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENIRLARPDASDAEIREALERagLDEFVAALPQGLDTPIGEggagLSGGQAQRLALARAFLRDAPL 479
|
170 180
....*....|....*....|....*..
gi 1832152097 155 LILDEPTEGIQPSIIKDIGRVIRKLAD 181
Cdd:TIGR02857 480 LLLDEPTAHLDAETEAEVLEALRALAQ 506
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-220 |
2.23e-26 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 104.92 E-value: 2.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVREgLAY 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR-VAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 81 VPQGRDIFSTLTVEENILIG----MAKFKG---AKTRKVPEHLYEIFpiLDEMKQRRGGDLSGGQQQQLAIARALASEPK 153
Cdd:PRK09536 82 VPQDTSLSFEFDVRQVVEMGrtphRSRFDTwteTDRAAVERAMERTG--VAQFADRPVTSLSGGERQRVLLARALAQATP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1832152097 154 VLILDEPTEGIqpsiikDIGR------VIRKLADSGEMAIVLVEQFyDFAEELADGYTVMARGQVIAQGAGRE 220
Cdd:PRK09536 160 VLLLDEPTASL------DINHqvrtleLVRRLVDDGKTAVAAIHDL-DLAARYCDELVLLADGRVRAAGPPAD 225
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
2-216 |
2.24e-26 |
|
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: 101.42 E-value: 2.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHILRDVSFqaPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRvreGLAYV 81
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFDLTF--AQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADR---PVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 82 PQGRDIFSTLTVEENILIGMA---KFKGAKTRKVPEHLYEIFpiLDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILD 158
Cdd:cd03298 76 FQENNLFAHLTVEQNVGLGLSpglKLTAEDRQAIEVALARVG--LAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1832152097 159 EPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQG 216
Cdd:cd03298 154 EPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-188 |
2.29e-26 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 101.33 E-value: 2.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHI-LRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLS----PEQRVRE 76
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraiPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 77 GLAYvpQGRDIFSTLTVEENILIGMaKFKGAKTRKVPEHLYEIFPILDEMKQRRG--GDLSGGQQQQLAIARALASEPKV 154
Cdd:cd03292 81 GVVF--QDFRLLPDRNVYENVAFAL-EVTGVPPREIRKRVPAALELVGLSHKHRAlpAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190
....*....|....*....|....*....|....
gi 1832152097 155 LILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIV 188
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVV 191
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-212 |
2.39e-26 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 105.86 E-value: 2.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNqfygGSHIlRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVREGLAYV 81
Cdd:PRK10762 258 LKVDNLS----GPGV-NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIVYI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 82 PQGRD---IFSTLTVEENI-LIGMAKF-------KGAKTRKVPEHLYEIFPILDEMKQRRGGDLSGGQQQQLAIARALAS 150
Cdd:PRK10762 333 SEDRKrdgLVLGMSVKENMsLTALRYFsraggslKHADEQQAVSDFIRLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMT 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1832152097 151 EPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGeMAIVLVEQfyDFAEEL--ADGYTVMARGQV 212
Cdd:PRK10762 413 RPKVLILDEPTRGVDVGAKKEIYQLINQFKAEG-LSIILVSS--EMPEVLgmSDRILVMHEGRI 473
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
32-231 |
2.45e-26 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 103.73 E-value: 2.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 32 VLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRvreGLAYVPQGRDIFSTLTVEENILIGMakfkgaKTRK 111
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLR---HINMVFQSYALFPHMTVEENVAFGL------KMRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 112 VPEHlyEIFP---------ILDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADS 182
Cdd:TIGR01187 72 VPRA--EIKPrvlealrlvQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1832152097 183 GEMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREMPEKGIRELVA 231
Cdd:TIGR01187 150 LGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVA 198
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-231 |
2.74e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 105.88 E-value: 2.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVN-QFYGGSHILRDVSFQAPVGAcsvVLGRNGV---GKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVREG 77
Cdd:COG3845 258 LEVENLSvRDDRGVPALKDVSLEVRAGE---ILGIAGVagnGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLG 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 78 LAYVP---QGRDIFSTLTVEENILIG------MAKF---KGAKTRKVPEHLYEIFPILDEMKQRRGGDLSGGQQQQLAIA 145
Cdd:COG3845 335 VAYIPedrLGRGLVPDMSVAENLILGryrrppFSRGgflDRKAIRAFAEELIEEFDVRTPGPDTPARSLSGGNQQKVILA 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 146 RALASEPKVLILDEPTEGIqpsiikDIG------RVIRKLADSGeMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGR 219
Cdd:COG3845 415 RELSRDPKLLIAAQPTRGL------DVGaiefihQRLLELRDAG-AAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAA 487
|
250
....*....|..
gi 1832152097 220 EMPEKGIRELVA 231
Cdd:COG3845 488 EATREEIGLLMA 499
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-220 |
3.69e-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: 102.14 E-value: 3.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYG-GS----HILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQR--V 74
Cdd:TIGR04521 1 IKLKNVSYIYQpGTpfekKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLkdL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 75 REGLAYVPQ--GRDIFSTlTVEENILIGMAKFKGAK---TRKVPEHLyEIFPILDEMKQRRGGDLSGGQQQQLAIARALA 149
Cdd:TIGR04521 81 RKKVGLVFQfpEHQLFEE-TVYKDIAFGPKNLGLSEeeaEERVKEAL-ELVGLDEEYLERSPFELSGGQMRRVAIAGVLA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1832152097 150 SEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGRE 220
Cdd:TIGR04521 159 MEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPRE 229
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-226 |
5.10e-26 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 105.25 E-value: 5.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVREGLAY 80
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 81 VPQGRDIFSTLTVEENILIG---MAKFKG------AKTRKVPEHLYEIFPI---LDEmkqrRGGDLSGGQQQQLAIARAL 148
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIGrhlTKKVCGvniidwREMRVRAAMMLLRVGLkvdLDE----KVANLSISHKQMLEIAKTL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1832152097 149 ASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGEmAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREMPEKGI 226
Cdd:PRK09700 161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGT-AIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDI 237
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-221 |
1.12e-25 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 100.59 E-value: 1.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLmGILP------IKSGQILLDGkdiSR-LSPEQR 73
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCI-NLLEqpeagtIRVGDITIDT---ARsLSQQKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 74 ----VREGLAYVPQGRDIFSTLTVEENILIGMAKFKGAKTRKVPEHLYEIFPIL-----DEMKQRRggdLSGGQQQQLAI 144
Cdd:PRK11264 79 lirqLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVglagkETSYPRR---LSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1832152097 145 ARALASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSgEMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREM 221
Cdd:PRK11264 156 ARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
4-216 |
2.11e-25 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 100.34 E-value: 2.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 4 VKDVNQFYGGSHI-LRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDIsrlspEQRVREGL-AYV 81
Cdd:PRK15056 9 VNDVTVTWRNGHTaLRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT-----RQALQKNLvAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 82 PQGRDI---FSTLtVEENILIG----MAKFKGAKTRK---VPEHLYEIfpILDEMKQRRGGDLSGGQQQQLAIARALASE 151
Cdd:PRK15056 84 PQSEEVdwsFPVL-VEDVVMMGryghMGWLRRAKKRDrqiVTAALARV--DMVEFRHRQIGELSGGQKKRVFLARAIAQQ 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1832152097 152 PKVLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAeELADgYTVMARGQVIAQG 216
Cdd:PRK15056 161 GQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVT-EFCD-YTVMVKGTVLASG 223
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
17-220 |
3.01e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 100.12 E-value: 3.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 17 LRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDIS----RLSpEQRVREGLAYVPQGRDIFSTlT 92
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkkvKLS-DIRKKVGLVFQYPEYQLFEE-T 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 93 VEENILIGMAKFkGAKTRKVPEHLYEIFPIL----DEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDEPTEGIQPSI 168
Cdd:PRK13637 101 IEKDIAFGPINL-GLSEEEIENRVKRAMNIVgldyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKG 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1832152097 169 IKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGRE 220
Cdd:PRK13637 180 RDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPRE 231
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-225 |
3.34e-25 |
|
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: 98.84 E-value: 3.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGG--SHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSpEQRVREGLA 79
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYT-LASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 80 YVPQGRDIFSTlTVEENILIGMAKFKGAKTRKVPE--HLYEI---FPI-LDEMKQRRGGDLSGGQQQQLAIARALASEPK 153
Cdd:cd03251 80 LVSQDVFLFND-TVAENIAYGRPGATREEVEEAARaaNAHEFimeLPEgYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1832152097 154 VLILDEPTEGIQPSIIKDIGRVIRKLAdSGEMAIVLveqfydfAEEL-----ADGYTVMARGQVIAQGAGREMPEKG 225
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLM-KNRTTFVI-------AHRLstienADRIVVLEDGKIVERGTHEELLAQG 227
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
5-160 |
4.21e-25 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 101.26 E-value: 4.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 5 KDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRvreGLAYVPQG 84
Cdd:PRK11000 7 RNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAER---GVGMVFQS 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1832152097 85 RDIFSTLTVEENILIGM--AKFKGAKTRKVPEHLYEIFPiLDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDEP 160
Cdd:PRK11000 84 YALYPHLSVAENMSFGLklAGAKKEEINQRVNQVAEVLQ-LAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
13-225 |
5.10e-25 |
|
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: 98.33 E-value: 5.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 13 GSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQrVREGLAYVPQGRDIFSTlT 92
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAW-LRRQVGVVLQENVLFNR-S 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 93 VEENI-----------LIGMAKFKGAKT--RKVPEHLyeifpilDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDE 159
Cdd:cd03252 92 IRDNIaladpgmsmerVIEAAKLAGAHDfiSELPEGY-------DTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1832152097 160 PTEGIQPSIIKDIGRVIRKLADsGEMAIVLVEQFYdfAEELADGYTVMARGQVIAQGAGREMPEKG 225
Cdd:cd03252 165 ATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLS--TVKNADRIIVMEKGRIVEQGSHDELLAEN 227
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
33-216 |
7.31e-25 |
|
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: 102.40 E-value: 7.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 33 LGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISrlSPEQRVREGLAYVPQGRDIFSTLTVEENILIgMAKFKGaktRKV 112
Cdd:TIGR01257 962 LGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE--TNLDAVRQSLGMCPQHNILFHHLTVAEHILF-YAQLKG---RSW 1035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 113 PEHLYEIFPILDEM-----KQRRGGDLSGGQQQQLAIARALASEPKVLILDEPTEGIQPSIIKDIGRVIRKLAdSGEmAI 187
Cdd:TIGR01257 1036 EEAQLEMEAMLEDTglhhkRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYR-SGR-TI 1113
|
170 180
....*....|....*....|....*....
gi 1832152097 188 VLVEQFYDFAEELADGYTVMARGQVIAQG 216
Cdd:TIGR01257 1114 IMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-217 |
8.16e-25 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 99.88 E-value: 8.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGS----HILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQ--RV 74
Cdd:PRK11153 1 MIELKNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 75 REGLAYVPQGRDIFSTLTVEENI-----LIGMAKfkgAKTRKVPEHLYEIFPiLDEMKQRRGGDLSGGQQQQLAIARALA 149
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNValpleLAGTPK---AEIKARVTELLELVG-LSDKADRYPAQLSGGQKQRVAIARALA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1832152097 150 SEPKVLILDEPTEGIQP----SIIKDIGRVIRKLAdsgeMAIVLVEQFYDFAEELADGYTVMARGQVIAQGA 217
Cdd:PRK11153 157 SNPKVLLCDEATSALDPattrSILELLKDINRELG----LTIVLITHEMDVVKRICDRVAVIDAGRLVEQGT 224
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
17-221 |
2.45e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 97.78 E-value: 2.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 17 LRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILL------DGKDISRLSPeqrVREGLAYVPQ--GRDIF 88
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNKKLKP---LRKKVGIVFQfpEHQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 89 STlTVEENILIGMAKF--KGAKTRKVPEHLYEIFPILDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDEPTEGIQP 166
Cdd:PRK13634 100 EE-TVEKDICFGPMNFgvSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1832152097 167 SIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREM 221
Cdd:PRK13634 179 KGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-221 |
3.37e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 97.07 E-value: 3.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFY-GGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDIS-RLSPEQRVREGL 78
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKyDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 79 AYVPQGRD--IFSTlTVEENILIGMAKFKGAK---TRKVPEHLYEIFpiLDEMKQRRGGDLSGGQQQQLAIARALASEPK 153
Cdd:PRK13639 81 GIVFQNPDdqLFAP-TVEEDVAFGPLNLGLSKeevEKRVKEALKAVG--MEGFENKPPHHLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1832152097 154 VLILDEPTEGIQPSIIKDIGRVIRKLADSGeMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREM 221
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDLNKEG-ITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1-215 |
5.97e-24 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 96.03 E-value: 5.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFY---------GGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPE 71
Cdd:TIGR02769 2 LLEVRDVTHTYrtgglfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 72 QR--VREGLAYVPQgrDIFSTL----TVEENI---LIGMAKFKGAKTRKVPEHLYEIFPILDEMKQRRGGDLSGGQQQQL 142
Cdd:TIGR02769 82 QRraFRRDVQLVFQ--DSPSAVnprmTVRQIIgepLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1832152097 143 AIARALASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQ 215
Cdd:TIGR02769 160 NIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEE 232
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-216 |
6.27e-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: 93.92 E-value: 6.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGS--HILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLspEQRVREGLA 79
Cdd:cd03247 1 LSINNVSFSYPEQeqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL--EKALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 80 YVPQGRDIFSTlTVEENIligmakfkgaktrkvpehlyeifpildemkqrrGGDLSGGQQQQLAIARALASEPKVLILDE 159
Cdd:cd03247 79 VLNQRPYLFDT-TLRNNL---------------------------------GRRFSGGERQRLALARILLQDAPIVLLDE 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1832152097 160 PTEGIQPSIIKDIGRVIRKLADSGEMAIVL-----VEQFydfaeelaDGYTVMARGQVIAQG 216
Cdd:cd03247 125 PTVGLDPITERQLLSLIFEVLKDKTLIWIThhltgIEHM--------DKILFLENGKIIMQG 178
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-221 |
9.71e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 95.92 E-value: 9.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFY-----GGSHI-LRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRV 74
Cdd:PRK13633 4 MIKCKNVSYKYesneeSTEKLaLDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 75 REGLAYVPQGRD--IFSTLtVEENILIGmakfkgaktrkvPEHL----YEIFPILDEMKQRRGGD---------LSGGQQ 139
Cdd:PRK13633 84 RNKAGMVFQNPDnqIVATI-VEEDVAFG------------PENLgippEEIRERVDESLKKVGMYeyrrhaphlLSGGQK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 140 QQLAIARALASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEElADGYTVMARGQVIAQGAGR 219
Cdd:PRK13633 151 QRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPK 229
|
..
gi 1832152097 220 EM 221
Cdd:PRK13633 230 EI 231
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
2-187 |
1.46e-23 |
|
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: 93.58 E-value: 1.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQrvREGLAYV 81
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP--HENILYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 82 PQGRDIFSTLTVEENiLIGMAKFKGAKTRKVPEHLYEIFpiLDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDEPT 161
Cdd:TIGR01189 79 GHLPGLKPELSALEN-LHFWAAIHGGAQRTIEDALAAVG--LTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPT 155
|
170 180
....*....|....*....|....*.
gi 1832152097 162 EGIQPSIIKDIGRVIRKLADSGEMAI 187
Cdd:TIGR01189 156 TALDKAGVALLAGLLRAHLARGGIVL 181
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-216 |
1.64e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 94.26 E-value: 1.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYggSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRvreGLAY 80
Cdd:PRK10771 1 MLKLTDITWLY--HHLPMRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRR---PVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 81 VPQGRDIFSTLTVEENILIGMA---KFKGAKTRKVPEHLYEIFpiLDEMKQRRGGDLSGGQQQQLAIARALASEPKVLIL 157
Cdd:PRK10771 76 LFQENNLFSHLTVAQNIGLGLNpglKLNAAQREKLHAIARQMG--IEDLLARLPGQLSGGQRQRVALARCLVREQPILLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1832152097 158 DEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQG 216
Cdd:PRK10771 154 DEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDG 212
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-161 |
2.59e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.44 E-value: 2.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLdGKDISrlspeqrvregLAY 80
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK-----------IGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 81 VPQGRDIF-STLTVEENI-----------LIGMAK---FKGAKTRKvpehlyeifPIldemkqrrgGDLSGGQQQQLAIA 145
Cdd:COG0488 383 FDQHQEELdPDKTVLDELrdgapggteqeVRGYLGrflFSGDDAFK---------PV---------GVLSGGEKARLALA 444
|
170
....*....|....*.
gi 1832152097 146 RALASEPKVLILDEPT 161
Cdd:COG0488 445 KLLLSPPNVLLLDEPT 460
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-225 |
3.17e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 94.43 E-value: 3.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGG--SHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRlSPEQRVREGL 78
Cdd:PRK13648 7 IIVFKNVSFQYQSdaSFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITD-DNFEKLRKHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 79 AYVPQGRD-IFSTLTVEENILIGMAKFK---GAKTRKVPEHLYEIfpildEMKQRRGGD---LSGGQQQQLAIARALASE 151
Cdd:PRK13648 86 GIVFQNPDnQFVGSIVKYDVAFGLENHAvpyDEMHRRVSEALKQV-----DMLERADYEpnaLSGGQKQRVAIAGVLALN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1832152097 152 PKVLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEqfYDFAEEL-ADGYTVMARGQVIAQGAGREMPEKG 225
Cdd:PRK13648 161 PSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISIT--HDLSEAMeADHVIVMNKGTVYKEGTPTEIFDHA 233
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-161 |
3.49e-23 |
|
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: 93.27 E-value: 3.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGS----HILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVR- 75
Cdd:COG4181 8 IIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 76 --EGLAYVPQGRDIFSTLTVEENILIGM--AKFKGAKTRKVPEhlyeifpiLDEM--KQRRG---GDLSGGQQQQLAIAR 146
Cdd:COG4181 88 raRHVGFVFQSFQLLPTLTALENVMLPLelAGRRDARARARAL--------LERVglGHRLDhypAQLSGGEQQRVALAR 159
|
170
....*....|....*
gi 1832152097 147 ALASEPKVLILDEPT 161
Cdd:COG4181 160 AFATEPAILFADEPT 174
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-221 |
3.67e-23 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 95.56 E-value: 3.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRvreGLAYV 81
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQR---DICMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 82 PQGRDIFSTLTVEENILIGMaKFKGAKTRKVPEHLYEIFPI--LDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDE 159
Cdd:PRK11432 84 FQSYALFPHMSLGENVGYGL-KMLGVPKEERKQRVKEALELvdLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1832152097 160 PTEGIQPSIIKDIGRVIRKLADSGEMAIVLV--EQFYDFAeeLADGYTVMARGQVIAQGAGREM 221
Cdd:PRK11432 163 PLSNLDANLRRSMREKIRELQQQFNITSLYVthDQSEAFA--VSDTVIVMNKGKIMQIGSPQEL 224
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
32-218 |
3.77e-23 |
|
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: 93.00 E-value: 3.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 32 VLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRvreGLAYVPQGRDIFSTLTVEENILIGMA---KFKGAK 108
Cdd:TIGR01277 29 IMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQR---PVSMLFQENNLFAHLTVRQNIGLGLHpglKLNAEQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 109 TRKVPEHLYEIFpiLDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIV 188
Cdd:TIGR01277 106 QEKVVDAAQQVG--IADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSERQRTLL 183
|
170 180 190
....*....|....*....|....*....|
gi 1832152097 189 LVEQFYDFAEELADGYTVMARGQVIAQGAG 218
Cdd:TIGR01277 184 MVTHHLSDARAIASQIAVVSQGKIKVVSDC 213
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
17-220 |
4.08e-23 |
|
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: 93.86 E-value: 4.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 17 LRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQ----RvREGLAYVPQGRDIFSTLT 92
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelR-RKKISMVFQSFALLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 93 VEENILIGM------AKFKGAKTRKVPEHLYeifpiLDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDEPTEGIQP 166
Cdd:cd03294 119 VLENVAFGLevqgvpRAEREERAAEALELVG-----LEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDP 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1832152097 167 SIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGRE 220
Cdd:cd03294 194 LIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEE 247
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
15-190 |
6.44e-23 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 96.15 E-value: 6.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 15 HILR--DVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILP-IKSGQILLDGKDISRLSPEQRVREGLAYVPQGRD---IF 88
Cdd:PRK13549 274 HIKRvdDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQAIAQGIAMVPEDRKrdgIV 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 89 STLTVEENI-LIGMAKFKGaktRKVPEHLYEIFPILDEMKQRRG---------GDLSGGQQQQLAIARALASEPKVLILD 158
Cdd:PRK13549 354 PVMGVGKNItLAALDRFTG---GSRIDDAAELKTILESIQRLKVktaspelaiARLSGGNQQKAVLAKCLLLNPKILILD 430
|
170 180 190
....*....|....*....|....*....|..
gi 1832152097 159 EPTEGIQPSIIKDIGRVIRKLADSGeMAIVLV 190
Cdd:PRK13549 431 EPTRGIDVGAKYEIYKLINQLVQQG-VAIIVI 461
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
14-223 |
7.46e-23 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 96.27 E-value: 7.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 14 SHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILP---IKSGQILLDGKDISRlsPEQRVREglAYVPQgRDIF-S 89
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLNGMPIDA--KEMRAIS--AYVQQ-DDLFiP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 90 TLTVEENiLIGMAKFKGAKTRKVPEHLYEIFPILDEMKQRRGGD-----------LSGGQQQQLAIARALASEPKVLILD 158
Cdd:TIGR00955 113 TLTVREH-LMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANtrigvpgrvkgLSGGERKRLAFASELLTDPPLLFCD 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1832152097 159 EPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREMPE 223
Cdd:TIGR00955 192 EPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-177 |
8.35e-23 |
|
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: 92.17 E-value: 8.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFY--GGSHILRDVSFQAP----VGACsvvlGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPeQRVR 75
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKpgekVGIV----GRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGL-HDLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 76 EGLAYVPQGRDIFSTlTVEENI-------------LIGMAKFKgaktrkvpEHLYEIFPILDEMKQRRGGDLSGGQQQQL 142
Cdd:cd03244 78 SRISIIPQDPVLFSG-TIRSNLdpfgeysdeelwqALERVGLK--------EFVESLPGGLDTVVEEGGENLSVGQRQLL 148
|
170 180 190
....*....|....*....|....*....|....*
gi 1832152097 143 AIARALASEPKVLILDEPTEGIQPSIIKDIGRVIR 177
Cdd:cd03244 149 CLARALLRKSKILVLDEATASVDPETDALIQKTIR 183
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-225 |
9.41e-23 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 92.29 E-value: 9.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVN-QFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQrVREGLAY 80
Cdd:cd03253 1 IEFENVTfAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDS-LRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 81 VPQGRDIFSTlTVEENILIGMAK------FKGAKTRKVPEHLyEIFP-----ILDEmkqrRGGDLSGGQQQQLAIARALA 149
Cdd:cd03253 80 VPQDTVLFND-TIGYNIRYGRPDatdeevIEAAKAAQIHDKI-MRFPdgydtIVGE----RGLKLSGGEKQRVAIARAIL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 150 SEPKVLILDEPTEGIQPSIIKDIGRVIRKLADsGEMAIVLveqfydfAEEL-----ADGYTVMARGQVIAQGAGREMPEK 224
Cdd:cd03253 154 KNPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVI-------AHRLstivnADKIIVLKDGRIVERGTHEELLAK 225
|
.
gi 1832152097 225 G 225
Cdd:cd03253 226 G 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-161 |
1.44e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.13 E-value: 1.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 4 VKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQIlldgkdisRLSPEQRVreglAYVPQ 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV--------SIPKGLRI----GYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 84 GRDIFSTLTVEENILIGMAKF------------KGAKTRKVPEHLYEIFPILDEMK----------------------QR 129
Cdd:COG0488 69 EPPLDDDLTVLDTVLDGDAELraleaeleeleaKLAEPDEDLERLAELQEEFEALGgweaearaeeilsglgfpeedlDR 148
|
170 180 190
....*....|....*....|....*....|..
gi 1832152097 130 RGGDLSGGQQQQLAIARALASEPKVLILDEPT 161
Cdd:COG0488 149 PVSELSGGWRRRVALARALLSEPDLLLLDEPT 180
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-190 |
1.88e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 91.31 E-value: 1.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEqRVREGLAY 80
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPE-IYRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 81 VPQGRDIFSTlTVEENILIGMAKFKGAKTRKVPEHLYEIFPILDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDEP 160
Cdd:PRK10247 86 CAQTPTLFGD-TVYDNLIFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEI 164
|
170 180 190
....*....|....*....|....*....|
gi 1832152097 161 TEGIQPSIIKDIGRVIRKLADSGEMAIVLV 190
Cdd:PRK10247 165 TSALDESNKHNVNEIIHRYVREQNIAVLWV 194
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-216 |
2.34e-22 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 94.78 E-value: 2.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSH-ILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSpEQRVREGLAY 80
Cdd:PRK10790 341 IDIDNVSFAYRDDNlVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLS-HSVLRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 81 VPQ---------------GRDIfstltVEENILIGMAKFKGAK-TRKVPEHLYEifpILDEmkqrRGGDLSGGQQQQLAI 144
Cdd:PRK10790 420 VQQdpvvladtflanvtlGRDI-----SEEQVWQALETVQLAElARSLPDGLYT---PLGE----QGNNLSVGQKQLLAL 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1832152097 145 ARALASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGEMaIVLVEQFYDFAEelADGYTVMARGQVIAQG 216
Cdd:PRK10790 488 ARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTL-VVIAHRLSTIVE--ADTILVLHRGQAVEQG 556
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-225 |
2.75e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 92.10 E-value: 2.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGG---SHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKdisRLSPEQ--RVR 75
Cdd:PRK13650 4 IIEVKNLTFKYKEdqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD---LLTEENvwDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 76 EGLAYVPQGRD-IFSTLTVEENILIGMAKfKGAKTRKVPEHLYEIFPILD--EMKQRRGGDLSGGQQQQLAIARALASEP 152
Cdd:PRK13650 81 HKIGMVFQNPDnQFVGATVEDDVAFGLEN-KGIPHEEMKERVNEALELVGmqDFKEREPARLSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1832152097 153 KVLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEqfYDFAE-ELADGYTVMARGQVIAQGAGREMPEKG 225
Cdd:PRK13650 160 KIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISIT--HDLDEvALSDRVLVMKNGQVESTSTPRELFSRG 231
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-221 |
3.09e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 91.65 E-value: 3.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 16 ILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGK------DISRLSPeQRVREGLAYVPQGRDIFS 89
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDA-IKLRKEVGMVFQQPNPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 90 TLTVEENILIGMaKFKGAKTRKvpehlyEIFPILDEMKQRRG-------------GDLSGGQQQQLAIARALASEPKVLI 156
Cdd:PRK14246 104 HLSIYDNIAYPL-KSHGIKEKR------EIKKIVEECLRKVGlwkevydrlnspaSQLSGGQQQRLTIARALALKPKVLL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1832152097 157 LDEPTEGIQPSIIKDIGRVIRKLADsgEMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREM 221
Cdd:PRK14246 177 MDEPTSMIDIVNSQAIEKLITELKN--EIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-216 |
3.74e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 94.12 E-value: 3.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFY--GGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSpEQRVREGLA 79
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYS-EAALRQAIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 80 YVPQGRDIFSTlTVEENILIGMAKFKGAKTRKV-----PEHLYEIFPILDEMKQRRGGDLSGGQQQQLAIARALASEPKV 154
Cdd:PRK11160 418 VVSQRVHLFSA-TLRDNLLLAAPNASDEALIEVlqqvgLEKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPL 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1832152097 155 LILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIV-----LVEQFydfaeelaDGYTVMARGQVIAQG 216
Cdd:PRK11160 497 LLLDEPTEGLDAETERQILELLAEHAQNKTVLMIthrltGLEQF--------DRICVMDNGQIIEQG 555
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
11-190 |
4.83e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 89.22 E-value: 4.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 11 YGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQIlldgkdisrlspEQRVREGLAYVPQGRDIFST 90
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV------------RRAGGARVAYVPQRSEVPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 91 L--TVEENILIGMAKFKG------AKTRKVPEHLYEIFPiLDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDEPTE 162
Cdd:NF040873 70 LplTVRDLVAMGRWARRGlwrrltRDDRAAVDDALERVG-LADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180
....*....|....*....|....*...
gi 1832152097 163 GIQPSIIKDIGRVIRKLADSGeMAIVLV 190
Cdd:NF040873 149 GLDAESRERIIALLAEEHARG-ATVVVV 175
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-216 |
6.71e-22 |
|
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: 89.12 E-value: 6.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGIlP---IKSGQILLDGKDISRLSPEQRVREGL 78
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH-PkyeVTEGEILFKGEDITDLPPEERARLGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 79 AYVPQGRDIFSTLTVEENIligmakfkgaktRKVPEhlyeifpildemkqrrggDLSGGQQQQLAIARALASEPKVLILD 158
Cdd:cd03217 80 FLAFQYPPEIPGVKNADFL------------RYVNE------------------GFSGGEKKRNEILQLLLLEPDLAILD 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1832152097 159 EPTEGIQPSIIKDIGRVIRKLADSGeMAIVLV---EQFYDFAEelADGYTVMARGQVIAQG 216
Cdd:cd03217 130 EPDSGLDIDALRLVAEVINKLREEG-KSVLIIthyQRLLDYIK--PDRVHVLYDGRIVKSG 187
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
1-161 |
1.26e-21 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 89.01 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSHI----LRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRV-- 74
Cdd:NF038007 1 MLNMQNAEKCYITKTIktkvLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIil 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 75 -REGLAYVPQGRDIFSTLTVEENILIGMaKFKG-AKTRKVPE--HLYEIFPIlDEMKQRRGGDLSGGQQQQLAIARALAS 150
Cdd:NF038007 81 rRELIGYIFQSFNLIPHLSIFDNVALPL-KYRGvAKKERIERvnQVLNLFGI-DNRRNHKPMQLSGGQQQRVAIARAMVS 158
|
170
....*....|.
gi 1832152097 151 EPKVLILDEPT 161
Cdd:NF038007 159 NPALLLADEPT 169
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-224 |
1.33e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 90.24 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSH--ILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGIL---PIKSGQILLDGKDISRLSPEQrVRE 76
Cdd:PRK13640 6 VEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWD-IRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 77 GLAYVPQGRD-IFSTLTVEENILIGMakfkgaKTRKVPEHlyEIFPILDEMKQRRG---------GDLSGGQQQQLAIAR 146
Cdd:PRK13640 85 KVGIVFQNPDnQFVGATVGDDVAFGL------ENRAVPRP--EMIKIVRDVLADVGmldyidsepANLSGGQKQRVAIAG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1832152097 147 ALASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAeELADGYTVMARGQVIAQGAGREMPEK 224
Cdd:PRK13640 157 ILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
16-160 |
1.46e-21 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 88.30 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 16 ILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGkdisrlspeqrvreGLAYVPQGRDIFSTlTVEE 95
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--------------SIAYVSQEPWIQNG-TIRE 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1832152097 96 NILIGmAKFKGAKTRKVPE--HLY---EIFPILDE-MKQRRGGDLSGGQQQQLAIARALASEPKVLILDEP 160
Cdd:cd03250 85 NILFG-KPFDEERYEKVIKacALEpdlEILPDGDLtEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDP 154
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
16-221 |
1.75e-21 |
|
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: 92.41 E-value: 1.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 16 ILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQrVREGLAYVPQGRDIFSTlTVEE 95
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRET-FGKHIGYLPQDVELFPG-TVAE 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 96 NIligmAKFKGAKTrkvPEHLYEIFPILD--EMKQR-----------RGGDLSGGQQQQLAIARALASEPKVLILDEP-- 160
Cdd:TIGR01842 411 NI----ARFGENAD---PEKIIEAAKLAGvhELILRlpdgydtvigpGGATLSGGQRQRIALARALYGDPKLVVLDEPns 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1832152097 161 ---TEGIQpSIIKDIGRVIRKladsgeMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREM 221
Cdd:TIGR01842 484 nldEEGEQ-ALANAIKALKAR------GITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEV 540
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-178 |
2.25e-21 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 87.85 E-value: 2.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGG--SHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLsPEQRVREGLA 79
Cdd:cd03369 7 IEVENLSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTI-PLEDLRSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 80 YVPQGRDIFSTlTVEENIligmakfkgaktrkVPEHLYEIFPILDEMKQRRGGD-LSGGQQQQLAIARALASEPKVLILD 158
Cdd:cd03369 86 IIPQDPTLFSG-TIRSNL--------------DPFDEYSDEEIYGALRVSEGGLnLSQGQRQLLCLARALLKRPRVLVLD 150
|
170 180
....*....|....*....|
gi 1832152097 159 EPTEGIQPSIIKDIGRVIRK 178
Cdd:cd03369 151 EATASIDYATDALIQKTIRE 170
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
16-161 |
2.25e-21 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 88.75 E-value: 2.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 16 ILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPeQRVREGLAYVPQGRDIFSTlTVEE 95
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNL-RWLRSQIGLVSQEPVLFDG-TIAE 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1832152097 96 NILIGmakfKGAKTRKVPEH---LYEI------FPI-LDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDEPT 161
Cdd:cd03249 96 NIRYG----KPDATDEEVEEaakKANIhdfimsLPDgYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEAT 167
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
15-216 |
2.59e-21 |
|
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: 91.81 E-value: 2.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 15 HILR--DVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIK-SGQILLDGKDISRLSPEQRVREGLAYVPQGRD---IF 88
Cdd:TIGR02633 272 HRKRvdDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKrhgIV 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 89 STLTVEENILigMAKFKGAKTRKVPEHLYEIFPILDEMKQRRG---------GDLSGGQQQQLAIARALASEPKVLILDE 159
Cdd:TIGR02633 352 PILGVGKNIT--LSVLKSFCFKMRIDAAAELQIIGSAIQRLKVktaspflpiGRLSGGNQQKAVLAKMLLTNPRVLILDE 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1832152097 160 PTEGIQPSIIKDIGRVIRKLADSGeMAIVLVeqfydfAEELADGYTVMARGQVIAQG 216
Cdd:TIGR02633 430 PTRGVDVGAKYEIYKLINQLAQEG-VAIIVV------SSELAEVLGLSDRVLVIGEG 479
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-228 |
3.04e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 89.02 E-value: 3.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFY-GGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRlSPEQRVREGLAY 80
Cdd:PRK13647 5 IEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNA-ENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 81 VPQGRD--IFSTlTVEENILIGMAKFkGAKTRKVPEHLYEIFPILD--EMKQRRGGDLSGGQQQQLAIARALASEPKVLI 156
Cdd:PRK13647 84 VFQDPDdqVFSS-TVWDDVAFGPVNM-GLDKDEVERRVEEALKAVRmwDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1832152097 157 LDEPTEGIQPSIIKDIGRVIRKLADSGEmAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREMPEKGIRE 228
Cdd:PRK13647 162 LDEPMAYLDPRGQETLMEILDRLHNQGK-TVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIVE 232
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-223 |
4.18e-21 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 88.67 E-value: 4.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQ--RVREGL 78
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRlyTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 79 AYVPQGRDIFSTLTVEENILIGMAKfkgaKTRKVPEHLYEIFPILDEMKQRRGG------DLSGGQQQQLAIARALASEP 152
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVAYPLRE----HTQLPAPLLHSTVMMKLEAVGLRGAaklmpsELSGGMARRAALARAIALEP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1832152097 153 KVLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEqfYDFAEEL--ADGYTVMARGQVIAQGAGREMPE 223
Cdd:PRK11831 163 DLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVS--HDVPEVLsiADHAYIVADKKIVAHGSAQALQA 233
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-226 |
4.67e-21 |
|
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: 91.04 E-value: 4.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKS--GQILLDGKDISRLSPEQRVREGL 78
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 79 AYVPQGRDIFSTLTVEENILIGMA-KFKG------AKTRKVPEHLYEIfpILDEMKQRRG-GDLSGGQQQQLAIARALAS 150
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNEiTLPGgrmaynAMYLRAKNLLREL--QLDADNVTRPvGDYGGGQQQLVEIAKALNK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1832152097 151 EPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGeMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREMPEKGI 226
Cdd:TIGR02633 159 QARLLILDEPSSSLTEKETEILLDIIRDLKAHG-VACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDI 233
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-221 |
6.54e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 87.91 E-value: 6.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCL--MGILPIK---SGQILLDGKDI-SRLSPEQRV 74
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIySPRTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 75 REGLAYVPQGRDIFStLTVEENILIGMaKFKGAKTRKVPEHLYEI----FPILDEMKQRRGGD---LSGGQQQQLAIARA 147
Cdd:PRK14239 85 RKEIGMVFQQPNPFP-MSIYENVVYGL-RLKGIKDKQVLDEAVEKslkgASIWDEVKDRLHDSalgLSGGQQQRVCIARV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1832152097 148 LASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVL--VEQfydfAEELADGYTVMARGQVIAQGAGREM 221
Cdd:PRK14239 163 LATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTrsMQQ----ASRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
17-216 |
8.02e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 88.26 E-value: 8.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 17 LRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVRE-----GLAYVPQGRDIFSTl 91
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQirkkvGLVFQFPESQLFEE- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 92 TVEENILIGMAKFKGAK--TRKVPEHLYEIFPILDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDEPTEGIQPSII 169
Cdd:PRK13649 102 TVLKDVAFGPQNFGVSQeeAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1832152097 170 KDIGRVIRKLADSGeMAIVLVEQFYDFAEELADGYTVMARGQVIAQG 216
Cdd:PRK13649 182 KELMTLFKKLHQSG-MTIVLVTHLMDDVANYADFVYVLEKGKLVLSG 227
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-229 |
1.10e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 89.99 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKS--GQILLDGKDISRLSPEQRVREGL 78
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQASNIRDTERAGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 79 AYVPQGRDIFSTLTVEENILIGMAKFKG------AKTRKVPEHLYEIFpiLDEMKQRRGGDLSGGQQQQLAIARALASEP 152
Cdd:PRK13549 85 AIIHQELALVKELSVLENIFLGNEITPGgimdydAMYLRAQKLLAQLK--LDINPATPVGNLGLGQQQLVEIAKALNKQA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 153 KVLILDEPTEGIQPSIIKDIGRVIRKLADSGeMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREMPEKGI------ 226
Cdd:PRK13549 163 RLLILDEPTASLTESETAVLLDIIRDLKAHG-IACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDIitmmvg 241
|
...
gi 1832152097 227 REL 229
Cdd:PRK13549 242 REL 244
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
19-161 |
1.23e-20 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 88.25 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 19 DVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQ--RVREGLAYVPQgrDIFSTL----- 91
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRElrPLRRRMQMVFQ--DPYASLnprmt 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 92 ---TVEENILI-GMAKFKGAKTR------KV---PEHLyeifpildemkQRRGGDLSGGQQQQLAIARALASEPKVLILD 158
Cdd:COG4608 114 vgdIIAEPLRIhGLASKAERRERvaelleLVglrPEHA-----------DRYPHEFSGGQRQRIGIARALALNPKLIVCD 182
|
...
gi 1832152097 159 EPT 161
Cdd:COG4608 183 EPV 185
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-220 |
1.36e-20 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 89.80 E-value: 1.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 3 EVKDVNQFYGGSHILRDVSFQAPVGaCSVVL-GRNGVGKTTLLKCLMGILPIKSGQILLDGKDISrlspEQRVREGL--- 78
Cdd:NF033858 3 RLEGVSHRYGKTVALDDVSLDIPAG-CMVGLiGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA----DARHRRAVcpr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 79 -AYVPQ--GRDIFSTLTVEENI-----LIGMAkfKGAKTRKVPEHLYE--IFPILDemkqRRGGDLSGGQQQQLAIARAL 148
Cdd:NF033858 78 iAYMPQglGKNLYPTLSVFENLdffgrLFGQD--AAERRRRIDELLRAtgLAPFAD----RPAGKLSGGMKQKLGLCCAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 149 ASEPKVLILDEPTEGIQP-------SIIKDIgRvirklADSGEMAiVLVEQFY-DFAEELaDGYTVMARGQVIAQGAGRE 220
Cdd:NF033858 152 IHDPDLLILDEPTTGVDPlsrrqfwELIDRI-R-----AERPGMS-VLVATAYmEEAERF-DWLVAMDAGRVLATGTPAE 223
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-160 |
2.78e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 86.29 E-value: 2.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVreglay 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGV------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 81 VPQGRDIFSTLTVEENILIGMaKFKGAKTRKVPEHLYEIFPI--LDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILD 158
Cdd:PRK11248 75 VFQNEGLLPWRNVQDNVAFGL-QLAGVEKMQRLEIAHQMLKKvgLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLD 153
|
..
gi 1832152097 159 EP 160
Cdd:PRK11248 154 EP 155
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-190 |
4.19e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 85.86 E-value: 4.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKS-----GQILLDGKDI-SRLSPEQRVR 75
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyERRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 76 EGLAYVPQGRDIFStLTVEENILIGMaKFKGAKTR----KVPEHLYEIFPILDEMK---QRRGGDLSGGQQQQLAIARAL 148
Cdd:PRK14258 88 RQVSMVHPKPNLFP-MSVYDNVAYGV-KIVGWRPKleidDIVESALKDADLWDEIKhkiHKSALDLSGGQQQRLCIARAL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1832152097 149 ASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLV 190
Cdd:PRK14258 166 AVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIV 207
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-161 |
5.06e-20 |
|
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: 84.79 E-value: 5.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDV-------NQfyGGSHI--LRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGK----DISR 67
Cdd:COG4778 4 LLEVENLsktftlhLQ--GGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 68 LSPEQ--RVREG-LAYVPQgrdiF-------STLTVEENILI--GMAKfKGAKTR--------KVPEHLYEIFPildemk 127
Cdd:COG4778 82 ASPREilALRRRtIGYVSQ----FlrviprvSALDVVAEPLLerGVDR-EEARARarellarlNLPERLWDLPP------ 150
|
170 180 190
....*....|....*....|....*....|....
gi 1832152097 128 qrrgGDLSGGQQQQLAIARALASEPKVLILDEPT 161
Cdd:COG4778 151 ----ATFSGGEQQRVNIARGFIADPPLLLLDEPT 180
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-232 |
7.81e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 85.45 E-value: 7.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGG--SHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKdisRLSPEQ--RVREG 77
Cdd:PRK13635 6 IRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VLSEETvwDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 78 LAYVPQGRD-IFSTLTVEENILIGMakfkgaKTRKVPEHlyEIFPILDEMKQRRG---------GDLSGGQQQQLAIARA 147
Cdd:PRK13635 83 VGMVFQNPDnQFVGATVQDDVAFGL------ENIGVPRE--EMVERVDQALRQVGmedflnrepHRLSGGQKQRVAIAGV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 148 LASEPKVLILDEPTegiqpSIIKDIGR-----VIRKLADSGEMAIVLVEQFYDFAEElADGYTVMARGQVIAQGAGREMP 222
Cdd:PRK13635 155 LALQPDIIILDEAT-----SMLDPRGRrevleTVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF 228
|
250
....*....|
gi 1832152097 223 EKGiRELVAI 232
Cdd:PRK13635 229 KSG-HMLQEI 237
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
14-161 |
8.89e-20 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 84.06 E-value: 8.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 14 SHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISrLSPEQRVREGLAYVPQGRDIFSTlTV 93
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIS-QYEHKYLHSKVSLVGQEPVLFAR-SL 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1832152097 94 EENILIGMAkfkGAKTRKVPE-----HLYEIFPIL----DEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDEPT 161
Cdd:cd03248 105 QDNIAYGLQ---SCSFECVKEaaqkaHAHSFISELasgyDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEAT 178
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
2-220 |
1.12e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 84.35 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGI--LPIKSGQILLDGKDISRLSPEQRVREGLA 79
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPDERARAGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 80 YVPQ------G---RDIFST-LTVEENILIGMAKFKgaktRKVPEHLYEIfpildEMKQ---RRG--GDLSGGQQQQLAI 144
Cdd:COG0396 81 LAFQypveipGvsvSNFLRTaLNARRGEELSAREFL----KLLKEKMKEL-----GLDEdflDRYvnEGFSGGEKKRNEI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1832152097 145 ARALASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSgEMAIVLV---EQFYDFAEelADGYTVMARGQVIAQGaGRE 220
Cdd:COG0396 152 LQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSP-DRGILIIthyQRILDYIK--PDFVHVLVDGRIVKSG-GKE 226
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-161 |
1.37e-19 |
|
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: 81.73 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKdisrlspeqrvrEGLAYV 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST------------VKIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 82 PQgrdifstltveeniligmakfkgaktrkvpehlyeifpildemkqrrggdLSGGQQQQLAIARALASEPKVLILDEPT 161
Cdd:cd03221 69 EQ--------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPT 98
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-229 |
1.53e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 86.60 E-value: 1.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVREGLAY 80
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGIGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 81 VPQGRDIFSTLTVEENILIGMaKFKGAKTRKVPEHLY-EIFPILDEMK-----QRRGGDLSGGQQQQLAIARALASEPKV 154
Cdd:PRK10762 84 IHQELNLIPQLTIAENIFLGR-EFVNRFGRIDWKKMYaEADKLLARLNlrfssDKLVGELSIGEQQMVEIAKVLSFESKV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 155 LILDEPTEGIQPSIIKDIGRVIRKLADSGeMAIV-----LVEQFydfaeELADGYTVMARGQVIAQGAGREMPEKGIREL 229
Cdd:PRK10762 163 IIMDEPTDALTDTETESLFRVIRELKSQG-RGIVyishrLKEIF-----EICDDVTVFRDGQFIAEREVADLTEDSLIEM 236
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
5-214 |
1.71e-19 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 86.32 E-value: 1.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 5 KDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVREGLAYVPQG 84
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 85 RDIFSTLTVEENILIGMAKFKG--AKTRKVPEHLYEIFPILD-EMKQR-RGGDLSGGQQQQLAIARALASEPKVLILDEP 160
Cdd:PRK10982 82 LNLVLQRSVMDNMWLGRYPTKGmfVDQDKMYRDTKAIFDELDiDIDPRaKVATLSVSQMQMIEIAKAFSYNAKIVIMDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1832152097 161 TEGIQPSIIKDIGRVIRKLADSGeMAIVLVEQFYDFAEELADGYTVMARGQVIA 214
Cdd:PRK10982 162 TSSLTEKEVNHLFTIIRKLKERG-CGIVYISHKMEEIFQLCDEITILRDGQWIA 214
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-221 |
1.76e-19 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 86.69 E-value: 1.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHI--LRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSpEQRVREGLA 79
Cdd:TIGR02203 331 VEFRNVTFRYPGRDRpaLDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT-LASLRRQVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 80 YVPQGRDIFSTlTVEENILIG-MAKFKGAKTRKVPEHLYEIFPI------LDEMKQRRGGDLSGGQQQQLAIARALASEP 152
Cdd:TIGR02203 410 LVSQDVVLFND-TIANNIAYGrTEQADRAEIERALAAAYAQDFVdklplgLDTPIGENGVLLSGGQRQRLAIARALLKDA 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1832152097 153 KVLILDEPTEGIQPSIIKDIGRVIRKLADsGEMAIVLVEQFYDFaeELADGYTVMARGQVIAQGAGREM 221
Cdd:TIGR02203 489 PILILDEATSALDNESERLVQAALERLMQ-GRTTLVIAHRLSTI--EKADRIVVMDDGRIVERGTHNEL 554
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-210 |
1.79e-19 |
|
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: 83.67 E-value: 1.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 17 LRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVreglayVPQGRDIFSTLTVEEN 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV------VFQNYSLLPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 97 ILIG----MAKFKGAKTRKVPEHLYEIFPiLDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDEPTEGIQPSIIKDI 172
Cdd:TIGR01184 75 IALAvdrvLPDLSKSERRAIVEEHIALVG-LTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 1832152097 173 GRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARG 210
Cdd:TIGR01184 154 QEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-216 |
2.45e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 84.40 E-value: 2.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYG-----GSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVR 75
Cdd:PRK13643 1 MIKFEKVNYTYQpnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 76 E-----GLAYVPQGRDIFSTlTVEENILIGMAKFKGAK--TRKVPEHLYEIFPILDEMKQRRGGDLSGGQQQQLAIARAL 148
Cdd:PRK13643 81 PvrkkvGVVFQFPESQLFEE-TVLKDVAFGPQNFGIPKekAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGIL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1832152097 149 ASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGEmAIVLVEQFYDFAEELADGYTVMARGQVIAQG 216
Cdd:PRK13643 160 AMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQ-TVVLVTHLMDDVADYADYVYLLEKGHIISCG 226
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-216 |
2.99e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 83.88 E-value: 2.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFY-GGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVREGLA 79
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 80 YVPQGRDI-FSTLTVEENILIGMAKFKGAKT---RKVPEHLYEIFpiLDEMKQRRGGDLSGGQQQQLAIARALASEPKVL 155
Cdd:PRK13644 81 IVFQNPETqFVGRTVEEDLAFGPENLCLPPIeirKRVDRALAEIG--LEKYRHRSPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1832152097 156 ILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFydfaEEL--ADGYTVMARGQVIAQG 216
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNL----EELhdADRIIVMDRGKIVLEG 217
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
13-221 |
3.61e-19 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 83.30 E-value: 3.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 13 GSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVREgLAYVPQGRDIFSTLT 92
Cdd:PRK10575 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARK-VAYLPQQLPAAEGMT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 93 VEENILIG-------MAKFKGAKTRKVPEHLYEIFpiLDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDEPTEGIQ 165
Cdd:PRK10575 102 VRELVAIGrypwhgaLGRFGAADREKVEEAISLVG--LKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1832152097 166 PSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREM 221
Cdd:PRK10575 180 IAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
3-161 |
4.06e-19 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 85.40 E-value: 4.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 3 EVKDVNQFYGGS-HILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSpEQRVREGLAYV 81
Cdd:PRK13657 336 EFDDVSFSYDNSrQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT-RASLRRNIAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 82 PQGRDIFSTlTVEENILIGmakfkgaKTRKVPEHLYEIFPI-------------LDEMKQRRGGDLSGGQQQQLAIARAL 148
Cdd:PRK13657 415 FQDAGLFNR-SIEDNIRVG-------RPDATDEEMRAAAERaqahdfierkpdgYDTVVGERGRQLSGGERQRLAIARAL 486
|
170
....*....|...
gi 1832152097 149 ASEPKVLILDEPT 161
Cdd:PRK13657 487 LKDPPILILDEAT 499
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-221 |
4.48e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 83.22 E-value: 4.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 11 YGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPI-----KSGQILLDGKDISRLSPEQRVREGLAYVPQGR 85
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYRDVLEFRRRVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 86 DIFStLTVEENILIGM--------AKFKGAKTRKVPEhlyeiFPILDEMKQRRGGD---LSGGQQQQLAIARALASEPKV 154
Cdd:PRK14271 111 NPFP-MSIMDNVLAGVrahklvprKEFRGVAQARLTE-----VGLWDAVKDRLSDSpfrLSGGQQQLLCLARTLAVNPEV 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1832152097 155 LILDEPTEGIQPSIIKDIGRVIRKLADsgEMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREM 221
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKIEEFIRSLAD--RLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-217 |
5.23e-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: 85.12 E-value: 5.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVN-QFYGGSHILR----------DVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPiKSGQILLDGKDISRLSP 70
Cdd:COG4172 276 LEARDLKvWFPIKRGLFRrtvghvkavdGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 71 EQ--RVREGLAYVPQgrDIFSTL----TVEENILIGMAKFKGAKTRKvpEHLYEIFPILDE------MKQRRGGDLSGGQ 138
Cdd:COG4172 355 RAlrPLRRRMQVVFQ--DPFGSLsprmTVGQIIAEGLRVHGPGLSAA--ERRARVAEALEEvgldpaARHRYPHEFSGGQ 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 139 QQQLAIARALASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEqfYDFA--EELADGYTVMARGQVIAQG 216
Cdd:COG4172 431 RQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFIS--HDLAvvRALAHRVMVMKDGKVVEQG 508
|
.
gi 1832152097 217 A 217
Cdd:COG4172 509 P 509
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
2-192 |
6.90e-19 |
|
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: 81.39 E-value: 6.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEqrVREGLAYV 81
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDS--IARGLLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 82 PQGRDIFSTLTVEENiLIGMAKFKGAKTrkvpehlyeIFPILDEMKQRRGGD-----LSGGQQQQLAIARALASEPKVLI 156
Cdd:cd03231 79 GHAPGIKTTLSVLEN-LRFWHADHSDEQ---------VEEALARVGLNGFEDrpvaqLSAGQQRRVALARLLLSGRPLWI 148
|
170 180 190
....*....|....*....|....*....|....*.
gi 1832152097 157 LDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQ 192
Cdd:cd03231 149 LDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQ 184
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-161 |
7.08e-19 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 84.69 E-value: 7.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHI--LRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDIS--RLSpeqRVREG 77
Cdd:PRK11176 342 IEFRNVTFTYPGKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRdyTLA---SLRNQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 78 LAYVPQGRDIFSTlTVEENILIGMAKF-------KGAKTRKVPEHLYEIFPILDEMKQRRGGDLSGGQQQQLAIARALAS 150
Cdd:PRK11176 419 VALVSQNVHLFND-TIANNIAYARTEQysreqieEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLR 497
|
170
....*....|.
gi 1832152097 151 EPKVLILDEPT 161
Cdd:PRK11176 498 DSPILILDEAT 508
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-221 |
7.15e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 82.75 E-value: 7.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDisrLSPEQR----VRE 76
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKP---LDYSKRgllaLRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 77 GLAYVPQGRD--IFSTlTVEENILIGMAKFkGAKTRKVPEHLYEIFPILD--EMKQRRGGDLSGGQQQQLAIARALASEP 152
Cdd:PRK13638 78 QVATVFQDPEqqIFYT-DIDSDIAFSLRNL-GVPEAEITRRVDEALTLVDaqHFRHQPIQCLSHGQKKRVAIAGALVLQA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1832152097 153 KVLILDEPTEGIQPSIIKDIGRVIRKLADSGEMaIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREM 221
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNH-VIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV 223
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
16-216 |
1.28e-18 |
|
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: 80.38 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 16 ILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIK---SGQILLDGKDISRLSpeQRVREGLAYVPQGRDIFSTLT 92
Cdd:cd03233 22 ILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFA--EKYPGEIIYVSEEDVHFPTLT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 93 VEENILIGmAKFKGaktrkvpehlyeifpilDEMKqrRGgdLSGGQQQQLAIARALASEPKVLILDEPTEGIQPSIIKDI 172
Cdd:cd03233 100 VRETLDFA-LRCKG-----------------NEFV--RG--ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1832152097 173 GRVIRKLADSGEM-AIVLVEQFYDFAEELADGYTVMARGQVIAQG 216
Cdd:cd03233 158 LKCIRTMADVLKTtTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-212 |
1.30e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 83.81 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 20 VSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVREGLAYVPQGRD---IFSTLTVEEN 96
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMLCPEDRKaegIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 97 ILIGMAKF--------KGAKTRKVPEHLYEIFPILDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDEPTEGIQPSI 168
Cdd:PRK11288 352 INISARRHhlragcliNNRWEAENADRFIRSLNIKTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGA 431
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1832152097 169 IKDIGRVIRKLADSGeMAIVLVEQfyDFAEEL--ADGYTVMARGQV 212
Cdd:PRK11288 432 KHEIYNVIYELAAQG-VAVLFVSS--DLPEVLgvADRIVVMREGRI 474
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
16-161 |
1.37e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 81.02 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 16 ILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSP----EQRVREgLAYVPQGRDIFSTL 91
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakaELRNQK-LGFIYQFHHLLPDF 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1832152097 92 TVEENI----LIGMAKFKGAKTRKVpEHLYEIFpiLDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDEPT 161
Cdd:PRK11629 103 TALENVamplLIGKKKPAEINSRAL-EMLAAVG--LEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPT 173
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1-216 |
1.55e-18 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 82.61 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFygGSHILrDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGK---DISR---LSPEQRv 74
Cdd:PRK11144 1 MLELNFKQQL--GDLCL-TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEKgicLPPEKR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 75 REGlaYVPQGRDIFSTLTVEENILIGMAKFKGAKTRKVP-----EHLYEIFPIldemkqrrggDLSGGQQQQLAIARALA 149
Cdd:PRK11144 77 RIG--YVFQDARLFPHYKVRGNLRYGMAKSMVAQFDKIVallgiEPLLDRYPG----------SLSGGEKQRVAIGRALL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1832152097 150 SEPKVLILDEPTEGIqpsiikDIGR------VIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQG 216
Cdd:PRK11144 145 TAPELLLMDEPLASL------DLPRkrellpYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFG 211
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-161 |
1.61e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 83.70 E-value: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVN-QFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILL-DGKDISRLS-----PEQR 73
Cdd:COG4178 362 ALALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLFLPqrpylPLGT 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 74 VREGLAYvPQGRDIFSTLTVEEnILigmakfkgaktRKVpeHLYEIFPILDEmKQRRGGDLSGGQQQQLAIARALASEPK 153
Cdd:COG4178 442 LREALLY-PATAEAFSDAELRE-AL-----------EAV--GLGHLAERLDE-EADWDQVLSLGEQQRLAFARLLLHKPD 505
|
....*...
gi 1832152097 154 VLILDEPT 161
Cdd:COG4178 506 WLFLDEAT 513
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-216 |
1.82e-18 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 81.13 E-value: 1.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGK-----DISRLS-PEQR- 73
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSeAERRr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 74 -VREGLAYVPQG-RD-IFSTLTVEENI---LIGM-AKFKGAKTRKVPEHLYEIfpildEMKQRRGGDL----SGGQQQQL 142
Cdd:PRK11701 86 lLRTEWGFVHQHpRDgLRMQVSAGGNIgerLMAVgARHYGDIRATAGDWLERV-----EIDAARIDDLpttfSGGMQQRL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1832152097 143 AIARALASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQG 216
Cdd:PRK11701 161 QIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
30-221 |
3.74e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 81.21 E-value: 3.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 30 SVVLGRNGVGKTTLLKCLMGILPIKSGQILLDG----KDISRLSPEQRVRE--GLAYVPQGRDIFSTlTVEENILIG--- 100
Cdd:PRK13645 40 TCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKKIKEVKRLRKeiGLVFQFPEYQLFQE-TIEKDIAFGpvn 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 101 MAKFKGAKTRKVPEhLYEIFPILDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDEPTEGIQPSIIKDIGRVIRKLA 180
Cdd:PRK13645 119 LGENKQEAYKKVPE-LLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLN 197
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1832152097 181 DSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREM 221
Cdd:PRK13645 198 KEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEI 238
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
6-221 |
4.43e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 80.52 E-value: 4.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 6 DVNQFYGgshilrdVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKdisRLSPEQ--RVREGLAYVPQ 83
Cdd:PRK13642 19 DVNQLNG-------VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE---LLTAENvwNLRRKIGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 84 GRD-IFSTLTVEENILIGMAKF---KGAKTRKVPEHLYEIfPILDeMKQRRGGDLSGGQQQQLAIARALASEPKVLILDE 159
Cdd:PRK13642 89 NPDnQFVGATVEDDVAFGMENQgipREEMIKRVDEALLAV-NMLD-FKTREPARLSGGQKQRVAVAGIIALRPEIIILDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1832152097 160 PTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEElADGYTVMARGQVIAQGAGREM 221
Cdd:PRK13642 167 STSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSEL 227
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-188 |
8.18e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 79.83 E-value: 8.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCL--MGILpIKS----GQILLDGKDI--SRLSP-EQ 72
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDL-IPGfrveGKVTFHGKNLyaPDVDPvEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 73 RVREGLAYvpQGRDIFSTlTVEENILIG--MAKFKGAKTRKVPEHLYEIfPILDEMKQR---RGGDLSGGQQQQLAIARA 147
Cdd:PRK14243 90 RRRIGMVF--QKPNPFPK-SIYDNIAYGarINGYKGDMDELVERSLRQA-ALWDEVKDKlkqSGLSLSGGQQQRLCIARA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1832152097 148 LASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIV 188
Cdd:PRK14243 166 IAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIV 206
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-175 |
9.92e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 78.76 E-value: 9.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFY-GGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQR--VREG 77
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVpfLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 78 LAYVPQGRDIFSTLTVEENILIGM--AKFKGAKTRKVPEHLYEIFPILDEMKQrRGGDLSGGQQQQLAIARALASEPKVL 155
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLiiAGASGDDIRRRVSAALDKVGLLDKAKN-FPIQLSGGEQQRVGIARAVVNKPAVL 159
|
170 180
....*....|....*....|
gi 1832152097 156 ILDEPTEGIQPSIIKDIGRV 175
Cdd:PRK10908 160 LADEPTGNLDDALSEGILRL 179
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-214 |
1.15e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 81.11 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVREGLAYV 81
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGVAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 82 PQGRDIFSTLTVEENILIGM--AKF----KGAKTRKVPEHLYEIFPILDemKQRRGGDLSGGQQQQLAIARALASEPKVL 155
Cdd:PRK11288 85 YQELHLVPEMTVAENLYLGQlpHKGgivnRRLLNYEAREQLEHLGVDID--PDTPLKYLSIGQRQMVEIAKALARNARVI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1832152097 156 ILDEPTEGIQPSIIKDIGRVIRKLADSGEmAIVLVEQFYDFAEELADGYTVMARGQVIA 214
Cdd:PRK11288 163 AFDEPTSSLSAREIEQLFRVIRELRAEGR-VILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-221 |
1.20e-17 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 79.49 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIK--------SGQILLDGKDISRLSPEQ 72
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 73 --RVReglAYVPQGRDIFSTLTVEENILIGM---AKFKGAKTRKVPEhlyeifpILDEMKQRRGGD---------LSGGQ 138
Cdd:PRK13547 81 laRLR---AVLPQAAQPAFAFSAREIVLLGRyphARRAGALTHRDGE-------IAWQALALAGATalvgrdvttLSGGE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 139 QQQLAIARALA---------SEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMAR 209
Cdd:PRK13547 151 LARVQFARVLAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLAD 230
|
250
....*....|..
gi 1832152097 210 GQVIAQGAGREM 221
Cdd:PRK13547 231 GAIVAHGAPADV 242
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1-212 |
3.37e-17 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 79.77 E-value: 3.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGShiLRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVREGLAY 80
Cdd:PRK10982 250 ILEVRNLTSLRQPS--IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHGFAL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 81 VPQGR---DIFSTLTVEENILIG-MAKFKGA----KTRKVPEhlyEIFPILDEMK------QRRGGDLSGGQQQQLAIAR 146
Cdd:PRK10982 328 VTEERrstGIYAYLDIGFNSLISnIRNYKNKvgllDNSRMKS---DTQWVIDSMRvktpghRTQIGSLSGGNQQKVIIGR 404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1832152097 147 ALASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFydfaEEL---ADGYTVMARGQV 212
Cdd:PRK10982 405 WLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEM----PELlgiTDRILVMSNGLV 469
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
13-216 |
7.83e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 78.73 E-value: 7.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 13 GSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKsGQILLDGKDISRLSPEQrVREGLAYVPQGRDIFSTlT 92
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRELDPES-WRKHLSWVGQNPQLPHG-T 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 93 VEENILIGM-----AKFKGAKTR-KVPEHLYEIFPILDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDEPTEGIqp 166
Cdd:PRK11174 439 LRDNVLLGNpdasdEQLQQALENaWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASL-- 516
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1832152097 167 siikDIG---RVIRKL--ADSGEMAIVLVEQFYDFAEelADGYTVMARGQVIAQG 216
Cdd:PRK11174 517 ----DAHseqLVMQALnaASRRQTTLMVTHQLEDLAQ--WDQIWVMQDGQIVQQG 565
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
16-161 |
8.12e-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: 78.71 E-value: 8.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 16 ILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQrVREGLAYVPQGRDIFSTlTVEE 95
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQAS-LRAAIGIVPQDTVLFND-TIAY 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 96 NILIG--------------MAK---F-----KGAKTRkVPEhlyeifpildemkqrRGGDLSGGQQQQLAIARALASEPK 153
Cdd:COG5265 451 NIAYGrpdaseeeveaaarAAQihdFieslpDGYDTR-VGE---------------RGLKLSGGEKQRVAIARTLLKNPP 514
|
....*...
gi 1832152097 154 VLILDEPT 161
Cdd:COG5265 515 ILIFDEAT 522
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-160 |
1.19e-16 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 77.58 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSH-ILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRvreGLA 79
Cdd:PRK11650 3 GLKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADR---DIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 80 YVPQGRDIFSTLTVEENiligMAKfkGAKTRKVPEH-----------LYEIFPILDemkqRRGGDLSGGQQQQLAIARAL 148
Cdd:PRK11650 80 MVFQNYALYPHMSVREN----MAY--GLKIRGMPKAeieervaeaarILELEPLLD----RKPRELSGGQRQRVAMGRAI 149
|
170
....*....|..
gi 1832152097 149 ASEPKVLILDEP 160
Cdd:PRK11650 150 VREPAVFLFDEP 161
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
15-159 |
1.44e-16 |
|
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: 75.65 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 15 HILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPeqrvreGLAYVPQgrdifstLTVE 94
Cdd:cd03220 36 WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGL------GGGFNPE-------LTGR 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1832152097 95 ENILIgMAKFKGAKTRKVPEHLYEI--FPILDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDE 159
Cdd:cd03220 103 ENIYL-NGRLLGLSRKEIDEKIDEIieFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDE 168
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
17-221 |
2.71e-16 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 77.00 E-value: 2.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 17 LRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSP---EQRVREGLAYVPQGRDIFSTLTV 93
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDaelREVRRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 94 EENILIGMAKFKGAKTRKVPEHLYEIFPI-LDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDEPTEGIQPSIIKDI 172
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVgLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1832152097 173 GRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREM 221
Cdd:PRK10070 204 QDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
17-221 |
3.89e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 75.59 E-value: 3.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 17 LRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVRE-----GLAYVPQGRDIFSTl 91
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPvrkriGMVFQFPESQLFED- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 92 TVEENILIGMAKFkGAKTRKVPEHLYEIFPIL----DEMKQRRGgDLSGGQQQQLAIARALASEPKVLILDEPTEGIQPS 167
Cdd:PRK13646 102 TVEREIIFGPKNF-KMNLDEVKNYAHRLLMDLgfsrDVMSQSPF-QMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQ 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1832152097 168 IIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREM 221
Cdd:PRK13646 180 SKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
27-224 |
4.99e-16 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 76.98 E-value: 4.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 27 GACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDIsrLSPEQRVREGLAYVPQGRDIFSTLTVEENILIgMAKFKG 106
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI--LTNISDVHQNMGYCPQFDAIDDLLTGREHLYL-YARLRG 2041
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 107 AKTRKVPEHL-YEIFPI-LDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGE 184
Cdd:TIGR01257 2042 VPAEEIEKVAnWSIQSLgLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGR 2121
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1832152097 185 mAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREMPEK 224
Cdd:TIGR01257 2122 -AVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSK 2160
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-221 |
5.79e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 74.87 E-value: 5.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYG-GSHI----LRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDI-----SRLSPE 71
Cdd:PRK13641 3 IKFENVDYIYSpGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 72 QRVREGLAYVPQGRDIFSTlTVEENILIGMAKFkGAKTRKVPEHLYEIFP---ILDEMKQRRGGDLSGGQQQQLAIARAL 148
Cdd:PRK13641 83 LRKKVSLVFQFPEAQLFEN-TVLKDVEFGPKNF-GFSEDEAKEKALKWLKkvgLSEDLISKSPFELSGGQMRRVAIAGVM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1832152097 149 ASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAeELADGYTVMARGQVIAQGAGREM 221
Cdd:PRK13641 161 AYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVA-EYADDVLVLEHGKLIKHASPKEI 232
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
15-160 |
9.41e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 75.93 E-value: 9.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 15 HILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLdgkdisrlspeqrVREGLAYVPQGRDIFSTlTVE 94
Cdd:PLN03130 631 PTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV-------------IRGTVAYVPQVSWIFNA-TVR 696
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1832152097 95 ENILIGmAKFKGAKTRKVPE-----HLYEIFP--ILDEMKQRrGGDLSGGQQQQLAIARALASEPKVLILDEP 160
Cdd:PLN03130 697 DNILFG-SPFDPERYERAIDvtalqHDLDLLPggDLTEIGER-GVNISGGQKQRVSMARAVYSNSDVYIFDDP 767
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
16-225 |
1.11e-15 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 75.53 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 16 ILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSpEQRVREGLAYVPQGRDIFSTlTVEE 95
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYD-HHYLHRQVALVGQEPVLFSG-SVRE 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 96 NILIGMAKFKGAKTRKVP------EHLYEIFPILDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDEPTEGIQpsii 169
Cdd:TIGR00958 574 NIAYGLTDTPDEEIMAAAkaanahDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALD---- 649
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1832152097 170 KDIGRVIRKLADSGEMAIVLVEQFYDFAEElADGYTVMARGQVIAQGAGREMPEKG 225
Cdd:TIGR00958 650 AECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-217 |
1.24e-15 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 75.11 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVN----QFYGGSHILRDVSFQAPVGACSVVLGRNGVGKT-TLLkCLMGILP----IKSGQILLDGKDISRLSPE 71
Cdd:COG4172 6 LLSVEDLSvafgQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTAL-SILRLLPdpaaHPSGSILFDGQDLLGLSER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 72 Q--RVReglayvpqGRDI---F----STL----TVE----ENILI--GMAKfKGAKTR------KV----PEHLYEIFPi 122
Cdd:COG4172 85 ElrRIR--------GNRIamiFqepmTSLnplhTIGkqiaEVLRLhrGLSG-AAARARalelleRVgipdPERRLDAYP- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 123 ldemKQrrggdLSGGQQQQLAIARALASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEqfYDFA--EEL 200
Cdd:COG4172 155 ----HQ-----LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLIT--HDLGvvRRF 223
|
250
....*....|....*..
gi 1832152097 201 ADGYTVMARGQVIAQGA 217
Cdd:COG4172 224 ADRVAVMRQGEIVEQGP 240
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
16-164 |
1.37e-15 |
|
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: 71.42 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 16 ILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLdgkdisrlsPEqrvREGLAYVPQgRDIFSTLTVEE 95
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------PE---GEDLLFLPQ-RPYLPLGTLRE 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1832152097 96 NIligmakfkgaktrkvpehlyeIFPILDEmkqrrggdLSGGQQQQLAIARALASEPKVLILDEPTEGI 164
Cdd:cd03223 83 QL---------------------IYPWDDV--------LSGGEQQRLAFARLLLHKPKFVFLDEATSAL 122
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-220 |
1.56e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 73.51 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGIL---PIKSGQILLDGKDIS---RLSPEQR- 73
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQregRLARDIRk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 74 VREGLAYVPQGRDIFSTLTVEENILIG-----------MAKFKGAKTRKVPEHLYEIFpiLDEMKQRRGGDLSGGQQQQL 142
Cdd:PRK09984 84 SRANTGYIFQQFNLVNRLSVLENVLIGalgstpfwrtcFSWFTREQKQRALQALTRVG--MVHFAHQRVSTLSGGQQQRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1832152097 143 AIARALASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGRE 220
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-160 |
1.86e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 71.90 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISR-LSPEQRvreGLA 79
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKdLCTYQK---QLC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 80 YVPQGRDIFSTLTVEENILIGMAKFKGAktRKVPEhLYEIFPiLDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDE 159
Cdd:PRK13540 78 FVGHRSGINPYLTLRENCLYDIHFSPGA--VGITE-LCRLFS-LEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDE 153
|
.
gi 1832152097 160 P 160
Cdd:PRK13540 154 P 154
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-226 |
2.11e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 75.01 E-value: 2.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 17 LRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLdgkdisrlspeqrVREGLAYVPQGRDIFSTlTVEEN 96
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV-------------IRGSVAYVPQVSWIFNA-TVREN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 97 ILIGmAKFKGAKTRKVP-----EHLYEIFPILDEMK-QRRGGDLSGGQQQQLAIARALASEPKVLILDEPTEGIQPSIIK 170
Cdd:PLN03232 699 ILFG-SDFESERYWRAIdvtalQHDLDLLPGRDLTEiGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAH 777
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1832152097 171 DIGRVIRKLADSGEMAIVLVEQFYDFAeeLADGYTVMARGQVIAQGAGREMPEKGI 226
Cdd:PLN03232 778 QVFDSCMKDELKGKTRVLVTNQLHFLP--LMDRIILVSEGMIKEEGTFAELSKSGS 831
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-188 |
3.47e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 71.37 E-value: 3.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVnQFYGGSHIL-RDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEqrVREGLA 79
Cdd:PRK13538 1 MLEARNL-ACERDERILfSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE--YHQDLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 80 YVPQGRDIFSTLTVEENILIGMAKFKGAKTRKVPEHL-------YEIFPIldemkqrrgGDLSGGQQQQLAIARALASEP 152
Cdd:PRK13538 78 YLGHQPGIKTELTALENLRFYQRLHGPGDDEALWEALaqvglagFEDVPV---------RQLSAGQQRRVALARLWLTRA 148
|
170 180 190
....*....|....*....|....*....|....*.
gi 1832152097 153 KVLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIV 188
Cdd:PRK13538 149 PLWILDEPFTAIDKQGVARLEALLAQHAEQGGMVIL 184
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-178 |
4.52e-15 |
|
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: 72.19 E-value: 4.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFY--GGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKsGQILLDGKDISRLsPEQRVREGLA 79
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSV-PLQKWRKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 80 YVPQGRDIFSTlTVEENiLIGMAKFKGAKTRKVPEH-----LYEIFP-ILDEMKQRRGGDLSGGQQQQLAIARALASEPK 153
Cdd:cd03289 81 VIPQKVFIFSG-TFRKN-LDPYGKWSDEEIWKVAEEvglksVIEQFPgQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAK 158
|
170 180
....*....|....*....|....*
gi 1832152097 154 VLILDEPTEGIQPSIIKDIGRVIRK 178
Cdd:cd03289 159 ILLLDEPSAHLDPITYQVIRKTLKQ 183
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-161 |
7.22e-15 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 73.05 E-value: 7.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLdGKDISrlspeqrvregLAYV 81
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK-----------LAYV 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 82 PQGRD-IFSTLTVEENILIGMAKFKGAKtRKVPEHLY-EIFPILDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDE 159
Cdd:TIGR03719 391 DQSRDaLDPNKTVWEEISGGLDIIKLGK-REIPSRAYvGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDE 469
|
..
gi 1832152097 160 PT 161
Cdd:TIGR03719 470 PT 471
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
11-221 |
7.26e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 71.56 E-value: 7.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 11 YGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVREgLAYVPQGRDIFST 90
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARR-IGLLAQNATTPGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 91 LTVEENILIGMAKFKGAKTRKVPEHLYEIFPIL-----DEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDEPTEGIQ 165
Cdd:PRK10253 96 ITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMqatgiTHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1832152097 166 PSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREM 221
Cdd:PRK10253 176 ISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
16-213 |
8.12e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 71.64 E-value: 8.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 16 ILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQR--VREGLAYVPQgrDIFSTL-- 91
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRkaFRRDIQMVFQ--DSISAVnp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 92 --TVEENI------LIGMAKfkGAKTRKVPEHLyEIFPILDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDEPTEG 163
Cdd:PRK10419 105 rkTVREIIreplrhLLSLDK--AERLARASEML-RAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSN 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1832152097 164 ----IQPSIIkdigRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVI 213
Cdd:PRK10419 182 ldlvLQAGVI----RLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-229 |
8.46e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 72.91 E-value: 8.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFY-----GGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILL----DGKDISRLSPE 71
Cdd:TIGR03269 279 IIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 72 Q--RVREGLAYVPQGRDIFSTLTVEENIL--IGM------AKFKGAKTRKV---PEHLYEifPILDEMKQrrggDLSGGQ 138
Cdd:TIGR03269 359 GrgRAKRYIGILHQEYDLYPHRTVLDNLTeaIGLelpdelARMKAVITLKMvgfDEEKAE--EILDKYPD----ELSEGE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 139 QQQLAIARALASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAg 218
Cdd:TIGR03269 433 RHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGD- 511
|
250
....*....|.
gi 1832152097 219 remPEKGIREL 229
Cdd:TIGR03269 512 ---PEEIVEEL 519
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
17-216 |
9.57e-15 |
|
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: 70.82 E-value: 9.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 17 LRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVREGLAYvPQGRDIFSTLTVEE- 95
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVF-GQKTQLWWDLPVIDs 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 96 -NILIGMAKFKGAKTRKVPEHLYEIFPILDEMKQ--RRggdLSGGQQQQLAIARALASEPKVLILDEPTEGIQPSIIKDI 172
Cdd:cd03267 116 fYLLAAIYDLPPARFKKRLDELSELLDLEELLDTpvRQ---LSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENI 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1832152097 173 GRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQG 216
Cdd:cd03267 193 RNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-224 |
1.00e-14 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 72.53 E-value: 1.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGI--LPIKSGQIL----------------LDGK 63
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpsKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 64 DISR----LSPEQ------------RVREGLAYVPQGR-DIFSTLTVEENILIGM--AKFKGAKTRKVPEHLYEIFPILD 124
Cdd:TIGR03269 81 PCPVcggtLEPEEvdfwnlsdklrrRIRKRIAIMLQRTfALYGDDTVLDNVLEALeeIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 125 EMKQRrGGDLSGGQQQQLAIARALASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGY 204
Cdd:TIGR03269 161 RITHI-ARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKA 239
|
250 260
....*....|....*....|
gi 1832152097 205 TVMARGQVIAQGAGREMPEK 224
Cdd:TIGR03269 240 IWLENGEIKEEGTPDEVVAV 259
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-178 |
1.13e-14 |
|
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: 72.64 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFY--GGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKsGQILLDGKDISRLSPeQRVREGLA 79
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTL-QTWRKAFG 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 80 YVPQGRDIFSTlTVEENiLIGMAKFKGAKTRKVPEH-----LYEIFP-ILDEMKQRRGGDLSGGQQQQLAIARALASEPK 153
Cdd:TIGR01271 1296 VIPQKVFIFSG-TFRKN-LDPYEQWSDEEIWKVAEEvglksVIEQFPdKLDFVLVDGGYVLSNGHKQLMCLARSILSKAK 1373
|
170 180
....*....|....*....|....*
gi 1832152097 154 VLILDEPTEGIQPSIIKDIGRVIRK 178
Cdd:TIGR01271 1374 ILLLDEPSAHLDPVTLQIIRKTLKQ 1398
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1-161 |
1.47e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 72.13 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKS--GQILLDG-----KDISrlSPEQR 73
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGevcrfKDIR--DSEAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 74 ----VREGLAYVPQgrdifstLTVEENILIGMAKFKG-----AKTRKVPEHLYEIFPiLDEMKQRRGGDLSGGQQQQLAI 144
Cdd:NF040905 79 giviIHQELALIPY-------LSIAENIFLGNERAKRgvidwNETNRRARELLAKVG-LDESPDTLVTDIGVGKQQLVEI 150
|
170
....*....|....*..
gi 1832152097 145 ARALASEPKVLILDEPT 161
Cdd:NF040905 151 AKALSKDVKLLILDEPT 167
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-161 |
1.65e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 70.19 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYG-GSH---ILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVR- 75
Cdd:PRK10584 6 IVEVHHLKKSVGqGEHelsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 76 --EGLAYVPQGRDIFSTLTVEENILIGmAKFKGAKTRKVPEHLYEIFPILDEMKQRRG--GDLSGGQQQQLAIARALASE 151
Cdd:PRK10584 86 raKHVGFVFQSFMLIPTLNALENVELP-ALLRGESSRQSRNGAKALLEQLGLGKRLDHlpAQLSGGEQQRVALARAFNGR 164
|
170
....*....|
gi 1832152097 152 PKVLILDEPT 161
Cdd:PRK10584 165 PDVLFADEPT 174
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
5-216 |
1.76e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 71.03 E-value: 1.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 5 KDVNQFYggshILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLdgKDI----------SRLSPEQR- 73
Cdd:PRK13631 34 KQENELV----ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQV--GDIyigdkknnheLITNPYSKk 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 74 ------VREGLAYVPQGRD--IFSTlTVEENILIGMAKFKGAK--TRKVPEHLYEIFPILDEMKQRRGGDLSGGQQQQLA 143
Cdd:PRK13631 108 iknfkeLRRRVSMVFQFPEyqLFKD-TIEKDIMFGPVALGVKKseAKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVA 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1832152097 144 IARALASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFyDFAEELADGYTVMARGQVIAQG 216
Cdd:PRK13631 187 IAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTM-EHVLEVADEVIVMDKGKILKTG 258
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
10-160 |
2.29e-14 |
|
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: 69.67 E-value: 2.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 10 FYGGSHI--LRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPE---QRVREGLAYVPQG 84
Cdd:cd03290 8 FSWGSGLatLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEatrSRNRYSVAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 85 RDIFSTlTVEENILIGmAKFKGAKTRKVPEHL-----YEIFPILDEMK-QRRGGDLSGGQQQQLAIARALASEPKVLILD 158
Cdd:cd03290 88 PWLLNA-TVEENITFG-SPFNKQRYKAVTDACslqpdIDLLPFGDQTEiGERGINLSGGQRQRICVARALYQNTNIVFLD 165
|
..
gi 1832152097 159 EP 160
Cdd:cd03290 166 DP 167
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
32-221 |
3.62e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 71.16 E-value: 3.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 32 VLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQrVREGLAYVPQGRDIFSTlTVEENIlIGMAKFKGAKTRK 111
Cdd:PLN03232 1267 VVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTD-LRRVLSIIPQSPVLFSG-TVRFNI-DPFSEHNDADLWE 1343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 112 VPE--HLYEIF---PI-LDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGEM 185
Cdd:PLN03232 1344 ALEraHIKDVIdrnPFgLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTM 1423
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1832152097 186 AIVlveqfydfAEEL-----ADGYTVMARGQVIAQGAGREM 221
Cdd:PLN03232 1424 LVI--------AHRLntiidCDKILVLSSGQVLEYDSPQEL 1456
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
19-166 |
5.89e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 70.54 E-value: 5.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 19 DVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILL-----DGKDIsrlspEQRVREGlaYVPQGRDIFSTLTV 93
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfgqpvDAGDI-----ATRRRVG--YMSQAFSLYGELTV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 94 EENILIGmakfkgAKTRKVPEHlyEIFPILDEMKQRRG---------GDLSGGQQQQLAIARALASEPKVLILDEPTEGI 164
Cdd:NF033858 357 RQNLELH------ARLFHLPAA--EIAARVAEMLERFDladvadalpDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGV 428
|
..
gi 1832152097 165 QP 166
Cdd:NF033858 429 DP 430
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-216 |
8.08e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 69.73 E-value: 8.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 15 HILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPiKSGQILLDGKDISRLSPEQR--VREGLAYVPQgrDIFSTL- 91
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNLNRRQLlpVRHRIQVVFQ--DPNSSLn 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 92 ---TVEENILIGMAKFK-----GAKTRKVPEHLYEIFpiLD-EMKQRRGGDLSGGQQQQLAIARALASEPKVLILDEPTE 162
Cdd:PRK15134 377 prlNVLQIIEEGLRVHQptlsaAQREQQVIAVMEEVG--LDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1832152097 163 GIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQG 216
Cdd:PRK15134 455 SLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQG 508
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-221 |
9.87e-14 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 69.97 E-value: 9.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 17 LRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKdisrlspeqrvregLAYVPQGRDIfSTLTVEEN 96
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--------------VAYVPQQAWI-QNDSLREN 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 97 ILIGMAkFKGAKTRKVPEHL-----YEIFPILDEMK-QRRGGDLSGGQQQQLAIARALASEPKVLILDEPTEGIQPSIIK 170
Cdd:TIGR00957 719 ILFGKA-LNEKYYQQVLEACallpdLEILPSGDRTEiGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGK 797
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1832152097 171 DI-GRVIRKLADSGEMAIVLVEQFYDFAEELaDGYTVMARGQVIAQGAGREM 221
Cdd:TIGR00957 798 HIfEHVIGPEGVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQEL 848
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
17-216 |
9.95e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 68.84 E-value: 9.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 17 LRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQR--VREGLAYVPQgrDIFSTL--- 91
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQklLRQKIQIVFQ--NPYGSLnpr 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 92 -----TVEENILIGMAKFKGAKTRKV----------PEHlYEIFPildEMkqrrggdLSGGQQQQLAIARALASEPKVLI 156
Cdd:PRK11308 109 kkvgqILEEPLLINTSLSAAERREKAlammakvglrPEH-YDRYP---HM-------FSGGQRQRIAIARALMLDPDVVV 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 157 LDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQG 216
Cdd:PRK11308 178 ADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKG 237
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
15-223 |
1.35e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.50 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 15 HILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPE--QRVREGLAYVPQgrDIFSTL- 91
Cdd:PRK10261 338 HAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGklQALRRDIQFIFQ--DPYASLd 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 92 ---TVEENILIGM---AKFKGAKTRKVPEHLYEIFPILDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDEPTEGIQ 165
Cdd:PRK10261 416 prqTVGDSIMEPLrvhGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1832152097 166 PSIikdIGRVIRKLAD-SGEMAIVLVEQFYDFA--EELADGYTVMARGQVIAQGAGREMPE 223
Cdd:PRK10261 496 VSI---RGQIINLLLDlQRDFGIAYLFISHDMAvvERISHRVAVMYLGQIVEIGPRRAVFE 553
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-164 |
1.64e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 67.45 E-value: 1.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKdisrlspeqrVREGlaY 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK----------LRIG--Y 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 81 VPQGRDIFST--LTVEENILIGMAKFKG----AKTRKVPEHLyeifpiLDEMKQRrggdLSGGQQQQLAIARALASEPKV 154
Cdd:PRK09544 72 VPQKLYLDTTlpLTVNRFLRLRPGTKKEdilpALKRVQAGHL------IDAPMQK----LSGGETQRVLLARALLNRPQL 141
|
170
....*....|
gi 1832152097 155 LILDEPTEGI 164
Cdd:PRK09544 142 LVLDEPTQGV 151
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-160 |
2.55e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 67.01 E-value: 2.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQiLLDGKdisrlSPEQRVREGLAYV 81
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-LLAGT-----APLAEAREDTRLM 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1832152097 82 PQGRDIFSTLTVEENILIGMakfKGAKTRKVPEHLYEIFpiLDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDEP 160
Cdd:PRK11247 87 FQDARLLPWKKVIDNVGLGL---KGQWRDAALQALAAVG--LADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-202 |
2.75e-13 |
|
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: 67.05 E-value: 2.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 31 VVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISrlspeqrvreglaYVPQGRDIFSTLTVEEniligmakFKGAKTR 110
Cdd:cd03237 29 GILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-------------YKPQYIKADYEGTVRD--------LLSSITK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 111 KVPEHLYEIFPILDEMK-----QRRGGDLSGGQQQQLAIARALASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGEM 185
Cdd:cd03237 88 DFYTHPYFKTEIAKPLQieqilDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEK 167
|
170
....*....|....*..
gi 1832152097 186 AIVLVEQFYDFAEELAD 202
Cdd:cd03237 168 TAFVVEHDIIMIDYLAD 184
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
16-188 |
3.90e-13 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 65.73 E-value: 3.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 16 ILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMG--ILPIKSGQILLDGKDIsrlspEQRVREGLAYVPQgRDIFS-TLT 92
Cdd:cd03232 22 LLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPL-----DKNFQRSTGYVEQ-QDVHSpNLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 93 VEENILIGmAKFKGaktrkvpehlyeifpildemkqrrggdLSGGQQQQLAIARALASEPKVLILDEPTEGIQPSIIKDI 172
Cdd:cd03232 96 VREALRFS-ALLRG---------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNI 147
|
170
....*....|....*.
gi 1832152097 173 GRVIRKLADSGeMAIV 188
Cdd:cd03232 148 VRFLKKLADSG-QAIL 162
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-161 |
3.91e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 67.84 E-value: 3.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLdGkdisrlspeQRVRegLAYV 81
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-G---------ETVK--LAYV 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 82 PQGRD-IFSTLTVEENI-----LIGMAK-------------FKGAktrkvpehlyeifpilDEmkQRRGGDLSGGQQQQL 142
Cdd:PRK11819 393 DQSRDaLDPNKTVWEEIsggldIIKVGNreipsrayvgrfnFKGG----------------DQ--QKKVGVLSGGERNRL 454
|
170
....*....|....*....
gi 1832152097 143 AIARALASEPKVLILDEPT 161
Cdd:PRK11819 455 HLAKTLKQGGNVLLLDEPT 473
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
15-159 |
4.38e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 66.26 E-value: 4.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 15 HILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPeqrvreGLAYVPQgrdifstLTVE 94
Cdd:COG1134 40 WALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSALLEL------GAGFHPE-------LTGR 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1832152097 95 ENI-LIGMakFKGAKTRKVPEHLYEI--------FpiLDE-MKQrrggdLSGGQQQQLAIARALASEPKVLILDE 159
Cdd:COG1134 107 ENIyLNGR--LLGLSRKEIDEKFDEIvefaelgdF--IDQpVKT-----YSSGMRARLAFAVATAVDPDILLVDE 172
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
16-188 |
7.43e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 65.26 E-value: 7.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 16 ILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRlSPEQRVREGLAYVPQGRDIFSTLtveE 95
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR-GDRSRFMAYLGHLPGLKADLSTL---E 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 96 NiLIGMAKFKGAKTRKVPEHLYEIFPILDEmKQRRGGDLSGGQQQQLAIARALASEPKVLILDEPTEGIQPSIIKDIGRV 175
Cdd:PRK13543 102 N-LHFLCGLHGRRAKQMPGSALAIVGLAGY-EDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRM 179
|
170
....*....|...
gi 1832152097 176 IRKLADSGEMAIV 188
Cdd:PRK13543 180 ISAHLRGGGAALV 192
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1-188 |
7.79e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 67.12 E-value: 7.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQF---YGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMG------IlpikSGQILLDGKDISRLSPE 71
Cdd:NF040905 257 VFEVKNWTVYhplHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGrsygrnI----SGTVFKDGKEVDVSTVS 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 72 QRVREGLAYVPQGRDIFStLTVEENIL--IGMAKFKGAKTRKVpehlyeifpiLDEMKQRR------------------- 130
Cdd:NF040905 333 DAIDAGLAYVTEDRKGYG-LNLIDDIKrnITLANLGKVSRRGV----------IDENEEIKvaeeyrkkmniktpsvfqk 401
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1832152097 131 GGDLSGGQQQQLAIARALASEPKVLILDEPTEGIqpsiikDIG------RVIRKLADSGEMAIV 188
Cdd:NF040905 402 VGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGI------DVGakyeiyTIINELAAEGKGVIV 459
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
105-224 |
9.34e-13 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 66.30 E-value: 9.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 105 KGAKTRKvpEHLYEIFPiLDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGE 184
Cdd:NF000106 119 KDARARA--DELLERFS-LTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGA 195
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1832152097 185 mAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREMPEK 224
Cdd:NF000106 196 -TVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTK 234
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-216 |
1.19e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 65.05 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMG--ILPIKSGQILLDGKDISRLSPEQRVREG- 77
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERAHLGi 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 78 -LAY-----VPqGRDIFSTLTVEENiliGMAKFKGaKTRKVPEHLYEIF-PILD--EMKQR-------RGgdLSGGQQQQ 141
Cdd:CHL00131 87 fLAFqypieIP-GVSNADFLRLAYN---SKRKFQG-LPELDPLEFLEIInEKLKlvGMDPSflsrnvnEG--FSGGEKKR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1832152097 142 LAIARALASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSgEMAIVLVEQFYDFAEELADGYT-VMARGQVIAQG 216
Cdd:CHL00131 160 NEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTS-ENSIILITHYQRLLDYIKPDYVhVMQNGKIIKTG 234
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-221 |
1.33e-12 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 65.88 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 19 DVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQR--VREGLAYVPQgrDIFSTL----T 92
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWraVRSDIQMIFQ--DPLASLnprmT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 93 VEENILIGMAKFKGAKTR-KVPEHLYEIFP---ILDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDEPTEGIQPSI 168
Cdd:PRK15079 117 IGEIIAEPLRTYHPKLSRqEVKDRVKAMMLkvgLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSI 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1832152097 169 IKDIGRVIRKLadSGEMAIVLVEQFYDFA--EELADGYTVMARGQVIAQGAGREM 221
Cdd:PRK15079 197 QAQVVNLLQQL--QREMGLSLIFIAHDLAvvKHISDRVLVMYLGHAVELGTYDEV 249
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
17-216 |
1.59e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 65.49 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 17 LRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVREGLAYVPQGRDIFSTL----- 91
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEKVLEKLVIQKTRFKKIkkike 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 92 -------------------TVEENILIGMAKF--KGAKTRKVPEHLYEIFPILDEMKQRRGGDLSGGQQQQLAIARALAS 150
Cdd:PRK13651 103 irrrvgvvfqfaeyqlfeqTIEKDIIFGPVSMgvSKEEAKKRAAKYIELVGLDESYLQRSPFELSGGQKRRVALAGILAM 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1832152097 151 EPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGEmAIVLVEQFYDFAEELADGYTVMARGQVIAQG 216
Cdd:PRK13651 183 EPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVLEWTKRTIFFKDGKIIKDG 247
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-191 |
1.63e-12 |
|
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: 65.96 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 32 VLGRNGVGKTTLLKCLMGILPIKSGQILLDGKdisrlspeqrvregLAYVPQGRDIFSTLTVEENIligmakfKGAKTRK 111
Cdd:COG1245 371 IVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK--------------ISYKPQYISPDYDGTVEEFL-------RSANTDD 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 112 VPEHLYE---IFPI-LDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDEPT------EGIQpsiikdIGRVIRKLAD 181
Cdd:COG1245 430 FGSSYYKteiIKPLgLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSahldveQRLA------VAKAIRRFAE 503
|
170
....*....|
gi 1832152097 182 SGEMAIVLVE 191
Cdd:COG1245 504 NRGKTAMVVD 513
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-216 |
1.95e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 66.29 E-value: 1.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 16 ILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLM----GILPIKSGQILLDGkdisrLSPEQ---RVREGLAYVPQGRDIF 88
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDG-----ITPEEikkHYRGDVVYNAETDVHF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 89 STLTVEENiLIGMAKFKGAKTR-----------KVPEHLYEIFPiLDEMKQRRGGD-----LSGGQQQQLAIARALASEP 152
Cdd:TIGR00956 151 PHLTVGET-LDFAARCKTPQNRpdgvsreeyakHIADVYMATYG-LSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGA 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1832152097 153 KVLILDEPTEGIQPSIIKDIGRVIRKLADSGEM-AIVLVEQFYDFAEELADGYTVMARGQVIAQG 216
Cdd:TIGR00956 229 KIQCWDNATRGLDSATALEFIRALKTSANILDTtPLVAIYQCSQDAYELFDKVIVLYEGYQIYFG 293
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-188 |
2.02e-12 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 65.90 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFY----GGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRV-- 74
Cdd:PRK10535 4 LLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAql 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 75 -REGLAYVPQGRDIFSTLTVEENILIGmAKFKGAKTRKVPEHLYEIFPIL--DEMKQRRGGDLSGGQQQQLAIARALASE 151
Cdd:PRK10535 84 rREHFGFIFQRYHLLSHLTAAQNVEVP-AVYAGLERKQRLLRAQELLQRLglEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 1832152097 152 PKVLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIV 188
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVII 199
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
20-220 |
2.25e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 64.18 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 20 VSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPiKSGQILLDGKDISRLS-PEQ-RVReglAYVPQgrdifstltvEENI 97
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSaAELaRHR---AYLSQ----------QQTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 98 LIGMAKFK--------GAKTRKVPEHLYEI--FPILDEMKQRRGGDLSGGQQQQ-------LAIARALASEPKVLILDEP 160
Cdd:PRK03695 81 PFAMPVFQyltlhqpdKTRTEAVASALNEVaeALGLDDKLGRSVNQLSGGEWQRvrlaavvLQVWPDINPAGQLLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1832152097 161 TEGIqpsiikDIG------RVIRKLADSGemaIVLVEQFYDFAEEL--ADGYTVMARGQVIAQGAGRE 220
Cdd:PRK03695 161 MNSL------DVAqqaaldRLLSELCQQG---IAVVMSSHDLNHTLrhADRVWLLKQGKLLASGRRDE 219
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
15-202 |
4.00e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.44 E-value: 4.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 15 HILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISrLSPEQRVREGLAyvpqgrDIFSTLTVE 94
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQ-FGREASLIDAIG------RKGDFKDAV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 95 EniLIGMAKFKGAKT--RKVPEhlyeifpildemkqrrggdLSGGQQQQLAIARALASEPKVLILDEPTEGIQPSIIKDI 172
Cdd:COG2401 117 E--LLNAVGLSDAVLwlRRFKE-------------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRV 175
|
170 180 190
....*....|....*....|....*....|
gi 1832152097 173 GRVIRKLADSGEMAIVLVEQFYDFAEELAD 202
Cdd:COG2401 176 ARNLQKLARRAGITLVVATHHYDVIDDLQP 205
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-190 |
5.68e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 64.67 E-value: 5.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFY---GGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIK------------------------ 54
Cdd:PTZ00265 1166 IEIMDVNFRYisrPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKndhhivfknehtndmtneqdyqgd 1245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 55 ------------------------------SGQILLDGKDISRLSPEQrVREGLAYVPQGRDIFStLTVEENILIGMAKF 104
Cdd:PTZ00265 1246 eeqnvgmknvnefsltkeggsgedstvfknSGKILLDGVDICDYNLKD-LRNLFSIVSQEPMLFN-MSIYENIKFGKEDA 1323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 105 KGAKTRKVPEhlyeiFPILDEMKQR-----------RGGDLSGGQQQQLAIARALASEPKVLILDEPTEGIQPSIIKDIG 173
Cdd:PTZ00265 1324 TREDVKRACK-----FAAIDEFIESlpnkydtnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIE 1398
|
250
....*....|....*..
gi 1832152097 174 RVIRKLADSGEMAIVLV 190
Cdd:PTZ00265 1399 KTIVDIKDKADKTIITI 1415
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
17-217 |
1.24e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 62.50 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 17 LRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDIS--------------------RLSPEQRVRE 76
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgdysyrsqrirmifqdpstSLNPRQRISQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 77 GLAYVPQGRDIFSTLTVEENILigmakfkgAKTRKV---PEHLYeIFPILdemkqrrggdLSGGQQQQLAIARALASEPK 153
Cdd:PRK15112 109 ILDFPLRLNTDLEPEQREKQII--------ETLRQVgllPDHAS-YYPHM----------LAPGQKQRLGLARALILRPK 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1832152097 154 VLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQGA 217
Cdd:PRK15112 170 VIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGS 233
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-191 |
1.94e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.90 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 32 VLGRNGVGKTTLLKCLMGILPIKSGQILLDGKdisrlspeqrvregLAYVPQGRDIFSTLTVEENIligmakfkgaktRK 111
Cdd:PRK13409 370 IVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK--------------ISYKPQYIKPDYDGTVEDLL------------RS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 112 VPEHL----YE---IFPI-LDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDEPT------EGIQpsiikdIGRVIR 177
Cdd:PRK13409 424 ITDDLgssyYKseiIKPLqLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSahldveQRLA------VAKAIR 497
|
170
....*....|....
gi 1832152097 178 KLADSGEMAIVLVE 191
Cdd:PRK13409 498 RIAEEREATALVVD 511
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-193 |
1.99e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.20 E-value: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 16 ILRDVSFQAPVGACSVVLGRNGVGKTTLLKCL-----MGIlpIKSGQILLDGkdISRLSPEQRVregLAYVPQgRDIFS- 89
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLaervtTGV--ITGGDRLVNG--RPLDSSFQRS---IGYVQQ-QDLHLp 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 90 TLTVEENiLIGMAKFKGAKtrKVP-----EHLYEIFPILdEMKQRR-------GGDLSGGQQQQLAIARALASEPKVLI- 156
Cdd:TIGR00956 850 TSTVRES-LRFSAYLRQPK--SVSksekmEYVEEVIKLL-EMESYAdavvgvpGEGLNVEQRKRLTIGVELVAKPKLLLf 925
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1832152097 157 LDEPTEGIQPSIIKDIGRVIRKLADSGEM--------AIVLVEQF 193
Cdd:TIGR00956 926 LDEPTSGLDSQTAWSICKLMRKLADHGQAilctihqpSAILFEEF 970
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
27-221 |
2.04e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 62.72 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 27 GACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQ---RV-----REGLAYVPQGRDIFStLTVEENIL 98
Cdd:PRK10938 29 GDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQlqkLVsdewqRNNTDMLSPGEDDTG-RTTAEIIQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 99 igmakfKGAKTRKVPEHLYEIFPIlDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDEPTEGIQPSIIKDIGRVIRK 178
Cdd:PRK10938 108 ------DEVKDPARCEQLAQQFGI-TALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLAS 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1832152097 179 LADSGeMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREM 221
Cdd:PRK10938 181 LHQSG-ITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEI 222
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
13-166 |
2.29e-11 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 62.84 E-value: 2.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 13 GSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDgkdisrlsPEQRvregLAYVPQgRDIFSTLT 92
Cdd:TIGR00954 464 GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKP--------AKGK----LFYVPQ-RPYMTLGT 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 93 VEENILIGMAKFKgAKTRKVPEHlyEIFPILDEMK-----QRRGG---------DLSGGQQQQLAIARALASEPKVLILD 158
Cdd:TIGR00954 531 LRDQIIYPDSSED-MKRRGLSDK--DLEQILDNVQlthilEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILD 607
|
....*...
gi 1832152097 159 EPTEGIQP 166
Cdd:TIGR00954 608 ECTSAVSV 615
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
34-216 |
2.67e-11 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 62.23 E-value: 2.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 34 GRNGVGKTTLLKCLMGILP----IKSGQILLDGKDISRLSPEQRVR-----------EGLAYVPQGRDIFSTLtvEENI- 97
Cdd:COG4170 40 GESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDLLKLSPRERRKiigreiamifqEPSSCLDPSAKIGDQL--IEAIp 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 98 ---LIG--MAKFKGAKTR----------KVPEHLYEIFPIldemkqrrggDLSGGQQQQLAIARALASEPKVLILDEPTE 162
Cdd:COG4170 118 swtFKGkwWQRFKWRKKRaiellhrvgiKDHKDIMNSYPH----------ELTEGECQKVMIAMAIANQPRLLIADEPTN 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1832152097 163 GIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQG 216
Cdd:COG4170 188 AMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESG 241
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-160 |
2.69e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 62.87 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 16 ILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDgkdisrlspeqrvrEGLAYVPQGRDIFSTlTVEE 95
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE--------------RSIAYVPQQAWIMNA-TVRG 739
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 96 NILI----GMAKFKGA-KTRKVPEHLYEIFPILDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDEP 160
Cdd:PTZ00243 740 NILFfdeeDAARLADAvRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDP 809
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-161 |
2.95e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 62.22 E-value: 2.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQIlldgkdisRLSPEQRVreglAYV 81
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV--------KWSENANI----GYY 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 82 PQgrDIFSTLTVEENILIGMAKFKGAKTrkvpehlyeifpilDEMKQR----R---GGD--------LSGGQQQQLAIAR 146
Cdd:PRK15064 388 AQ--DHAYDFENDLTLFDWMSQWRQEGD--------------DEQAVRgtlgRllfSQDdikksvkvLSGGEKGRMLFGK 451
|
170
....*....|....*
gi 1832152097 147 ALASEPKVLILDEPT 161
Cdd:PRK15064 452 LMMQKPNVLVMDEPT 466
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
6-216 |
4.78e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 61.65 E-value: 4.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 6 DVNQF-YGGSH--ILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQrVREGLAYVP 82
Cdd:PRK10789 317 NIRQFtYPQTDhpALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDS-WRSRLAVVS 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 83 QGRDIFSTlTVEENILIGmakfKGAKTRKVPEHLYEIFPILDEMKQ----------RRGGDLSGGQQQQLAIARALASEP 152
Cdd:PRK10789 396 QTPFLFSD-TVANNIALG----RPDATQQEIEHVARLASVHDDILRlpqgydtevgERGVMLSGGQKQRISIARALLLNA 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1832152097 153 KVLILDEPTEGIQpsiikdiGR----VIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQG 216
Cdd:PRK10789 471 EILILDDALSAVD-------GRtehqILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRG 531
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
32-188 |
4.92e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 62.06 E-value: 4.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 32 VLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQrVREGLAYVPQGRDIFSTlTVEENiLIGMAKFKGAKTRK 111
Cdd:PLN03130 1270 IVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMD-LRKVLGIIPQAPVLFSG-TVRFN-LDPFNEHNDADLWE 1346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 112 VPE--HLYEIF---PI-LDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGEM 185
Cdd:PLN03130 1347 SLEraHLKDVIrrnSLgLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTM 1426
|
...
gi 1832152097 186 AIV 188
Cdd:PLN03130 1427 LII 1429
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
20-221 |
8.74e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 60.53 E-value: 8.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 20 VSFQAPVGACSVVLGRNGVGKTTLLKCLMGILP----IKSGQILLDGKDISRLSPEQR---VREGLAYVPQgrDIFSTL- 91
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQRISEKERrnlVGAEVAMIFQ--DPMTSLn 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 92 ---TVEENILIGMAKFKGA--KTRKV-------------PEHLYEIFPildemkqrrgGDLSGGQQQQLAIARALASEPK 153
Cdd:PRK11022 104 pcyTVGFQIMEAIKVHQGGnkKTRRQraidllnqvgipdPASRLDVYP----------HQLSGGMSQRVMIAMAIACRPK 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1832152097 154 VLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREM 221
Cdd:PRK11022 174 LLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
12-161 |
1.05e-10 |
|
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: 60.72 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 12 GGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGIlpiksgqilldGKDIS---RLSPEQRVreglAYVPQGRDIF 88
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-----------DKDFNgeaRPQPGIKV----GYLPQEPQLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 89 STLTVEENILIGMAKFKGAKTR------KVPEHLYEIFPILDEMK------QRRGG------------------------ 132
Cdd:TIGR03719 81 PTKTVRENVEEGVAEIKDALDRfneisaKYAEPDADFDKLAAEQAelqeiiDAADAwdldsqleiamdalrcppwdadvt 160
|
170 180
....*....|....*....|....*....
gi 1832152097 133 DLSGGQQQQLAIARALASEPKVLILDEPT 161
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPT 189
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
29-161 |
1.98e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.96 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 29 CSVvlGRNGVGKTTLLKCLMGILPIKSGQILLDgKD--ISRLspEQR------------VREGLAYVPQGRDIFSTLT-- 92
Cdd:PRK11147 33 CLV--GRNGAGKSTLMKILNGEVLLDDGRIIYE-QDliVARL--QQDpprnvegtvydfVAEGIEEQAEYLKRYHDIShl 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 93 VE----ENILIGMAKFKGaktrkVPEHL---------YEIFPILDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDE 159
Cdd:PRK11147 108 VEtdpsEKNLNELAKLQE-----QLDHHnlwqlenriNEVLAQLGLDPDAALSSLSGGWLRKAALGRALVSNPDVLLLDE 182
|
..
gi 1832152097 160 PT 161
Cdd:PRK11147 183 PT 184
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-164 |
2.87e-10 |
|
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: 59.57 E-value: 2.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 16 ILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQrVREGLAYVPQGRDIFS-TLTV- 93
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHD-LRFKITIIPQDPVLFSgSLRMn 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 94 --------EENI-----LIGMAKFKGAKTRKvpehlyeifpiLDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDEP 160
Cdd:TIGR00957 1380 ldpfsqysDEEVwwaleLAHLKTFVSALPDK-----------LDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEA 1448
|
....
gi 1832152097 161 TEGI 164
Cdd:TIGR00957 1449 TAAV 1452
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
2-221 |
3.92e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 59.41 E-value: 3.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQFY--GGSHILRDVSFQ-AP---VGacsvVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQrVR 75
Cdd:PTZ00243 1309 LVFEGVQMRYreGLPLVLRGVSFRiAPrekVG----IVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRE-LR 1383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 76 EGLAYVPQGRDIFSTlTVEENI----------------LIGMAKFKGAKTRKVpehlyeifpilDEMKQRRGGDLSGGQQ 139
Cdd:PTZ00243 1384 RQFSMIPQDPVLFDG-TVRQNVdpfleassaevwaaleLVGLRERVASESEGI-----------DSRVLEGGSNYSVGQR 1451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 140 QQLAIARALASEPKVLIL-DEPTEGIQPSIIKDIGRVIRKlADSGEMAIVLVEQFYDFAEelADGYTVMARGQVIAQGAG 218
Cdd:PTZ00243 1452 QLMCMARALLKKGSGFILmDEATANIDPALDRQIQATVMS-AFSAYTVITIAHRLHTVAQ--YDKIIVMDHGAVAEMGSP 1528
|
...
gi 1832152097 219 REM 221
Cdd:PTZ00243 1529 REL 1531
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
16-220 |
7.21e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 58.35 E-value: 7.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 16 ILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKS--GQILLDGKdisrlSPEQRVREGLAYVPQGRDIFSTLTV 93
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNR-----KPTKQILKRTGFVTQDDILYPHLTV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 94 EEN-ILIGMAKFKGAKTRKVPEHLYEifPILDEMKQRRGGD----------LSGGQQQQLAIARALASEPKVLILDEPTE 162
Cdd:PLN03211 158 RETlVFCSLLRLPKSLTKQEKILVAE--SVISELGLTKCENtiignsfirgISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1832152097 163 GIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGRE 220
Cdd:PLN03211 236 GLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSD 293
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-161 |
1.04e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 57.65 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 3 EVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGK------DISR--LSPEQRV 74
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKlevayfDQHRaeLDPEKTV 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 75 REGLAYVPQgrdifstlTVEENiligmakfkgAKTRKVPEHLYE-IFPILDEMKQRRGgdLSGGQQQQLAIARALASEPK 153
Cdd:PRK11147 401 MDNLAEGKQ--------EVMVN----------GRPRHVLGYLQDfLFHPKRAMTPVKA--LSGGERNRLLLARLFLKPSN 460
|
....*...
gi 1832152097 154 VLILDEPT 161
Cdd:PRK11147 461 LLILDEPT 468
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
20-221 |
1.49e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 57.12 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 20 VSFQAPVGACSVVLGRNGVGKTTLLKCLMGI----LPIKSGQILLDGKDISRLSPEQR---VREGLAYV---PQgrdifS 89
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnWRVTADRMRFDDIDLLRLSPRERrklVGHNVSMIfqePQ-----S 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 90 TLTVEENI------LIGMAKFKGA-------KTRKVPEHLYEIfPILDEMKQRRG--GDLSGGQQQQLAIARALASEPKV 154
Cdd:PRK15093 101 CLDPSERVgrqlmqNIPGWTYKGRwwqrfgwRKRRAIELLHRV-GIKDHKDAMRSfpYELTEGECQKVMIAIALANQPRL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1832152097 155 LILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREM 221
Cdd:PRK15093 180 LIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKEL 246
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-217 |
3.00e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.40 E-value: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 17 LRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPE------------QRVREG-LAYVPQ 83
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQvielseqsaaqmRHVRGAdMAMIFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 84 G--RDIFSTLTVEENILIGMAKFKGAKTRkvpEHLYEIFPILDEMK--------QRRGGDLSGGQQQQLAIARALASEPK 153
Cdd:PRK10261 112 EpmTSLNPVFTVGEQIAESIRLHQGASRE---EAMVEAKRMLDQVRipeaqtilSRYPHQLSGGMRQRVMIAMALSCRPA 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1832152097 154 VLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQGA 217
Cdd:PRK10261 189 VLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGS 252
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-161 |
4.86e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.90 E-value: 4.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 5 KDVNQFYGGS-HILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGIlpiksgqillDgKDIS---RLSPEQRVreglAY 80
Cdd:PRK11819 10 NRVSKVVPPKkQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV----------D-KEFEgeaRPAPGIKV----GY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 81 VPQGRDIFSTLTVEENILIGMAKFKGAKTR--KVPEHLYEIFPILDEMKQRRG--------------------------- 131
Cdd:PRK11819 75 LPQEPQLDPEKTVRENVEEGVAEVKAALDRfnEIYAAYAEPDADFDALAAEQGelqeiidaadawdldsqleiamdalrc 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 1832152097 132 --GD-----LSGGQQQQLAIARALASEPKVLILDEPT 161
Cdd:PRK11819 155 ppWDakvtkLSGGERRRVALCRLLLEKPDMLLLDEPT 191
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
9-159 |
5.99e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 54.11 E-value: 5.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 9 QFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSpeqrvREGLAYVPQGRDIF 88
Cdd:PRK13541 8 QFNIEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA-----KPYCTYIGHNLGLK 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1832152097 89 STLTVEENILIGMAKFKGAKTRKVPEHLYEIFPILDEmkqrRGGDLSGGQQQQLAIARALASEPKVLILDE 159
Cdd:PRK13541 83 LEMTVFENLKFWSEIYNSAETLYAAIHYFKLHDLLDE----KCYSLSSGMQKIVAIARLIACQSDLWLLDE 149
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-221 |
6.16e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 55.48 E-value: 6.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 19 DVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILP-----IKSGQILLDGKDISRlSPEQRVReGLayvpQGRD---IFST 90
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSVTALSILRLLPsppvvYPSGDIRFHGESLLH-ASEQTLR-GV----RGNKiamIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 91 LTVEENILIGMAKfkgaktrkvpeHLYEIFPILDEMKQ--------------------RRGGD----LSGGQQQQLAIAR 146
Cdd:PRK15134 101 PMVSLNPLHTLEK-----------QLYEVLSLHRGMRReaargeilncldrvgirqaaKRLTDyphqLSGGERQRVMIAM 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1832152097 147 ALASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMARGQVIAQGAGREM 221
Cdd:PRK15134 170 ALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATL 244
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
16-216 |
6.34e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 55.62 E-value: 6.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 16 ILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGIlpiKSGQiLLDGkDIsRLSPEQRVREGLA----YVPQGrDIFS-T 90
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGR---KTGG-YIEG-DI-RISGFPKKQETFArisgYCEQN-DIHSpQ 967
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 91 LTVEENIL----IGMAK--FKGAKTRKVPE--HLYEifpiLDEMKQRRGG-----DLSGGQQQQLAIARALASEPKVLIL 157
Cdd:PLN03140 968 VTVRESLIysafLRLPKevSKEEKMMFVDEvmELVE----LDNLKDAIVGlpgvtGLSTEQRKRLTIAVELVANPSIIFM 1043
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1832152097 158 DEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQ-----FYDFAEELadgytVMAR-GQVIAQG 216
Cdd:PLN03140 1044 DEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQpsidiFEAFDELL-----LMKRgGQVIYSG 1103
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
13-160 |
8.32e-09 |
|
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: 55.30 E-value: 8.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 13 GSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKdisrlspeqrvregLAYVPQGRDIFSTlT 92
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR--------------ISFSPQTSWIMPG-T 502
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1832152097 93 VEENILIGMA--KFKGAKTRKVP--EHLYEIFPILDEMKQRRGG-DLSGGQQQQLAIARALASEPKVLILDEP 160
Cdd:TIGR01271 503 IKDNIIFGLSydEYRYTSVIKACqlEEDIALFPEKDKTVLGEGGiTLSGGQRARISLARAVYKDADLYLLDSP 575
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
13-160 |
8.78e-09 |
|
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: 54.48 E-value: 8.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 13 GSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKdisrlspeqrvregLAYVPQGRDIFSTlT 92
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--------------ISFSSQFSWIMPG-T 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1832152097 93 VEENILIGMA----KFKGA-KTRKVPEHLYEiFPILDEMKQRRGG-DLSGGQQQQLAIARALASEPKVLILDEP 160
Cdd:cd03291 114 IKENIIFGVSydeyRYKSVvKACQLEEDITK-FPEKDNTVLGEGGiTLSGGQRARISLARAVYKDADLYLLDSP 186
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
2-191 |
1.08e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 53.10 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 2 LEVKDVNQfyggsHILRDVSFQAPVGACSVVLGRNGVGKTTLL---------KCLMGILPIKSGQILLDGKDISRLspeq 72
Cdd:cd03238 1 LTVSGANV-----HNLQNLDVSIPLNVLVVVTGVSGSGKSTLVneglyasgkARLISFLPKFSRNKLIFIDQLQFL---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 73 rVREGLAYVPQGRdIFSTLtveeniligmakfkgaktrkvpehlyeifpildemkqrrggdlSGGQQQQLAIARALASEP 152
Cdd:cd03238 72 -IDVGLGYLTLGQ-KLSTL-------------------------------------------SGGELQRVKLASELFSEP 106
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1832152097 153 K--VLILDEPTEGIQPSIIKDIGRVIRKLADSGEmAIVLVE 191
Cdd:cd03238 107 PgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGN-TVILIE 146
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
12-161 |
1.45e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.48 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 12 GGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKcLMGILPI----KSGQIL-----LDGKDISRL-----SPEQRVR-- 75
Cdd:PLN03073 188 GGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLR-YMAMHAIdgipKNCQILhveqeVVGDDTTALqcvlnTDIERTQll 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 76 -EGLAYVPQGRDI-FSTLTVEEniliGMAKFKGAKTRKVPEHLYEIFPILD----------------------EMKQRRG 131
Cdd:PLN03073 267 eEEAQLVAQQRELeFETETGKG----KGANKDGVDKDAVSQRLEEIYKRLElidaytaearaasilaglsftpEMQVKAT 342
|
170 180 190
....*....|....*....|....*....|
gi 1832152097 132 GDLSGGQQQQLAIARALASEPKVLILDEPT 161
Cdd:PLN03073 343 KTFSGGWRMRIALARALFIEPDLLLLDEPT 372
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-163 |
1.60e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 53.94 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 17 LRDVSFQapVGACSVV--LGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPE----------QR--------VRE 76
Cdd:COG4586 38 VDDISFT--IEPGEIVgfIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEfarrigvvfgQRsqlwwdlpAID 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 77 GLAYVpqgRDIFStltveenilIGMAKFKgaKTRkvpEHLYEIFPILDEMKQ--RRggdLSGGQQQQLAIARALASEPKV 154
Cdd:COG4586 116 SFRLL---KAIYR---------IPDAEYK--KRL---DELVELLDLGELLDTpvRQ---LSLGQRMRCELAAALLHRPKI 175
|
....*....
gi 1832152097 155 LILDEPTEG 163
Cdd:COG4586 176 LFLDEPTIG 184
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
26-164 |
1.80e-08 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 53.37 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 26 VGACsvvlGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLsPEQRVREGLAYVPQGRDIFStltveeniliGMAKFK 105
Cdd:cd03288 50 VGIC----GRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKL-PLHTLRSRLSIILQDPILFS----------GSIRFN 114
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1832152097 106 GAKTRKVPE-HLYEIFPI-------------LDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDEPTEGI 164
Cdd:cd03288 115 LDPECKCTDdRLWEALEIaqlknmvkslpggLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASI 187
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-191 |
4.78e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.89 E-value: 4.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 32 VLGRNGVGKTTLLKclmgILpikSGQILLD-GKDISRLSPE---------------QRVREG---LAYVPQGRDIFSTL- 91
Cdd:PRK13409 104 ILGPNGIGKTTAVK----IL---SGELIPNlGDYEEEPSWDevlkrfrgtelqnyfKKLYNGeikVVHKPQYVDLIPKVf 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 92 --TVEEniLIGMAKFKGaKTRKVPEHLyEIFPILDemkqRRGGDLSGGQQQQLAIARALASEPKVLILDEPTEGIqpsii 169
Cdd:PRK13409 177 kgKVRE--LLKKVDERG-KLDEVVERL-GLENILD----RDISELSGGELQRVAIAAALLRDADFYFFDEPTSYL----- 243
|
170 180
....*....|....*....|....*...
gi 1832152097 170 kDIG------RVIRKLADsgEMAIVLVE 191
Cdd:PRK13409 244 -DIRqrlnvaRLIRELAE--GKYVLVVE 268
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-216 |
2.08e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 50.17 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGI--LPIKSGQILLDGKDISRLSPEQRVREG- 77
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEGi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 78 -LAY-----VPQGRDIFSTLTVeeniLIGMAKFKGAKT------RKVPEHLYEIFPILDEMKQRR-GGDLSGGQQQQLAI 144
Cdd:PRK09580 81 fMAFqypveIPGVSNQFFLQTA----LNAVRSYRGQEPldrfdfQDLMEEKIALLKMPEDLLTRSvNVGFSGGEKKRNDI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1832152097 145 ARALASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADsGEMAIVLVEQFYDFAEELADGYT-VMARGQVIAQG 216
Cdd:PRK09580 157 LQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRD-GKRSFIIVTHYQRILDYIKPDYVhVLYQGRIVKSG 228
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-221 |
2.69e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 50.11 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDvnqfyggshiLRdVSFQAPVGACSVV---------------LGRNGVGKTTLLKCLMGILP---IKSGQILLDG 62
Cdd:PRK09473 12 LLDVKD----------LR-VTFSTPDGDVTAVndlnfslragetlgiVGESGSGKSQTAFALMGLLAangRIGGSATFNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 63 KDISRLSPEQ--RVR-EGLAYVPQgrDIFSTLT----VEENILIGMAKFKGAKTRKVPEhlyEIFPILD-----EMKQRR 130
Cdd:PRK09473 81 REILNLPEKElnKLRaEQISMIFQ--DPMTSLNpymrVGEQLMEVLMLHKGMSKAEAFE---ESVRMLDavkmpEARKRM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 131 G---GDLSGGQQQQLAIARALASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVM 207
Cdd:PRK09473 156 KmypHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVM 235
|
250
....*....|....
gi 1832152097 208 ARGQVIAQGAGREM 221
Cdd:PRK09473 236 YAGRTMEYGNARDV 249
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
12-161 |
3.42e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.24 E-value: 3.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 12 GGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLdgkdisrlSPEQRVREGLAYVPQGRDIFStl 91
Cdd:PLN03073 520 GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFR--------SAKVRMAVFSQHHVDGLDLSS-- 589
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1832152097 92 tveeNILIGMAK-FKGAKTRKVPEHLYEiFPILDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDEPT 161
Cdd:PLN03073 590 ----NPLLYMMRcFPGVPEQKLRAHLGS-FGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPS 655
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
134-202 |
4.87e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 50.21 E-value: 4.87e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1832152097 134 LSGGQQQQLAIARALASEPK--VLILDEPTEGIQPSIIKDIGRVIRKLADSGEmAIVLVE---QFYDFAEELAD 202
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGN-TVLLVEhdeQMISLADRIID 549
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
3-166 |
4.99e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.63 E-value: 4.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 3 EVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIK-SGQILLDGK---------DI------- 65
Cdd:PRK10938 262 VLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGySNDLTLFGRrrgsgetiwDIkkhigyv 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 66 -SRLSPEQRVreglayvpqgrdifSTlTVEENIL------IGMAKFKGAKTRKVPEHLYEIFPILDEMKQRRGGDLSGGQ 138
Cdd:PRK10938 342 sSSLHLDYRV--------------ST-SVRNVILsgffdsIGIYQAVSDRQQKLAQQWLDILGIDKRTADAPFHSLSWGQ 406
|
170 180
....*....|....*....|....*...
gi 1832152097 139 QQQLAIARALASEPKVLILDEPTEGIQP 166
Cdd:PRK10938 407 QRLALIVRALVKHPTLLILDEPLQGLDP 434
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-191 |
5.00e-07 |
|
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: 49.78 E-value: 5.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 32 VLGRNGVGKTTLLKCLMGIL-P--------------IK--SGQILLDG-KDISrlspEQRVRegLAYVPQGRDI---FST 90
Cdd:COG1245 104 ILGPNGIGKSTALKILSGELkPnlgdydeepswdevLKrfRGTELQDYfKKLA----NGEIK--VAHKPQYVDLipkVFK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 91 LTVEEnILigmakfKGAKTRKVPEHLYEIF---PILDemkqRRGGDLSGGQQQQLAIARALASEPKVLILDEPTEGIqps 167
Cdd:COG1245 178 GTVRE-LL------EKVDERGKLDELAEKLgleNILD----RDISELSGGELQRVAIAAALLRDADFYFFDEPSSYL--- 243
|
170 180 190
....*....|....*....|....*....|
gi 1832152097 168 iikDIG------RVIRKLADSGEmAIVLVE 191
Cdd:COG1245 244 ---DIYqrlnvaRLIRELAEEGK-YVLVVE 269
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
17-159 |
1.40e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 48.43 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 17 LRDVSFQAPVGACSV--------------VLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEqrvreglAYVP 82
Cdd:PRK10522 325 LRNVTFAYQDNGFSVgpinltikrgellfLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPE-------DYRK 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 83 QGRDIFSTLTVEENILigmakfkGAKTRKVPEHLYEIFPILDEMKQR---RGG-----DLSGGQQQQLAIARALASEPKV 154
Cdd:PRK10522 398 LFSAVFTDFHLFDQLL-------GPEGKPANPALVEKWLERLKMAHKlelEDGrisnlKLSKGQKKRLALLLALAEERDI 470
|
....*
gi 1832152097 155 LILDE 159
Cdd:PRK10522 471 LLLDE 475
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
16-216 |
5.86e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 45.85 E-value: 5.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 16 ILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILP----IKSGQILLDGKdisRLSPEQRVREGLAYVPQG-RDIFST 90
Cdd:PRK10418 18 LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPagvrQTAGRVLLDGK---PVAPCALRGRKIATIMQNpRSAFNP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 91 L-TVEENIL-IGMAKFKGAKTRKVPEHLYEI-FPILDEMKQRRGGDLSGGQQQQLAIARALASEPKVLILDEPTEGI--- 164
Cdd:PRK10418 95 LhTMHTHAReTCLALGKPADDATLTAALEAVgLENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLdvv 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1832152097 165 -QPSIIKDIGRVIRKLAdsgeMAIVLVEQFYDFAEELADGYTVMARGQVIAQG 216
Cdd:PRK10418 175 aQARILDLLESIVQKRA----LGMLLVTHDMGVVARLADDVAVMSHGRIVEQG 223
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
134-164 |
1.21e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.79 E-value: 1.21e-05
10 20 30
....*....|....*....|....*....|.
gi 1832152097 134 LSGGQQQQLAIARALASEPKVLILDEPTEGI 164
Cdd:PTZ00265 580 LSGGQKQRISIARAIIRNPKILILDEATSSL 610
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
34-159 |
1.74e-05 |
|
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: 45.17 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 34 GRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEqrvreglAYvpqgRDIFSTltveenI---------LIGMAkf 104
Cdd:COG4615 365 GGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNRE-------AY----RQLFSA------VfsdfhlfdrLLGLD-- 425
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1832152097 105 KGAKTRKVPEHlyeifpiLDEMK-----QRRGG-----DLSGGQQQQLAIARALASEPKVLILDE 159
Cdd:COG4615 426 GEADPARAREL-------LERLEldhkvSVEDGrfsttDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-161 |
1.82e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.16 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 1 MLEVKDVNQFYGGSHILRDVSFQAPVGACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLdGKDISrlspeqrvregLAY 80
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGIK-----------LGY 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 81 VPQGRDIFstLTVEENILigmakfkgaktrkvpEHLYEIFPILDEMKQR--------RG-------GDLSGGQQQQLAIA 145
Cdd:PRK10636 380 FAQHQLEF--LRADESPL---------------QHLARLAPQELEQKLRdylggfgfQGdkvteetRRFSGGEKARLVLA 442
|
170
....*....|....*.
gi 1832152097 146 RALASEPKVLILDEPT 161
Cdd:PRK10636 443 LIVWQRPNLLLLDEPT 458
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-161 |
5.01e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 41.98 E-value: 5.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 32 VLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISRLSPEQRVREGLAYvpqgrdifstltveeniligmakfkgaktrk 111
Cdd:smart00382 7 IVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVG------------------------------- 55
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1832152097 112 vpehlyeifpildemkqRRGGDLSGGQQQQLAIARALASEPKVLILDEPT 161
Cdd:smart00382 56 -----------------GKKASGSGELRLRLALALARKLKPDVLILDEIT 88
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
29-161 |
6.80e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 42.59 E-value: 6.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 29 CSVVLGRNGVGKTTLLKC----LMGILPIKSGQILLDGKDIsrlspeqRVREGLAYVpqgrdifsTLTVEENiligmakf 104
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEAlkyaLTGELPPNSKGGAHDPKLI-------REGEVRAQV--------KLAFENA-------- 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1832152097 105 KGAK---TRKVPEHLYEIF--------PILDEMKQrrggdLSGGQQQ------QLAIARALASEPKVLILDEPT 161
Cdd:cd03240 81 NGKKytiTRSLAILENVIFchqgesnwPLLDMRGR-----CSGGEKVlasliiRLALAETFGSNCGILALDEPT 149
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
11-228 |
1.07e-04 |
|
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: 41.40 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 11 YGGSHILrdvsFQAPV---GACSVVLGRNGVGKTTLLKCLMGILPIKSGQILLDGKDISrlspeqrvreglaYVPQgrdi 87
Cdd:cd03222 10 YGVFFLL----VELGVvkeGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV-------------YKPQ---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 88 fstltveeniligmakfkgaktrKVpehlyeifpildemkqrrggDLSGGQQQQLAIARALASEPKVLILDEPTEGIQPS 167
Cdd:cd03222 69 -----------------------YI--------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIE 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1832152097 168 IIKDIGRVIRKLADSGEMAIVLVEQFYDFAEELADGYTVMaRGQviAQGAGREMPEKGIRE 228
Cdd:cd03222 106 QRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVF-EGE--PGVYGIASQPKGTRE 163
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
22-191 |
4.01e-04 |
|
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: 40.43 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 22 FQAPVGACSVVLG---RNGVGKTTLLKCLMGILPIKSGQilLDGK-------DISRLSPEQ----RVREG---LAYVPQG 84
Cdd:cd03236 18 HRLPVPREGQVLGlvgPNGIGKSTALKILAGKLKPNLGK--FDDPpdwdeilDEFRGSELQnyftKLLEGdvkVIVKPQY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 85 RDIFSTLTVEENILIGMAKFKGAKTRKVPEHLyEIFPILDemkqRRGGDLSGGQQQQLAIARALASEPKVLILDEPTEGI 164
Cdd:cd03236 96 VDLIPKAVKGKVGELLKKKDERGKLDELVDQL-ELRHVLD----RNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYL 170
|
170 180 190
....*....|....*....|....*....|...
gi 1832152097 165 qpsiikDIG------RVIRKLADSGEmAIVLVE 191
Cdd:cd03236 171 ------DIKqrlnaaRLIRELAEDDN-YVLVVE 196
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
134-188 |
1.26e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 39.13 E-value: 1.26e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1832152097 134 LSGGQQQQLAIARAL---ASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIV 188
Cdd:cd03271 170 LSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVV 227
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
134-216 |
1.32e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.61 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832152097 134 LSGGQQQQLAIARAL---ASEPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGEmAIVLVEQFYDFAEElADgYTV---- 206
Cdd:TIGR00630 830 LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGN-TVVVIEHNLDVIKT-AD-YIIdlgp 906
|
90
....*....|...
gi 1832152097 207 ---MARGQVIAQG 216
Cdd:TIGR00630 907 eggDGGGTVVASG 919
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
134-189 |
1.96e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.04 E-value: 1.96e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1832152097 134 LSGGQQQQLAIARALAS---EPKVLILDEPTEGIQPSIIKDIGRVIRKLADSGEMAIVL 189
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVII 868
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
129-191 |
4.66e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 37.24 E-value: 4.66e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1832152097 129 RRGGDLSGGQQQQLAIARALASE-PKVL-ILDEPTEGIQPSIIKDIGRVIRKLADSGEmAIVLVE 191
Cdd:cd03270 133 RSAPTLSGGEAQRIRLATQIGSGlTGVLyVLDEPSIGLHPRDNDRLIETLKRLRDLGN-TVLVVE 196
|
|
| |
