|
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 |
2.25e-142 |
|
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: 397.28 E-value: 2.25e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQSGVAYV 81
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 82 PQGREIFPRLTVEENLLMGLSRFsAGNARSVPEEIWQLFPVLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEPT 161
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTGLAAL-PRRSRKIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737198856 162 EGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQGRGENMEQEGVRGLVAI 232
Cdd:TIGR03410 160 EGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDKVRRYLAV 230
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-221 |
3.00e-116 |
|
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: 331.18 E-value: 3.00e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQSGVAY 80
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 81 VPQGREIFPRLTVEENLLMGL-SRFSAGNARSVPEEIWQLFPVLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDE 159
Cdd:COG0410 83 VPEGRRIFPSLTVEENLLLGAyARRDRAEVRADLERVYELFPRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1737198856 160 PTEGIQPSVIKEIGQVIRSLANRGdMAILLVEQFYDFAAELADSYLVMSRGSIVQQGRGENM 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 ... |
2-224 |
2.53e-113 |
|
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: 323.23 E-value: 2.53e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQSGVAYV 81
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 82 PQGREIFPRLTVEENLLMGLSRFSAGNARSVPEEIWQLFPVLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEPT 161
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1737198856 162 EGIQPSVIKEIGQVIRSLANRGdMAILLVEQFYDFAAELADSYLVMSRGSIVQQGRGENMEQE 224
Cdd:cd03224 161 EGLAPKIVEEIFEAIRELRDEG-VTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-216 |
1.47e-57 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 182.19 E-value: 1.47e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSkpHQRVQSGVAYV 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARD--PAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 82 PQGREIFPRLTVEENLLM--GLSRFSAGNARSVPEEIWQLFPvLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDE 159
Cdd:COG1131 79 PQEPALYPDLTVRENLRFfaRLYGLPRKEARERIDELLELFG-LTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1737198856 160 PTEGIQPSVIKEIGQVIRSLANRGdMAILLVEQFYDFAAELADSYLVMSRGSIVQQG 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 ... |
2-217 |
5.62e-55 |
|
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: 175.70 E-value: 5.62e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQSGVAYV 81
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 82 PQGREIFPRLTVEENLLMGLSR------FSAGNARSVPEEIWQLFPVLKEMK-----HRRGGDLSGGQQQQLAIGRALAS 150
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAQArtgsglLLARARREEREARERAEELLERVGladlaDRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1737198856 151 RPRLLILDEPTEGIQPSVIKEIGQVIRSLANRGdMAILLVEQFYDFAAELADSYLVMSRGSIVQQGR 217
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRERG-ITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGT 226
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-216 |
1.56e-53 |
|
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: 172.53 E-value: 1.56e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQSGVAY 80
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLGIAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 81 VPQGREIFPRLTVEENLLMGLSRFSAGNA--------------RSVPEEIWQL--FPVLKEMKHRRGGDLSGGQQQQLAI 144
Cdd:COG0411 84 TFQNPRLFPELTVLENVLVAAHARLGRGLlaallrlprarreeREARERAEELleRVGLADRADEPAGNLSYGQQRRLEI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1737198856 145 GRALASRPRLLILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:COG0411 164 ARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEG 235
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-216 |
3.88e-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: 3.88e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPhqRVQSGVAY 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR--EARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 81 VPQGREIFPRLTVEENLLMgLSRFSAGNARSVPEEIWQLFPVLK--EMKHRRGGDLSGGQQQQLAIGRALASRPRLLILD 158
Cdd:COG4555 79 LPDERGLYDRLTVRENIRY-FAELYGLFDEELKKRIEELIELLGleEFLDRRVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1737198856 159 EPTEGIQPSVIKEIGQVIRSLANRGdMAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:COG4555 158 EPTNGLDVMARRLLREILRALKKEG-KTVLFSSHIMQEVEALCDRVVILHKGKVVAQG 214
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-227 |
2.45e-51 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 166.59 E-value: 2.45e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQSGVAY 80
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 81 VPQGREIFPRLTVEENLLMGLSRFSAGNARSVPEEIWQLFPVLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEP 160
Cdd:PRK11614 85 VPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1737198856 161 TEGIQPSVIKEIGQVIRSLANRGdMAILLVEQFYDFAAELADSYLVMSRGSIVQQGRGEN-MEQEGVR 227
Cdd:PRK11614 165 SLGLAPIIIQQIFDTIEQLREQG-MTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDAlLANEAVR 231
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-216 |
1.03e-49 |
|
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: 162.91 E-value: 1.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQSgVAY 80
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARR-IAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 81 VPQGREIFPRLTVEENLLMG-------LSRFSAGNARSVPEEIWQLfpVLKEMKHRRGGDLSGGQQQQLAIGRALASRPR 153
Cdd:COG1120 80 VPQEPPAPFGLTVRELVALGryphlglFGRPSAEDREAVEEALERT--GLEHLADRPVDELSGGERQRVLIARALAQEPP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1737198856 154 LLILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:COG1120 158 LLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQG 220
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-212 |
3.05e-49 |
|
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: 159.10 E-value: 3.05e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSIThsKPHQRVQSGVAYV 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK--KEPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 82 PQGREIFPRLTVEENLlmglsrfsagnarsvpeeiwqlfpvlkemkhrrggDLSGGQQQQLAIGRALASRPRLLILDEPT 161
Cdd:cd03230 79 PEEPSLYENLTVRENL-----------------------------------KLSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1737198856 162 EGIQPSVIKEIGQVIRSLANRGdMAILLVEQFYDFAAELADSYLVMSRGSI 212
Cdd:cd03230 124 SGLDPESRREFWELLRELKKEG-KTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-216 |
1.45e-47 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 156.69 E-value: 1.45e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPH-QRVQSGVA 79
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDiNKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 80 YVPQGREIFPRLTVEENLLMGLSR---FSAGNARSVPEEiwQLFPV-LKEMKHRRGGDLSGGQQQQLAIGRALASRPRLL 155
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPIKvkkMSKAEAEERAME--LLERVgLADKADAYPAQLSGGQQQRVAIARALAMEPKVM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737198856 156 ILDEPTEGIQPSVIKEIGQVIRSLANRGdMAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:COG1126 159 LFDEPTSALDPELVGEVLDVMRDLAKEG-MTMVVVTHEMGFAREVADRVVFMDGGRIVEEG 218
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-216 |
3.09e-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: 155.37 E-value: 3.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRvqsGVAYV 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERR---NIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 82 PQGREIFPRLTVEENLLMGLSRFSAGNA---RSVPEEIWQLfpVLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILD 158
Cdd:cd03259 78 FQDYALFPHLTVAENIAFGLKLRGVPKAeirARVRELLELV--GLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1737198856 159 EPTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:cd03259 156 EPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-212 |
3.28e-47 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 156.02 E-value: 3.28e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHqrvqsgVAY 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR------IGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 81 VPQGREI---FPrLTVEENLLMGL-------SRFSAGNARSVPEeiwqlfpVLKEM-----KHRRGGDLSGGQQQQLAIG 145
Cdd:COG1121 80 VPQRAEVdwdFP-ITVRDVVLMGRygrrglfRRPSRADREAVDE-------ALERVgledlADRPIGELSGGQQQRVLLA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1737198856 146 RALASRPRLLILDEPTEGIQPSVIKEIGQVIRSLANRGdMAILLVEQFYDFAAELADSYLVMSRGSI 212
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREG-KTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-212 |
2.22e-45 |
|
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: 150.37 E-value: 2.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPH-QRVQSGVAY 80
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNiNELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 81 VPQGREIFPRLTVEENLLMGL---SRFSAGNARSVPEEIwqLFPV-LKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLI 156
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPikvKGMSKAEAEERALEL--LEKVgLADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1737198856 157 LDEPTEGIQPSVIKEIGQVIRSLANRGdMAILLVEQFYDFAAELADSYLVMSRGSI 212
Cdd:cd03262 159 FDEPTSALDPELVGEVLDVMKDLAEEG-MTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-188 |
8.64e-45 |
|
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: 148.78 E-value: 8.64e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQsgVAY 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRR--LAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 81 VPQGREIFPRLTVEENLlmglsRFSAG--NARSVPEEIWQLFPV--LKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLI 156
Cdd:COG4133 80 LGHADGLKPELTVRENL-----RFWAAlyGLRADREAIDEALEAvgLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190
....*....|....*....|....*....|..
gi 1737198856 157 LDEPTEGIQPSVIKEIGQVIRSLANRGDMAIL 188
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAHLARGGAVLL 186
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-189 |
9.56e-45 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 149.79 E-value: 9.56e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQSGVAY 80
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 81 VPQGREIFPRLTVEENLLMGL--SRFSAGNARSVPEEIWQLFPvLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILD 158
Cdd:COG1137 83 LPQEASIFRKLTVEDNILAVLelRKLSKKEREERLEELLEEFG-ITHLRKSKAYSLSGGERRRVEIARALATNPKFILLD 161
|
170 180 190
....*....|....*....|....*....|.
gi 1737198856 159 EPTEGIQPSVIKEIGQVIRSLANRGdMAILL 189
Cdd:COG1137 162 EPFAGVDPIAVADIQKIIRHLKERG-IGVLI 191
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-227 |
1.51e-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: 146.15 E-value: 1.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQSGVAYV 81
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 82 PQGREIFPRLTVEENLLMGLSRFSAGNA--RSVPEEIWQLFPvLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDE 159
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKerEEKLEELLEEFH-ITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1737198856 160 PTEGIQPSVIKEIGQVIRSLANRGdMAILLVEQFYDFAAELADSYLVMSRGSIVQQGRGENM-EQEGVR 227
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIKILKDRG-IGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIaANELVR 227
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-190 |
3.30e-43 |
|
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: 144.98 E-value: 3.30e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 3 QVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSIThskphqRVQSGVAYVP 82
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE------KERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 83 QGREI---FPrLTVEENLLMGL---SRFSAGNARSVPEEIWQL--FPVLKEMKHRRGGDLSGGQQQQLAIGRALASRPRL 154
Cdd:cd03235 75 QRRSIdrdFP-ISVRDVVLMGLyghKGLFRRLSKADKAKVDEAleRVGLSELADRQIGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190
....*....|....*....|....*....|....*.
gi 1737198856 155 LILDEPTEGIQPSVIKEIGQVIRSLANRGdMAILLV 190
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLRELRREG-MTILVV 188
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-216 |
9.14e-43 |
|
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: 150.82 E-value: 9.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGS-----HILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQR-- 73
Cdd:COG1123 260 LLEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLre 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 74 VQSGVAYVPQG--REIFPRLTVEENLLMGLSRFSAGNARSVPE------EIWQLFPvlkEMKHRRGGDLSGGQQQQLAIG 145
Cdd:COG1123 340 LRRRVQMVFQDpySSLNPRMTVGDIIAEPLRLHGLLSRAERRErvaellERVGLPP---DLADRYPHELSGGQRQRVAIA 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737198856 146 RALASRPRLLILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:COG1123 417 RALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDG 487
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-216 |
1.07e-42 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 147.55 E-value: 1.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRvqsGVAY 80
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKR---NVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 81 VPQGREIFPRLTVEENLLMGLS--RFSAGNARSVPEEIWQLfpV-LKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLIL 157
Cdd:COG3842 82 VFQDYALFPHLTVAENVAFGLRmrGVPKAEIRARVAELLEL--VgLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1737198856 158 DEPTEGIQPSVIKEIGQVIRSLANRGDMAILLV-----EqfydfAAELADSYLVMSRGSIVQQG 216
Cdd:COG3842 160 DEPLSALDAKLREEMREELRRLQRELGITFIYVthdqeE-----ALALADRIAVMNDGRIEQVG 218
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
9-213 |
1.27e-42 |
|
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: 143.17 E-value: 1.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 9 QYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSIthsKPHQRVQSgVAYVPQ--GRE 86
Cdd:cd03226 8 SYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKS-IGYVMQdvDYQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 87 IFpRLTVEENLLMGLSRFSAGNARSvpEEIWQLFPvLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEPTEGIQP 166
Cdd:cd03226 84 LF-TDSVREELLLGLKELDAGNEQA--ETVLKDLD-LYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDY 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1737198856 167 SVIKEIGQVIRSLANRGdMAILLVEQFYDFAAELADSYLVMSRGSIV 213
Cdd:cd03226 160 KNMERVGELIRELAAQG-KAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-229 |
1.40e-42 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 144.43 E-value: 1.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELN-QYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPH--QRVQSG 77
Cdd:COG3638 2 MLELRNLSkRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRalRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 78 VAYVPQGREIFPRLTVEENLLMG-LSRFSAgnARSvpeeIWQLFPV--------------LKEMKHRRGGDLSGGQQQQL 142
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVLAGrLGRTST--WRS----LLGLFPPedreralealervgLADKAYQRADQLSGGQQQRV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 143 AIGRALASRPRLLILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQGRGENME 222
Cdd:COG3638 156 AIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAELT 235
|
....*..
gi 1737198856 223 QEGVRGL 229
Cdd:COG3638 236 DAVLREI 242
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
10-216 |
1.90e-41 |
|
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: 140.93 E-value: 1.90e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 10 YYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQSgVAYVPQgreiFP 89
Cdd:COG1122 10 YPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRK-VGLVFQ----NP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 90 RL-----TVEENLL-----MGLSRfsagnarsvpEEIWQLfpV--------LKEMKHRRGGDLSGGQQQQLAIGRALASR 151
Cdd:COG1122 85 DDqlfapTVEEDVAfgpenLGLPR----------EEIRER--VeealelvgLEHLADRPPHELSGGQKQRVAIAGVLAME 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1737198856 152 PRLLILDEPTEGIQPSVIKEIGQVIRSLANRGdMAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRRELLELLKRLNKEG-KTVIIVTHDLDLVAELADRVIVLDDGRIVADG 216
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-216 |
2.79e-41 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 140.33 E-value: 2.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGS----HILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQS 76
Cdd:cd03257 1 LLEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 77 G--VAYVPQ--GREIFPRLTVEENLLMGLSRFSAGNARSVPEEIWQL----FPVLKEMKHRRGGDLSGGQQQQLAIGRAL 148
Cdd:cd03257 81 RkeIQMVFQdpMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLllvgVGLPEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1737198856 149 ASRPRLLILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-216 |
2.89e-41 |
|
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: 138.72 E-value: 2.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 3 QVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQSgVAYVP 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARK-IAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 83 QGREifprltveenlLMGLSrfsagnarsvpeeiwqlfpvlkEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEPTE 162
Cdd:cd03214 80 QALE-----------LLGLA----------------------HLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1737198856 163 GIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:cd03214 127 HLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
9-210 |
1.09e-40 |
|
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: 138.37 E-value: 1.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 9 QYYGGSH-ILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQSgVAYVPQgrei 87
Cdd:cd03225 8 SYPDGARpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRK-VGLVFQ---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 88 FPR-----LTVEENLLmglsrFSAGNARSVPEEIWQ-----LFPV-LKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLI 156
Cdd:cd03225 83 NPDdqffgPTVEEEVA-----FGLENLGLPEEEIEErveeaLELVgLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1737198856 157 LDEPTEGIQPSVIKEIGQVIRSLANRGdMAILLVEQFYDFAAELADSYLVMSRG 210
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAEG-KTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-216 |
1.58e-40 |
|
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: 145.05 E-value: 1.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYY--GGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKG---GEVVWQGKSITHSKPHQRVQ 75
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 76 SgVAYVPQGREI-FPRLTVEENLLMGLSRFSAGNARSVPEEIWQLFPV-LKEMKHRRGGDLSGGQQQQLAIGRALASRPR 153
Cdd:COG1123 84 R-IGMVFQDPMTqLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVgLERRLDRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1737198856 154 LLILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:COG1123 163 LLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDG 225
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-210 |
2.13e-40 |
|
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: 136.55 E-value: 2.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSIT-HSKPHQRVQSGVAY 80
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 81 VPQGREIFPRLTVEENLLMGlsrfsagnarsvpeeiwqlfpvlkemkhrrggdLSGGQQQQLAIGRALASRPRLLILDEP 160
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG---------------------------------LSGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1737198856 161 TEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRG 210
Cdd:cd03229 128 TSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-216 |
2.23e-40 |
|
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: 138.78 E-value: 2.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYG----GSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKP---HQR 73
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRkafRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 74 VQsgvaYVPQ-GREIF-PRLTVEENL-----LMGLSRfsagnarsVPEEIWQLFPVL---KEMKHRRGGDLSGGQQQQLA 143
Cdd:COG1124 81 VQ----MVFQdPYASLhPRHTVDRILaeplrIHGLPD--------REERIAELLEQVglpPSFLDRYPHQLSGGQRQRVA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1737198856 144 IGRALASRPRLLILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEEL 221
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-216 |
1.51e-39 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 135.42 E-value: 1.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITH-SKPHQRVQSGVAY 80
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKnIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 81 vPqgrEIFPRLTVEENL-----LMGLSRfsagnarsvpEEIWQLFPV--LKEMKHRRGGDLSGGQQQQLAIGRALASRPR 153
Cdd:cd03268 81 -P---GFYPNLTARENLrllarLLGIRK----------KRIDEVLDVvgLKDSAKKKVKGFSLGMKQRLGIALALLGNPD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1737198856 154 LLILDEPTEGIQPSVIKEIGQVIRSLANRGdMAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:cd03268 147 LLILDEPTNGLDPDGIKELRELILSLRDQG-ITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
10-227 |
1.67e-38 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 133.46 E-value: 1.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 10 YYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPH--QRVQSGVAYVPQGREI 87
Cdd:cd03256 10 YPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKalRQLRRQIGMIFQQFNL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 88 FPRLTVEENLLMG-LSRFSAGNArsvpeeIWQLFPV--------------LKEMKHRRGGDLSGGQQQQLAIGRALASRP 152
Cdd:cd03256 90 IERLSVLENVLSGrLGRRSTWRS------LFGLFPKeekqralaalervgLLDKAYQRADQLSGGQQQRVAIARALMQQP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1737198856 153 RLLILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQGRGENMEQEGVR 227
Cdd:cd03256 164 KLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEVLD 238
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-216 |
2.42e-38 |
|
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: 132.63 E-value: 2.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGS--HILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHqrVQSGVA 79
Cdd:cd03263 1 LQIRNLTKTYKKGtkPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKA--ARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 80 YVPQGREIFPRLTVEENLLMgLSRFSAGNARSVPEEIWQLFPV--LKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLIL 157
Cdd:cd03263 79 YCPQFDALFDELTVREHLRF-YARLKGLPKSEIKEEVELLLRVlgLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1737198856 158 DEPTEGIQPSVIKEIGQVIRSLanRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
17-212 |
2.62e-38 |
|
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: 131.40 E-value: 2.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 17 LRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQSGVAYVPQGRE---IFPRLTV 93
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAYVPEDRKregLVLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 94 EENLLMGLSrfsagnarsvpeeiwqlfpvlkemkhrrggdLSGGQQQQLAIGRALASRPRLLILDEPTEGIQPSVIKEIG 173
Cdd:cd03215 96 AENIALSSL-------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIY 144
|
170 180 190
....*....|....*....|....*....|....*....
gi 1737198856 174 QVIRSLANRGdMAILLVEQFYDFAAELADSYLVMSRGSI 212
Cdd:cd03215 145 RLIRELADAG-KAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-231 |
5.54e-38 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 132.07 E-value: 5.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGSHiLRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRvqsGVAYV 81
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKR---DISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 82 PQGREIFPRLTVEENLLMGLsRFSAGNARSVPEEIWQLFPVLK--EMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDE 159
Cdd:cd03299 77 PQNYALFPHMTVYKNIAYGL-KKRKVDKKEIERKVLEIAEMLGidHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1737198856 160 PTEG----IQPSVIKEIGQVIRSLanrgDMAILLVEQFYDFAAELADSYLVMSRGSIVQQGRGENMEQEGVRGLVA 231
Cdd:cd03299 156 PFSAldvrTKEKLREELKKIRKEF----GVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVA 227
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-221 |
5.96e-38 |
|
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: 131.72 E-value: 5.96e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSIThsKPHQRVQSGVAYV 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV--REPREVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 82 PQGREIFPRLTVEENLLM--GLSRFSAGNARSVPEEIWQLFPvLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDE 159
Cdd:cd03265 79 FQDLSVDDELTGWENLYIhaRLYGVPGAERRERIDELLDFVG-LLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1737198856 160 PTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQGRGENM 221
Cdd:cd03265 158 PTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-210 |
1.09e-37 |
|
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: 128.90 E-value: 1.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 3 QVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQrVQSGVAYVP 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEE-LRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 83 QgreifprltveenllmglsrfsagnarsvpeeiwqlfpvlkemkhrrggdLSGGQQQQLAIGRALASRPRLLILDEPTE 162
Cdd:cd00267 80 Q--------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1737198856 163 GIQPSVIKEIGQVIRSLANRGdMAILLVEQFYDFAAELADSYLVMSRG 210
Cdd:cd00267 110 GLDPASRERLLELLRELAEEG-RTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-161 |
4.74e-37 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 126.99 E-value: 4.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 17 LRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHsKPHQRVQSGVAYVPQGREIFPRLTVEEN 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTD-DERKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737198856 97 LLMG--LSRFSAGNARSVPEEIWQLFPvLKEMKHRR----GGDLSGGQQQQLAIGRALASRPRLLILDEPT 161
Cdd:pfam00005 80 LRLGllLKGLSKREKDARAEEALEKLG-LGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-216 |
1.17e-36 |
|
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: 128.77 E-value: 1.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQ----RVQSG 77
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 78 VAYvpQGREIFPRLTVEENLLMGLSRFSAGNARSVPEEIWQ-LFPV-LKEMKHRRGGDLSGGQQQQLAIGRALASRPRLL 155
Cdd:cd03261 81 MLF--QSGALFDSLTVFENVAFPLREHTRLSEEEIREIVLEkLEAVgLRGAEDLYPAELSGGMKKRVALARALALDPELL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737198856 156 ILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:cd03261 159 LYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEG 219
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-216 |
1.26e-36 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 127.80 E-value: 1.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 27 GEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQG-------KSItHSKPHQRvqsGVAYVPQGREIFPRLTVEENLLM 99
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrKKI-NLPPQQR---KIGLVFQQYALFPHLNVRENLAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 100 GLSRFSAGNARSVPEEIWQLFPvLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEPTEGIQPSVIKEIGQVIRSL 179
Cdd:cd03297 99 GLKRKRNREDRISVDELLDLLG-LDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQI 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 1737198856 180 ANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:cd03297 178 KKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-216 |
2.35e-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: 127.48 E-value: 2.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYY----GGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKphQRVQS 76
Cdd:cd03266 1 MITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEP--AEARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 77 GVAYVPQGREIFPRLTVEENL-----LMGLSRfSAGNARSvpEEIWQLFPvLKEMKHRRGGDLSGGQQQQLAIGRALASR 151
Cdd:cd03266 79 RLGFVSDSTGLYDRLTARENLeyfagLYGLKG-DELTARL--EELADRLG-MEELLDRRVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1737198856 152 PRLLILDEPTEGIQPSVIKEIGQVIRSLANRGDmAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQLRALGK-CILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-216 |
4.32e-36 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 129.88 E-value: 4.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSI-THSKPHQRvqsGVAY 80
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRER---RVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 81 VPQGREIFPRLTVEENLLMGLS--RFSAGNARSVPEEIWQLFPvLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILD 158
Cdd:COG1118 80 VFQHYALFPHMTVAENIAFGLRvrPPSKAEIRARVEELLELVQ-LEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1737198856 159 EPTEGIQPSVIKEIGQVIRSLANRGDMAILLV-----EqfydfAAELADSYLVMSRGSIVQQG 216
Cdd:COG1118 159 EPFGALDAKVRKELRRWLRRLHDELGGTTVFVthdqeE-----ALELADRVVVMNQGRIEQVG 216
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-213 |
5.50e-36 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 132.45 E-value: 5.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQSGVAY 80
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAGIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 81 VPQGREIFPRLTVEENLLMG-------LSRFSAGNARSvpEEIwqlfpvLKEMK-----HRRGGDLSGGQQQQLAIGRAL 148
Cdd:COG1129 84 IHQELNLVPNLSVAENIFLGreprrggLIDWRAMRRRA--REL------LARLGldidpDTPVGDLSVAQQQLVEIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1737198856 149 ASRPRLLILDEPTEGIQPSVIKEIGQVIRSLANRGdMAILLVEQFYDFAAELADSYLVMSRGSIV 213
Cdd:COG1129 156 SRDARVLILDEPTASLTEREVERLFRIIRRLKAQG-VAIIYISHRLDEVFEIADRVTVLRDGRLV 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-226 |
5.85e-36 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 132.45 E-value: 5.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNqyygGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQSGVAY 80
Cdd:COG1129 256 VLEVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAGIAY 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 81 VP-----QGreIFPRLTVEENLLMG-LSRFSAGNARSVPEEIWQLFPVLKEMK------HRRGGDLSGGQQQQLAIGRAL 148
Cdd:COG1129 332 VPedrkgEG--LVLDLSIRENITLAsLDRLSRGGLLDRRRERALAEEYIKRLRiktpspEQPVGNLSGGNQQKVVLAKWL 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 149 ASRPRLLILDEPTEGIQPSVIKEIGQVIRSLANRGdMAILLV-----EqfydfAAELADSYLVMSRGSIVQQGRGENMEQ 223
Cdd:COG1129 410 ATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEG-KAVIVIsselpE-----LLGLSDRILVMREGRIVGELDREEATE 483
|
...
gi 1737198856 224 EGV 226
Cdd:COG1129 484 EAI 486
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
2-216 |
1.39e-35 |
|
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: 129.00 E-value: 1.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRvqsGVAYV 81
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKR---DYGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 82 PQGREIFPRLTVEENLLMGLS--RFSAGNARSVPEEIWQLFPvLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDE 159
Cdd:TIGR03265 82 FQSYALFPNLTVADNIAYGLKnrGMGRAEVAERVAELLDLVG-LPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1737198856 160 PTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:TIGR03265 161 PLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVG 217
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-217 |
1.82e-35 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 125.16 E-value: 1.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGS----HILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQ- 75
Cdd:COG1136 4 LLELRNLTKSYGTGegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 76 --SGVAYVPQGREIFPRLTVEENLLMGL--SRFSAGNARSVPEEIWQLFPvLKEMKHRRGGDLSGGQQQQLAIGRALASR 151
Cdd:COG1136 84 rrRHIGFVFQFFNLLPELTALENVALPLllAGVSRKERRERARELLERVG-LGDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1737198856 152 PRLLILDEPT------EGiqpsviKEIGQVIRSLANRGDMAILLV--EQfydFAAELADSYLVMSRGSIVQQGR 217
Cdd:COG1136 163 PKLILADEPTgnldskTG------EEVLELLRELNRELGTTIVMVthDP---ELAARADRVIRLRDGRIVSDER 227
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
20-216 |
2.01e-35 |
|
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: 128.68 E-value: 2.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 20 VSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEV-----VWQ-GKSITHSKPHQRvqsGVAYVPQGREIFPRLTV 93
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIrlggeVLQdSARGIFLPPHRR---RIGYVFQEARLFPHLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 94 EENLLMGLSRFSAGNARSVPEEIWQLF---PVLKemkhRRGGDLSGGQQQQLAIGRALASRPRLLILDEPTEGIQPSVIK 170
Cdd:COG4148 95 RGNLLYGRKRAPRAERRISFDEVVELLgigHLLD----RRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1737198856 171 EIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:COG4148 171 EILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASG 216
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-216 |
2.05e-35 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 127.15 E-value: 2.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQrvqsgVAY 80
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRR-----IGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 81 VPQGREIFPRLTVEENL-----LMGLSRfSAGNARSvpeEIWqlfpvLK--EMKHRRG---GDLSGGQQQQLAIGRALAS 150
Cdd:COG4152 76 LPEERGLYPKMKVGEQLvylarLKGLSK-AEAKRRA---DEW-----LErlGLGDRANkkvEELSKGNQQKVQLIAALLH 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1737198856 151 RPRLLILDEPTEGIQP---SVIKEigqVIRSLANRGdMAIL-------LVEqfydfaaELADSYLVMSRGSIVQQG 216
Cdd:COG4152 147 DPELLILDEPFSGLDPvnvELLKD---VIRELAAKG-TTVIfsshqmeLVE-------ELCDRIVIINKGRKVLSG 211
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-231 |
2.19e-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: 125.43 E-value: 2.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRvqsGVAYV 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKR---PVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 82 PQGREIFPRLTVEENLLMGLSRfsagnARSVPEEI-----WQLFPV-LKEMKHRRGGDLSGGQQQQLAIGRALASRPRLL 155
Cdd:cd03300 78 FQNYALFPHLTVFENIAFGLRL-----KKLPKAEIkervaEALDLVqLEGYANRKPSQLSGGQQQRVAIARALVNEPKVL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1737198856 156 ILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQGRGENMEQEGVRGLVA 231
Cdd:cd03300 153 LLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVA 228
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-210 |
3.20e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 124.16 E-value: 3.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQ-RVQsgVAY 80
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwRRQ--VAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 81 VPQgrEifPRL---TVEENLLMGlsrFSAGNARSVPEEIWQLFPVL---KEMKHRRGGDLSGGQQQQLAIGRALASRPRL 154
Cdd:COG4619 79 VPQ--E--PALwggTVRDNLPFP---FQLRERKFDRERALELLERLglpPDILDKPVERLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 155 LILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILLV----EQfydfAAELADSYLVMSRG 210
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVshdpEQ----IERVADRVLTLEAG 207
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-213 |
5.07e-35 |
|
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: 122.15 E-value: 5.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQSGVAYV 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 82 PQgreifprltveenllmglsrfsagnarsvpeeiwqlfpvlkemkhrrggdLSGGQQQQLAIGRALASRPRLLILDEPT 161
Cdd:cd03216 81 YQ--------------------------------------------------LSVGERQMVEIARALARNARLLILDEPT 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1737198856 162 EGIQPSVIKEIGQVIRSLANRGdMAILLVEQFYDFAAELADSYLVMSRGSIV 213
Cdd:cd03216 111 AALTPAEVERLFKVIRRLRAQG-VAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-227 |
5.73e-35 |
|
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: 124.72 E-value: 5.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYG-GSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPH--QRVQSG 77
Cdd:TIGR02315 1 MLEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKklRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 78 VAYVPQGREIFPRLTVEENLLMGlsRFSAGNARSVpeeIWQLFPV--------------LKEMKHRRGGDLSGGQQQQLA 143
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHG--RLGYKPTWRS---LLGRFSEedkeralsalervgLADKAYQRADQLSGGQQQRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 144 IGRALASRPRLLILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQGRGENMEQ 223
Cdd:TIGR02315 156 IARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDD 235
|
....
gi 1737198856 224 EGVR 227
Cdd:TIGR02315 236 EVLR 239
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-216 |
6.11e-35 |
|
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: 124.37 E-value: 6.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRvqsGVAYV 81
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER---NVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 82 PQGREIFPRLTVEENLLMGL------SRFSAGNARSVPEEIWQLFPvLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLL 155
Cdd:cd03296 80 FQHYALFRHMTVFDNVAFGLrvkprsERPPEAEIRAKVHELLKLVQ-LDWLADRYPAQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737198856 156 ILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:cd03296 159 LLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVG 219
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-216 |
9.67e-35 |
|
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: 123.44 E-value: 9.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKG-----GEVVWQGKSITHSKPH-QRVQ 75
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPgapdeGEVLLDGKDIYDLDVDvLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 76 SGVAYVPQGREIFPrLTVEENLLMGLS---RFSAGNARSVPEEIWQLFPVLKEMKHR-RGGDLSGGQQQQLAIGRALASR 151
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRlhgIKLKEELDERVEEALRKAALWDEVKDRlHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1737198856 152 PRLLILDEPTEGIQPSVIKEIGQVIRSLANrgDMAILLV----EQfydfAAELADSYLVMSRGSIVQQG 216
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKK--EYTIVIVthnmQQ----AARVADRTAFLLNGRLVEFG 222
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-216 |
1.19e-34 |
|
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: 122.77 E-value: 1.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQrvqsgVAYV 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNR-----IGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 82 PQGREIFPRLTVEENL-----LMGLSRFSAgnARSVPEEIWQLfpVLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLI 156
Cdd:cd03269 76 PEERGLYPKMKVIDQLvylaqLKGLKKEEA--RRRIDEWLERL--ELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 157 LDEPTEGIQPSVIKEIGQVIRSLANRGdMAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRELARAG-KTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
20-221 |
1.60e-34 |
|
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: 125.99 E-value: 1.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 20 VSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSK------PHQRvqsGVAYVPQGREIFPRLTV 93
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRkgiflpPEKR---RIGYVFQEARLFPHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 94 EENLLMGLSRFSAGNARSVPEEIWQLFPvLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEPTEGIQPSVIKEIG 173
Cdd:TIGR02142 93 RGNLRYGMKRARPSERRISFERVIELLG-IGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEIL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1737198856 174 QVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQGRGENM 221
Cdd:TIGR02142 172 PYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-216 |
2.38e-34 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 122.89 E-value: 2.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQR-VQSGVA 79
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERlIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 80 YVPQGREIFPRLTVEENLLMGLSRF---SAGNARSVPEEIwqLFPV-LKEMKHRRGGDLSGGQQQQLAIGRALASRPRLL 155
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFGPLRVrgaSKEEAEKQAREL--LAKVgLAERAHHYPSELSGGQQQRVAIARALAVKPKLM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737198856 156 ILDEPTEGIQPSVIKEIGQVIRSLANRGdMAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:PRK09493 159 LFDEPTSALDPELRHEVLKVMQDLAEEG-MTMVIVTHEIGFAEKVASRLIFIDKGRIAEDG 218
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-212 |
3.11e-34 |
|
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: 121.83 E-value: 3.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGG----SHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQ-- 75
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAfr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 76 -SGVAYVPQGREIFPRLTVEENLLMGLsRFSAGNARSVPEEIWQLFPV--LKEMKHRRGGDLSGGQQQQLAIGRALASRP 152
Cdd:cd03255 81 rRHIGFVFQSFNLLPDLTALENVELPL-LLAGVPKKERRERAEELLERvgLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1737198856 153 RLLILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILLV---EQFydfaAELADSYLVMSRGSI 212
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVthdPEL----AEYADRIIELRDGKI 218
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-210 |
3.13e-34 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 122.89 E-value: 3.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYY----GGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSIThsKPHQRvqs 76
Cdd:COG1116 7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT--GPGPD--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 77 gVAYVPQGREIFPRLTVEENLLMGL--SRFSAGNARSVPEEIWQLfpV-LKEMKHRRGGDLSGGQQQQLAIGRALASRPR 153
Cdd:COG1116 82 -RGVVFQEPALLPWLTVLDNVALGLelRGVPKAERRERARELLEL--VgLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 154 LLILDEP-------T-EGIQpsvikeigQVIRSLANRGDMAILLV-----EqfydfAAELADSYLVMSRG 210
Cdd:COG1116 159 VLLMDEPfgaldalTrERLQ--------DELLRLWQETGKTVLFVthdvdE-----AVFLADRVVVLSAR 215
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-160 |
2.16e-33 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 122.87 E-value: 2.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRvqsGVAY 80
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDR---NIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 81 VPQGREIFPRLTVEENLLMGLSrfsagnARSVPE-----------EIWQLFPVLkemkHRRGGDLSGGQQQQLAIGRALA 149
Cdd:COG3839 80 VFQSYALYPHMTVYENIAFPLK------LRKVPKaeidrrvreaaELLGLEDLL----DRKPKQLSGGQRQRVALGRALV 149
|
170
....*....|.
gi 1737198856 150 SRPRLLILDEP 160
Cdd:COG3839 150 REPKVFLLDEP 160
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-225 |
2.32e-33 |
|
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: 126.03 E-value: 2.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELN-QYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRvQSGVAY 80
Cdd:COG4988 337 IELEDVSfSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW-RRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 81 VPQGREIFPrLTVEENLLMGLSRFSagnarsvPEEIWQ------LFPVLKEMKH-------RRGGDLSGGQQQQLAIGRA 147
Cdd:COG4988 416 VPQNPYLFA-GTIRENLRLGRPDAS-------DEELEAaleaagLDEFVAALPDgldtplgEGGRGLSGGQAQRLALARA 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1737198856 148 LASRPRLLILDEPTEGIQPSVIKEIGQVIRSLAnRGDMAILLVEQFYDfaAELADSYLVMSRGSIVQQGRGEN-MEQEG 225
Cdd:COG4988 488 LLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLAL--LAQADRILVLDDGRIVEQGTHEElLAKNG 563
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-216 |
4.76e-33 |
|
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: 119.31 E-value: 4.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQR--VQSGV 78
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELyeLRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 79 AYVPQGREIFPRLTVEENLLMGLSRFSAGNarsvPEEIWQLfpV--------LKEMKHRRGGDLSGGQQQQLAIGRALAS 150
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVAFPLREHTDLS----EAEIREL--VleklelvgLPGAADKMPSELSGGMRKRVALARALAL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1737198856 151 RPRLLILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:COG1127 159 DPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEG 224
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-215 |
3.26e-32 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 116.80 E-value: 3.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGS----HILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSIThskphqRVQSG 77
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT------GPGPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 78 VAYVPQGREIFPRLTVEENLLMGLS--RFSAGNARSVPEEIWQLFPvLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLL 155
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALGLElqGVPKAEARERAEELLELVG-LSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1737198856 156 ILDEP-------TEGiqpsvikEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSR--GSIVQQ 215
Cdd:cd03293 154 LLDEPfsaldalTRE-------QLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAE 215
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-219 |
4.06e-32 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 117.40 E-value: 4.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQSGVAY 80
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 81 VPQGREIFPRLTVEENLLMGLSRFSAGNA-----------RSVPEEI-----WQLFPVLKEMKHRRGGDLSGGQQQQLAI 144
Cdd:PRK11300 85 TFQHVRLFREMTVIENLLVAQHQQLKTGLfsgllktpafrRAESEALdraatWLERVGLLEHANRQAGNLAYGQQRRLEI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1737198856 145 GRALASRPRLLILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQGRGE 219
Cdd:PRK11300 165 ARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPE 239
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-188 |
1.45e-31 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 114.59 E-value: 1.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRvqsgVAY 80
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEA----CHY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 81 VPQGREIFPRLTVEENLLMgLSRFSAGNARSVPE--EIWQLFPVLkemkHRRGGDLSGGQQQQLAIGRALASRPRLLILD 158
Cdd:PRK13539 78 LGHRNAMKPALTVAENLEF-WAAFLGGEELDIAAalEAVGLAPLA----HLPFGYLSAGQKRRVALARLLVSNRPIWILD 152
|
170 180 190
....*....|....*....|....*....|
gi 1737198856 159 EPTEGIQPSVIKEIGQVIRSLANRGDMAIL 188
Cdd:PRK13539 153 EPTAALDAAAVALFAELIRAHLAQGGIVIA 182
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-216 |
2.55e-31 |
|
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: 114.21 E-value: 2.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGSHILRGVSFEAVVGeVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKphQRVQSGVAYV 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP--QKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 82 PQGREIFPRLTVEENL--LMGLSRFSAGNARSVPEEIWQLFPvLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDE 159
Cdd:cd03264 78 PQEFGVYPNFTVREFLdyIAWLKGIPSKEVKARVDEVLELVN-LGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1737198856 160 PTEGIQP-------SVIKEIGqvirslANRgdMAIL---LVEQFYDFAAELAdsylVMSRGSIVQQG 216
Cdd:cd03264 157 PTAGLDPeerirfrNLLSELG------EDR--IVILsthIVEDVESLCNQVA----VLNKGKLVFEG 211
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-216 |
3.40e-31 |
|
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: 114.29 E-value: 3.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 16 ILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKG---GEVVWQGKSithSKPHQrVQSGVAYVPQGREIFPRLT 92
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQP---RKPDQ-FQKCVAYVRQDDILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 93 VEENLL-MGLSRFSAGNARSVPEEIWQlFPVLKEMKHRRGGD-----LSGGQQQQLAIGRALASRPRLLILDEPTEGIQP 166
Cdd:cd03234 98 VRETLTyTAILRLPRKSSDAIRKKRVE-DVLLRDLALTRIGGnlvkgISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1737198856 167 SVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:cd03234 177 FTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-217 |
5.42e-31 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 116.47 E-value: 5.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQSGVayV 81
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGV--V 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 82 PQGREIFPRLTVEENLLMgLSRFSAGNARSVPEEIWQL--FPVLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDE 159
Cdd:PRK13536 120 PQFDNLDLEFTVRENLLV-FGRYFGMSTREIEAVIPSLleFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDE 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1737198856 160 PTEGIQPSVIKEIGQVIRSLANRGdMAILLVEQFYDFAAELADSYLVMSRGSIVQQGR 217
Cdd:PRK13536 199 PTTGLDPHARHLIWERLRSLLARG-KTILLTTHFMEEAERLCDRLCVLEAGRKIAEGR 255
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-216 |
5.69e-31 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 115.67 E-value: 5.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQSGVayV 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGV--V 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 82 PQGREIFPRLTVEENLLMgLSRF---SAGNARSVPEEIWQlFPVLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILD 158
Cdd:PRK13537 86 PQFDNLDPDFTVRENLLV-FGRYfglSAAAARALVPPLLE-FAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1737198856 159 EPTEGIQPSVIKEIGQVIRSLANRGDmAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:PRK13537 164 EPTTGLDPQARHLMWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVIEEGRKIAEG 220
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-216 |
9.35e-31 |
|
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: 112.73 E-value: 9.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRvqsGVAYV 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDR---DIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 82 PQGREIFPRLTVEENLLMGLSRfsagnaRSVPE-----------EIWQLFPVLkemkHRRGGDLSGGQQQQLAIGRALAS 150
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLKL------RKVPKdeidervrevaELLQIEHLL----DRKPKQLSGGQRQRVALGRAIVR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1737198856 151 RPRLLILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:cd03301 148 EPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
2-221 |
9.78e-31 |
|
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: 113.54 E-value: 9.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCL--MG-LIPVK--GGEVVWQGKSITHSK---PHQR 73
Cdd:TIGR00972 2 IEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLnrMNdLVPGVriEGKVLFDGQDIYDKKidvVELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 74 VQSGVayVPQGREIFPrLTVEENLLMGLsRFSAGNARSVPEEIWQ-------LFPVLKEMKHRRGGDLSGGQQQQLAIGR 146
Cdd:TIGR00972 82 RRVGM--VFQKPNPFP-MSIYDNIAYGP-RLHGIKDKKELDEIVEeslkkaaLWDEVKDRLHDSALGLSGGQQQRLCIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1737198856 147 ALASRPRLLILDEPTEGIQPSVIKEIGQVIRSLanRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQGRGENM 221
Cdd:TIGR00972 158 ALAVEPEVLLLDEPTSALDPIATGKIEELIQEL--KKKYTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQI 230
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
11-226 |
2.46e-30 |
|
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: 118.01 E-value: 2.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 11 YGGSH--ILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQSgVAYVPQGREIF 88
Cdd:COG2274 483 YPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQ-IGVVLQDVFLF 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 89 PRlTVEENLLMGLSRFSagnarsvPEEIWQ------LFPVLKEMKHR-------RGGDLSGGQQQQLAIGRALASRPRLL 155
Cdd:COG2274 562 SG-TIRENITLGDPDAT-------DEEIIEaarlagLHDFIEALPMGydtvvgeGGSNLSGGQRQRLAIARALLRNPRIL 633
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1737198856 156 ILDEPTEGIQPSVIKEIGQVIRSLAnrGDMAILLVeqfydfA-----AELADSYLVMSRGSIVQQG-RGENMEQEGV 226
Cdd:COG2274 634 ILDEATSALDAETEAIILENLRRLL--KGRTVIII------AhrlstIRLADRIIVLDKGRIVEDGtHEELLARKGL 702
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-219 |
9.36e-30 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 113.78 E-value: 9.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRvqsGVAY 80
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQR---PINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 81 VPQGREIFPRLTVEENLLMGLS--RFSAGNARSVPEEIWQLFPvLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILD 158
Cdd:PRK11607 96 MFQSYALFPHMTVEQNIAFGLKqdKLPKAEIASRVNEMLGLVH-MQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737198856 159 EPTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQGRGE 219
Cdd:PRK11607 175 EPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPE 235
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-216 |
9.49e-30 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 111.40 E-value: 9.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQSgVAY 80
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARR-RAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 81 VPQGREI-FPrLTVEENLLMGLSRFSAGNAR--SVPEEIWQLFPVLkEMKHRRGGDLSGGQQQQLAIGRALA------SR 151
Cdd:PRK13548 81 LPQHSSLsFP-FTVEEVVAMGRAPHGLSRAEddALVAAALAQVDLA-HLAGRDYPQLSGGEQQRVQLARVLAqlwepdGP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1737198856 152 PRLLILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:PRK13548 159 PRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADG 223
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
12-213 |
1.39e-29 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 114.74 E-value: 1.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 12 GGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQSGVAYVP---QGREIF 88
Cdd:COG3845 269 RGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVAYIPedrLGRGLV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 89 PRLTVEENLLMGLSR---FSAGN------ARSVPEEIWQLFPVLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDE 159
Cdd:COG3845 349 PDMSVAENLILGRYRrppFSRGGfldrkaIRAFAEELIEEFDVRTPGPDTPARSLSGGNQQKVILARELSRDPKLLIAAQ 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1737198856 160 PTEGIQPSVIKEIGQVIRSLANRGdMAILLVEQFYDFAAELADSYLVMSRGSIV 213
Cdd:COG3845 429 PTRGLDVGAIEFIHQRLLELRDAG-AAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-217 |
1.45e-29 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 110.23 E-value: 1.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGsHILRgVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRvqsGVAY 80
Cdd:COG3840 1 MLRLDDLTYRYGD-FPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAER---PVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 81 VPQGREIFPRLTVEENLLMGLS---RFSAGNARSVPEEIWQLfpVLKEMKHRRGGDLSGGQQQQLAIGRALA-SRPrLLI 156
Cdd:COG3840 76 LFQENNLFPHLTVAQNIGLGLRpglKLTAEQRAQVEQALERV--GLAGLLDRLPGQLSGGQRQRVALARCLVrKRP-ILL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737198856 157 LDEPTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQGR 217
Cdd:COG3840 153 LDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGP 213
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
2-188 |
2.36e-29 |
|
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: 108.60 E-value: 2.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQrvQSGVAYV 81
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP--HENILYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 82 PQGREIFPRLTVEENLlmglsRFSAGNARSVPEEIWQLFPV--LKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDE 159
Cdd:TIGR01189 79 GHLPGLKPELSALENL-----HFWAAIHGGAQRTIEDALAAvgLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDE 153
|
170 180
....*....|....*....|....*....
gi 1737198856 160 PTEGIQPSVIKEIGQVIRSLANRGDMAIL 188
Cdd:TIGR01189 154 PTTALDKAGVALLAGLLRAHLARGGIVLL 182
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
32-224 |
2.41e-29 |
|
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: 111.82 E-value: 2.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 32 LLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRvqsGVAYVPQGREIFPRLTVEENLLMGLSRFSAGNARS 111
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLR---HINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 112 VPEEIWQLFPV-LKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILLV 190
Cdd:TIGR01187 78 KPRVLEALRLVqLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFV 157
|
170 180 190
....*....|....*....|....*....|....
gi 1737198856 191 EQFYDFAAELADSYLVMSRGSIVQQGRGENMEQE 224
Cdd:TIGR01187 158 THDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEE 191
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-213 |
3.64e-29 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 113.58 E-value: 3.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQSGVAY 80
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALGIGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 81 VPQGREIFPRLTVEENLLMGLsrfsagnarsvpEEIWQLFPVLKEMK----------------HRRGGDLSGGQQQQLAI 144
Cdd:COG3845 85 VHQHFMLVPNLTVAENIVLGL------------EPTKGGRLDRKAARarirelserygldvdpDAKVEDLSVGEQQRVEI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1737198856 145 GRALASRPRLLILDEPTEGIQPSVIKEIGQVIRSLANRGdMAILLV-----EqfydfAAELADSYLVMSRGSIV 213
Cdd:COG3845 153 LKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEG-KSIIFIthklrE-----VMAIADRVTVLRRGKVV 220
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-223 |
4.56e-29 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 108.95 E-value: 4.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSI-----THSKPHQRVQS 76
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsqkPSEKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 77 GVAYVPQGREIFPRLTVEENLL------MGLSRfsaGNARSVPEEIW-QLfpVLKEMKHRRGGDLSGGQQQQLAIGRALA 149
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENLIeapckvLGLSK---EQAREKAMKLLaRL--RLTDKADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1737198856 150 SRPRLLILDEPTEGIQPSVIKEIGQVIRSLANRGDMAIlLVEQFYDFAAELADSYLVMSRGSIVQQGRGENMEQ 223
Cdd:COG4161 158 MEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQV-IVTHEVEFARKVASQVVYMEKGRIIEQGDASHFTQ 230
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
16-216 |
5.66e-29 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 107.64 E-value: 5.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 16 ILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKG--GEVVWQGKSITHSKPHQRVqsgvAYVPQGREIFPRLTV 93
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLDKRSFRKII----GYVPQDDILHPTLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 94 EENLlmglsRFSAgnarsvpeeiwqlfpvlkemkHRRGgdLSGGQQQQLAIGRALASRPRLLILDEPTEGIQPSVIKEIG 173
Cdd:cd03213 100 RETL-----MFAA---------------------KLRG--LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVM 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1737198856 174 QVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:cd03213 152 SLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-223 |
9.77e-29 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 108.18 E-value: 9.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQG-----KSITHSKPHQRVQS 76
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfSKTPSDKAIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 77 GVAYVPQGREIFPRLTVEENLL------MGLSRFSAgNARSvpEEIWQLFPvLKEMKHRRGGDLSGGQQQQLAIGRALAS 150
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLIeapcrvLGLSKDQA-LARA--EKLLERLR-LKPYADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1737198856 151 RPRLLILDEPTEGIQPSVIKEIGQVIRSLANRGdMAILLVEQFYDFAAELADSYLVMSRGSIVQQGRGENMEQ 223
Cdd:PRK11124 159 EPQVLLFDEPTAALDPEITAQIVSIIRELAETG-ITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASCFTQ 230
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-216 |
1.54e-28 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 107.96 E-value: 1.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCL-------MGLIPVKGGEVVWQGKSITHSKPH-- 71
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCInlletpdSGEIRVGGEEIRLKPDRDGELVPAdr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 72 ---QRVQSGVAYVPQGREIFPRLTVEENLL------MGLSRFSA-GNARSVPEEIWqlfpvLKEMKHRRGGDLSGGQQQQ 141
Cdd:COG4598 88 rqlQRIRTRLGMVFQSFNLWSHMTVLENVIeapvhvLGRPKAEAiERAEALLAKVG-----LADKRDAYPAHLSGGQQQR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1737198856 142 LAIGRALASRPRLLILDEPTEGIQPSVIKEIGQVIRSLANRGdMAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:COG4598 163 AAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEG-RTMLVVTHEMGFARDVSSHVVFLHQGRIEEQG 236
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-217 |
2.20e-28 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 107.29 E-value: 2.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQSGVAYV 81
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 82 PQGREIFPRLTVEENLLMGLS---RFSAGNARSVPEEIWQLFPVlKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILD 158
Cdd:PRK10895 84 PQEASIFRRLSVYDNLMAVLQirdDLSAEQREDRANELMEEFHI-EHLRDSMGQSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1737198856 159 EPTEGIQPSVIKEIGQVIRSLANRGdMAILLVEQfydfaaELADSYLVMSRGSIVQQGR 217
Cdd:PRK10895 163 EPFAGVDPISVIDIKRIIEHLRDSG-LGVLITDH------NVRETLAVCERAYIVSQGH 214
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-216 |
3.13e-28 |
|
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: 108.60 E-value: 3.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYY----GGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIP---VKGGEVVWQGKSITHSKPHQR 73
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 74 VQ---SGVAYVPQgrEIF----PRLTVEENLLMGLSRFSAGNARSVPEEIWQLF-----PVLKEMKHRRGGDLSGGQQQQ 141
Cdd:COG0444 81 RKirgREIQMIFQ--DPMtslnPVMTVGDQIAEPLRIHGGLSKAEARERAIELLervglPDPERRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1737198856 142 LAIGRALASRPRLLILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQfyDFA--AELADSYLVMSRGSIVQQG 216
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITH--DLGvvAEIADRVAVMYAGRIVEEG 233
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
16-225 |
3.21e-28 |
|
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: 111.40 E-value: 3.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 16 ILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSkPHQRVQSGVAYVPQGREIFpRLTVEE 95
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDL-DEDDLRRRIAVVPQRPHLF-DTTLRE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 96 NLLMGlsrfsAGNARsvPEEIWQ------LFPVLKEMKHR-------RGGDLSGGQQQQLAIGRALASRPRLLILDEPTE 162
Cdd:COG4987 428 NLRLA-----RPDAT--DEELWAalervgLGDWLAALPDGldtwlgeGGRRLSGGERRRLALARALLRDAPILLLDEPTE 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1737198856 163 GIQPSVIKEIGQVIRSLAnrGDMAILLV---EQfydfAAELADSYLVMSRGSIVQQGRGEN-MEQEG 225
Cdd:COG4987 501 GLDAATEQALLADLLEAL--AGRTVLLIthrLA----GLERMDRILVLEDGRIVEQGTHEElLAQNG 561
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-216 |
3.32e-28 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 107.14 E-value: 3.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKP--HQ-----R 73
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSlsQQkglirQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 74 VQSGVAYVPQGREIFPRLTVEENLLMGLSRFSAGNARSVPEEIWQLFPVL----KEMKHRRggDLSGGQQQQLAIGRALA 149
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVglagKETSYPR--RLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1737198856 150 SRPRLLILDEPTEGIQPSVIKEIGQVIRSLAN-RGDMAILLVEQfyDFAAELADSYLVMSRGSIVQQG 216
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQeKRTMVIVTHEM--SFARDVADRAIFMDQGRIVEQG 226
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
9-221 |
4.64e-28 |
|
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: 106.62 E-value: 4.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 9 QYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPhQRVQSGVAYVPQGREIF 88
Cdd:cd03295 9 RYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDP-VELRRKIGYVIQQIGLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 89 PRLTVEEN--LLMGLSRFSAGNARSVPEEIWQLFPV-LKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEPTEGIQ 165
Cdd:cd03295 88 PHMTVEENiaLVPKLLKWPKEKIRERADELLALVGLdPAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1737198856 166 PSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQGRGENM 221
Cdd:cd03295 168 PITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
11-190 |
5.15e-28 |
|
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: 104.39 E-value: 5.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 11 YGGSH--ILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQSgVAYVPQGREIF 88
Cdd:cd03228 10 YPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN-IAYVPQDPFLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 89 PRlTVEENLLmglsrfsagnarsvpeeiwqlfpvlkemkhrrggdlSGGQQQQLAIGRALASRPRLLILDEPTEGIQPSV 168
Cdd:cd03228 89 SG-TIRENIL------------------------------------SGGQRQRIAIARALLRDPPILILDEATSALDPET 131
|
170 180
....*....|....*....|..
gi 1737198856 169 IKEIGQVIRSLanRGDMAILLV 190
Cdd:cd03228 132 EALILEALRAL--AKGKTVIVI 151
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-216 |
1.19e-27 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 109.76 E-value: 1.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQSGVAY 80
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 81 VPQGREIFPRLTVEENLLMGLSRfSAGNARSVPEEIWQLFPVLKemKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEP 160
Cdd:PRK15439 91 VPQEPLLFPNLSVKENILFGLPK-RQASMQKMKQLLAALGCQLD--LDSSAGSLEVADRQIVEILRGLMRDSRILILDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1737198856 161 TEGIQPSVIKEIGQVIRSLANRGdMAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:PRK15439 168 TASLTPAETERLFSRIRELLAQG-VGIVFISHKLPEIRQLADRISVMRDGTIALSG 222
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-216 |
1.64e-27 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 107.48 E-value: 1.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRvqsGVAYV 81
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDR---KVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 82 PQGREIFPRLTVEENLLMGLS---RFSAGNARSVPEEIWQLFPV--LKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLI 156
Cdd:PRK10851 80 FQHYALFRHMTVFDNIAFGLTvlpRRERPNAAAIKAKVTQLLEMvqLAHLADRYPAQLSGGQKQRVALARALAVEPQILL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 157 LDEPTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:PRK10851 160 LDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAG 219
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-217 |
1.91e-27 |
|
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: 104.59 E-value: 1.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGS----HILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRV-- 74
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 75 QSGVAYVPQGREIFPRLTVEENLLMGLSrfSAGNARS-VPEEIWQLFPV--LKEMKHRRGGDLSGGQQQQLAIGRALASR 151
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLE--IAGVPKAeIEERVLELLELvgLEDKADAYPAQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1737198856 152 PRLLILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQGR 217
Cdd:cd03258 159 PKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGT 224
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
10-217 |
6.01e-27 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 107.94 E-value: 6.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 10 YYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQrVQSGVAYVPQGREIFP 89
Cdd:COG1132 349 YPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLES-LRRQIGVVPQDTFLFS 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 90 RlTVEENLLMGLSRFSagnarsvPEEIW------QLFPVLKEMKH-------RRGGDLSGGQQQQLAIGRALASRPRLLI 156
Cdd:COG1132 428 G-TIRENIRYGRPDAT-------DEEVEeaakaaQAHEFIEALPDgydtvvgERGVNLSGGQRQRIAIARALLKDPPILI 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1737198856 157 LDEPTEGIQPSVIKEIGQVIRSLanRGDMAILLVeqfydfA-----AELADSYLVMSRGSIVQQGR 217
Cdd:COG1132 500 LDEATSALDTETEALIQEALERL--MKGRTTIVI------AhrlstIRNADRILVLDDGRIVEQGT 557
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
10-207 |
9.09e-27 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 107.37 E-value: 9.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 10 YYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRvQSGVAYVPQGREIFP 89
Cdd:TIGR02857 331 YPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW-RDQIAWVPQHPFLFA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 90 RlTVEENLLMGLSRFSAGNARSVPE--EIWQLFPVLKEMKHRRGGD----LSGGQQQQLAIGRALASRPRLLILDEPTEG 163
Cdd:TIGR02857 410 G-TIAENIRLARPDASDAEIREALEraGLDEFVAALPQGLDTPIGEggagLSGGQAQRLALARAFLRDAPLLLLDEPTAH 488
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1737198856 164 IQPSVIKEIGQVIRSLANRgdmAILLVEQFYDFAAELADSYLVM 207
Cdd:TIGR02857 489 LDAETEAEVLEALRALAQG---RTVLLVTHRLALAALADRIVVL 529
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-221 |
1.70e-26 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 102.81 E-value: 1.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCL--MG-LIP---VKgGEVVWQGKSITHSK--PHQr 73
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMNdLIPgarVE-GEILLDGEDIYDPDvdVVE- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 74 VQSGVAYVPQGREIFPrLTVEENLLMGLsRFSAGNARSVPEEI----------WqlfpvlKEMKHR---RGGDLSGGQQQ 140
Cdd:COG1117 90 LRRRVGMVFQKPNPFP-KSIYDNVAYGL-RLHGIKSKSELDEIveeslrkaalW------DEVKDRlkkSALGLSGGQQQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 141 QLAIGRALASRPRLLILDEPTEGIQP-SVIKeIGQVIRSLanRGDMAILLV----EQfydfAAELADSYLVMSRGSIVQQ 215
Cdd:COG1117 162 RLCIARALAVEPEVLLMDEPTSALDPiSTAK-IEELILEL--KKDYTIVIVthnmQQ----AARVSDYTAFFYLGELVEF 234
|
....*.
gi 1737198856 216 GRGENM 221
Cdd:COG1117 235 GPTEQI 240
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
17-216 |
3.18e-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: 102.53 E-value: 3.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 17 LRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHS--KPHQRVQSGVAYVPQgreiFPR---- 90
Cdd:TIGR04521 21 LDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKkkKKLKDLRKKVGLVFQ----FPEhqlf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 91 -LTVEENLLMGLSRF--SAGNARSVPEEIWQLFPVLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEPTEGIQPS 167
Cdd:TIGR04521 97 eETVYKDIAFGPKNLglSEEEAEERVKEALELVGLDEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPK 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1737198856 168 VIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:TIGR04521 177 GRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDG 225
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-216 |
5.17e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 101.53 E-value: 5.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLI-----PVKGGEVVWQGKSITH---SKPHQR 73
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIFKmdvIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 74 VQSgVAYVPQGreiFPRLTVEENLLMG--LSRFsAGNARSVPEEI-WQL--FPVLKEMKHRRG---GDLSGGQQQQLAIG 145
Cdd:PRK14247 84 VQM-VFQIPNP---IPNLSIFENVALGlkLNRL-VKSKKELQERVrWALekAQLWDEVKDRLDapaGKLSGGQQQRLCIA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737198856 146 RALASRPRLLILDEPTEGIQPSVIKEIGQVIRSLanRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLDPENTAKIESLFLEL--KKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWG 227
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-216 |
5.77e-26 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 103.49 E-value: 5.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRvqsGVAYV 81
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENR---HVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 82 PQGREIFPRLTVEENLLMGLSRFSAGNARSVPEEIWQLFPV-LKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEP 160
Cdd:PRK09452 92 FQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVqLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDES 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1737198856 161 TEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:PRK09452 172 LSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDG 227
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-226 |
6.28e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 101.62 E-value: 6.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKP---HQRVQSG 77
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRgllALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 78 VAYVPQGREIFpRLTVEENLLMGLSRFSAGN---ARSVPEEIwqlfpVLKEMKHRRGGD---LSGGQQQQLAIGRALASR 151
Cdd:PRK13638 81 TVFQDPEQQIF-YTDIDSDIAFSLRNLGVPEaeiTRRVDEAL-----TLVDAQHFRHQPiqcLSHGQKKRVAIAGALVLQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 152 PRLLILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFyDFAAELADSYLVMSRGSIVQQG-------RGENMEQE 224
Cdd:PRK13638 155 ARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDI-DLIYEISDAVYVLRQGQILTHGapgevfaCTEAMEQA 233
|
..
gi 1737198856 225 GV 226
Cdd:PRK13638 234 GL 235
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-183 |
7.89e-26 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 100.13 E-value: 7.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGSH-ILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQ----RVQ 75
Cdd:COG2884 1 MIRFENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 76 SGVayVPQGREIFPRLTVEENL-----LMGLSRFSAgnARSVPEEIWQlfpV-LKEMKHRRGGDLSGGQQQQLAIGRALA 149
Cdd:COG2884 81 IGV--VFQDFRLLPDRTVYENValplrVTGKSRKEI--RRRVREVLDL---VgLSDKAKALPHELSGGEQQRVAIARALV 153
|
170 180 190
....*....|....*....|....*....|....
gi 1737198856 150 SRPRLLILDEPTEGIQPSVIKEIGQVIRSLANRG 183
Cdd:COG2884 154 NRPELLLADEPTGNLDPETSWEIMELLEEINRRG 187
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
20-226 |
1.52e-25 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 103.86 E-value: 1.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 20 VSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIP-VKGGEVVWQGKSITHSKPHQRVQSGVAYVPQGRE---IFPRLTVEE 95
Cdd:PRK13549 281 VSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQAIAQGIAMVPEDRKrdgIVPVMGVGK 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 96 NL-LMGLSRFSAGNARSVPEEIWQLFPVLKEMKHR------RGGDLSGGQQQQLAIGRALASRPRLLILDEPTEGIQPSV 168
Cdd:PRK13549 361 NItLAALDRFTGGSRIDDAAELKTILESIQRLKVKtaspelAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGA 440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1737198856 169 IKEIGQVIRSLANRGdMAILLVeqfydfAAEL------ADSYLVMSRGSIVQQGRGENMEQEGV 226
Cdd:PRK13549 441 KYEIYKLINQLVQQG-VAIIVI------SSELpevlglSDRVLVMHEGKLKGDLINHNLTQEQV 497
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-216 |
2.88e-25 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 99.66 E-value: 2.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSIT------------HSK 69
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvaDKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 70 PHQRVQSGVAYVPQGREIFPRLTVEENLL------MGLSRFSAG-------NARSVPEEIWQLFPVlkemkhrrggDLSG 136
Cdd:PRK10619 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVMeapiqvLGLSKQEAReravkylAKVGIDERAQGKYPV----------HLSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 137 GQQQQLAIGRALASRPRLLILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFyDFAAELADSYLVMSRGSIVQQG 216
Cdd:PRK10619 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEM-GFARHVSSHVIFLHQGKIEEEG 234
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-224 |
4.95e-25 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 102.39 E-value: 4.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNqyygGSHIlRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQSGVAYV 81
Cdd:PRK10762 258 LKVDNLS----GPGV-NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIVYI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 82 PQGRE---IFPRLTVEENL-LMGLSRFS--AGNARSVPEEIW-----QLFPVLKEMKHRRGGDLSGGQQQQLAIGRALAS 150
Cdd:PRK10762 333 SEDRKrdgLVLGMSVKENMsLTALRYFSraGGSLKHADEQQAvsdfiRLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMT 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1737198856 151 RPRLLILDEPTEGIQPSVIKEIGQVIRSLANRGdMAILLVEQFYDFAAELADSYLVMSRGSIVQQGRGENMEQE 224
Cdd:PRK10762 413 RPKVLILDEPTRGVDVGAKKEIYQLINQFKAEG-LSIILVSSEMPEVLGMSDRILVMHEGRISGEFTREQATQE 485
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
2-192 |
5.13e-25 |
|
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: 97.56 E-value: 5.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPhqRVQSGVAYV 81
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD--SIARGLLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 82 PQGREIFPRLTVEENLLMglsrFSAGNARsvpEEIWQLFPV--LKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDE 159
Cdd:cd03231 79 GHAPGIKTTLSVLENLRF----WHADHSD---EQVEEALARvgLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDE 151
|
170 180 190
....*....|....*....|....*....|...
gi 1737198856 160 PTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQ 192
Cdd:cd03231 152 PTTALDKAGVARFAEAMAGHCARGGMVVLTTHQ 184
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
10-225 |
9.39e-25 |
|
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: 97.30 E-value: 9.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 10 YYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSItHSKPHQRVQSGVAYVPQGREIFP 89
Cdd:cd03254 12 YDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDI-RDISRKSLRSMIGVVLQDTFLFS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 90 RlTVEENLLMGLSRFS------AGNARSVPEEIWQLFPVLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEPTEG 163
Cdd:cd03254 91 G-TIMENIRLGRPNATdeevieAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSN 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1737198856 164 IQPSVIKEIGQVIRSLaNRGDMAILLveqfydfAAEL-----ADSYLVMSRGSIVQQG-RGENMEQEG 225
Cdd:cd03254 170 IDTETEKLIQEALEKL-MKGRTSIII-------AHRLstiknADKILVLDDGKIIEEGtHDELLAKKG 229
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-224 |
9.67e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 97.99 E-value: 9.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKG-----GEVVWQGKSITHSKPHQ-RVQ 75
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIYSPDVDPiEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 76 SGVAYVPQGREIFPRLTVEENLLMGLSRFSAGNARSVPEEI--WQL--FPVLKEMKHR---RGGDLSGGQQQQLAIGRAL 148
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKKELDERveWALkkAALWDEVKDRlndYPSNLSGGQRQRLVIARAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 149 ASRPRLLILDEPTEGIQPSVIKEIGQVIRSLANrgDMAILLVEQFYDFAAELADSYLVMSRGSIVQQGRG----ENMEQE 224
Cdd:PRK14267 165 AMKPKILLMDEPTANIDPVGTAKIEELLFELKK--EYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTrkvfENPEHE 242
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-210 |
1.64e-24 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 96.77 E-value: 1.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 17 LRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVqsgvayVPQGREIFPRLTVEEN 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV------VFQNYSLLPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 97 LLMGLSR----FSAGNARSVPEEIWQLFPvLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEPTEGIQPSVIKEI 172
Cdd:TIGR01184 75 IALAVDRvlpdLSKSERRAIVEEHIALVG-LTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 1737198856 173 GQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRG 210
Cdd:TIGR01184 154 QEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-161 |
1.93e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 100.52 E-value: 1.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWqGKSIThskphqrvqsgVAY 80
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK-----------IGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 81 VPQGREIF-PRLTVEENLLMGLSRFSAGNARSV-------PEEIWQlfPVlkemkhrrgGDLSGGQQQQLAIGRALASRP 152
Cdd:COG0488 383 FDQHQEELdPDKTVLDELRDGAPGGTEQEVRGYlgrflfsGDDAFK--PV---------GVLSGGEKARLALAKLLLSPP 451
|
....*....
gi 1737198856 153 RLLILDEPT 161
Cdd:COG0488 452 NVLLLDEPT 460
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-190 |
2.07e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 97.41 E-value: 2.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKG-----GEVVWQGKSITHSKPH-QRVQ 75
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERRVNlNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 76 SGVAYVPQGREIFPrLTVEENLLMGLS------RFSAGNARSVPEEIWQLFPVLKEMKHRRGGDLSGGQQQQLAIGRALA 149
Cdd:PRK14258 88 RQVSMVHPKPNLFP-MSVYDNVAYGVKivgwrpKLEIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARALA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1737198856 150 SRPRLLILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILLV 190
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIV 207
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
9-216 |
3.11e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 97.18 E-value: 3.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 9 QYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQ-RVQSGVAYVPQGREI 87
Cdd:PRK13652 12 SYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREvRKFVGLVFQNPDDQI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 88 FPRlTVEENLLMG---LSRFSAGNARSVPEEIWQLFpvLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEPTEGI 164
Cdd:PRK13652 92 FSP-TVEQDIAFGpinLGLDEETVAHRVSSALHMLG--LEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1737198856 165 QPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:PRK13652 169 DPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYG 220
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-216 |
4.15e-24 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 96.53 E-value: 4.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKS------ITHSKPHQR- 73
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrdlYALSEAERRr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 74 -VQSGVAYVPQGREIFPRLTVEE--NL---LMGLSRFSAGNARSVPEEiWqLFPVlkEMKHRRGGDL----SGGQQQQLA 143
Cdd:PRK11701 86 lLRTEWGFVHQHPRDGLRMQVSAggNIgerLMAVGARHYGDIRATAGD-W-LERV--EIDAARIDDLpttfSGGMQQRLQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1737198856 144 IGRALASRPRLLILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:PRK11701 162 IARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
14-220 |
4.33e-24 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 99.74 E-value: 4.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 14 SHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIP---VKGGEVVWQGKSITHSKPHQRvqsgVAYVPQGREIFPR 90
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLNGMPIDAKEMRAI----SAYVQQDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 91 LTVEENlLMGLSRFSAGNARSVPEEIWQLFPVLKEM-----KHRRGGD------LSGGQQQQLAIGRALASRPRLLILDE 159
Cdd:TIGR00955 114 LTVREH-LMFQAHLRMPRRVTKKEKRERVDEVLQALglrkcANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737198856 160 PTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQGRGEN 220
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQ 253
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-221 |
4.67e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 96.38 E-value: 4.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCL--MG-LIP--VKGGEVVWQGKSItHSKPHQRVQ 75
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNdLNPevTITGSIVYNGHNI-YSPRTDTVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 76 --SGVAYVPQGREIFPrLTVEENLLMGLsRFSAGNARSVPEE----------IWQlfpVLKEMKHRRGGDLSGGQQQQLA 143
Cdd:PRK14239 84 lrKEIGMVFQQPNPFP-MSIYENVVYGL-RLKGIKDKQVLDEavekslkgasIWD---EVKDRLHDSALGLSGGQQQRVC 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1737198856 144 IGRALASRPRLLILDEPTEGIQPSVIKEIGQVIRSLanRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQGRGENM 221
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLGL--KDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
10-172 |
6.25e-24 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 99.36 E-value: 6.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 10 YYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSItHSKPHQRVQSGVAYVPQGREIFP 89
Cdd:TIGR02868 344 YPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPV-SSLDQDEVRRRVSVCAQDAHLFD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 90 RlTVEENLlmglsRFSAGNArsVPEEIW------QLFPVLKEMK-------HRRGGDLSGGQQQQLAIGRALASRPRLLI 156
Cdd:TIGR02868 423 T-TVRENL-----RLARPDA--TDEELWaalervGLADWLRALPdgldtvlGEGGARLSGGERQRLALARALLADAPILL 494
|
170
....*....|....*.
gi 1737198856 157 LDEPTEGIQPSVIKEI 172
Cdd:TIGR02868 495 LDEPTEHLDAETADEL 510
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
18-221 |
8.57e-24 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 98.58 E-value: 8.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 18 RGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQSGVAYVPQGRE---IFPRLTVE 94
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVYLPEDRQssgLYLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 95 EN---LLMGLSRF--SAGNARSVPEEIWQLFPVLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEPTEGIQPSVI 169
Cdd:PRK15439 360 WNvcaLTHNRRGFwiKPARENAVLERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSAR 439
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1737198856 170 KEIGQVIRSLANRGdMAILLVEQFYDFAAELADSYLVMSRGSIVQQGRGENM 221
Cdd:PRK15439 440 NDIYQLIRSIAAQN-VAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAI 490
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
18-214 |
1.27e-23 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 98.32 E-value: 1.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 18 RGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQSGVAYVPQGRE---IFPRLTVE 94
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYITESRRdngFFPNFSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 95 ENL-------------LMGLsrFSAGNARSVPEEIWQLFPVLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEPT 161
Cdd:PRK09700 360 QNMaisrslkdggykgAMGL--FHEVDEQRTAENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPT 437
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1737198856 162 EGIQPSVIKEIGQVIRSLANRGdMAILLVEQFYDFAAELADSYLVMSRGSIVQ 214
Cdd:PRK09700 438 RGIDVGAKAEIYKVMRQLADDG-KVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-228 |
1.34e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 95.68 E-value: 1.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYG-GSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKP---HQRVQS 76
Cdd:PRK13636 5 ILKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKglmKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 77 GVAYVPQGREIFPRlTVEENLlmglsRFSAGNARSVPEEIWQLFPVLKE------MKHRRGGDLSGGQQQQLAIGRALAS 150
Cdd:PRK13636 85 GMVFQDPDNQLFSA-SVYQDV-----SFGAVNLKLPEDEVRKRVDNALKrtgiehLKDKPTHCLSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 151 RPRLLILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQGRGENM--EQEGVRG 228
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVfaEKEMLRK 238
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-219 |
1.79e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 97.22 E-value: 1.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSItHSKPHQRVQSGVAY 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDV-EALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 81 VPQGREIFPRLTVEENLLMG----LSRFSA---GNARSVPEEIWQLfpVLKEMKHRRGGDLSGGQQQQLAIGRALASRPR 153
Cdd:PRK09536 82 VPQDTSLSFEFDVRQVVEMGrtphRSRFDTwteTDRAAVERAMERT--GVAQFADRPVTSLSGGERQRVLLARALAQATP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1737198856 154 LLILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFyDFAAELADSYLVMSRGSIVQQGRGE 219
Cdd:PRK09536 160 VLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDL-DLAARYCDELVLLADGRVRAAGPPA 224
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
11-183 |
2.25e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 92.68 E-value: 2.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 11 YGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVvwqgksitHSKPHQRVqsgvAYVPQGREI--- 87
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV--------RRAGGARV----AYVPQRSEVpds 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 88 FPrLTVEENLLMG-------LSRFSAGNARSVPEEIWQLfpVLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEP 160
Cdd:NF040873 70 LP-LTVRDLVAMGrwarrglWRRLTRDDRAAVDDALERV--GLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEP 146
|
170 180
....*....|....*....|...
gi 1737198856 161 TEGIQPSVIKEIGQVIRSLANRG 183
Cdd:NF040873 147 TTGLDAESRERIIALLAEEHARG 169
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-217 |
2.66e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 94.67 E-value: 2.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGSH--ILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSIT-HSKPHQRVQSG 77
Cdd:PRK13632 7 MIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISkENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 78 VAYV-PQGReiFPRLTVEENLLMGLSrfsagNARSVPEEIWQlfpVLKEMKHRRGGD---------LSGGQQQQLAIGRA 147
Cdd:PRK13632 87 IIFQnPDNQ--FIGATVEDDIAFGLE-----NKKVPPKKMKD---IIDDLAKKVGMEdyldkepqnLSGGQKQRVAIASV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 148 LASRPRLLILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDfAAELADSYLVMSRGSIVQQGR 217
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMD-EAILADKVIVFSEGKLIAQGK 225
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-160 |
4.08e-23 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 93.77 E-value: 4.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGS----HILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVqs 76
Cdd:COG4525 3 MLTVRHVSVRYPGGgqpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRGV-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 77 gvayVPQGREIFPRLTVEENLLMGLsRF---SAGNARSVPEEIWQLfpV-LKEMKHRRGGDLSGGQQQQLAIGRALASRP 152
Cdd:COG4525 81 ----VFQKDALLPWLNVLDNVAFGL-RLrgvPKAERRARAEELLAL--VgLADFARRRIWQLSGGMRQRVGIARALAADP 153
|
....*...
gi 1737198856 153 RLLILDEP 160
Cdd:COG4525 154 RFLLMDEP 161
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-161 |
5.77e-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: 92.88 E-value: 5.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGS----HILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQ- 75
Cdd:COG4181 8 IIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 76 --SGVAYVPQGREIFPRLTVEENLLMGLSRFSAGNARSVPEEIwqlfpvLKEM--KHRRG---GDLSGGQQQQLAIGRAL 148
Cdd:COG4181 88 raRHVGFVFQSFQLLPTLTALENVMLPLELAGRRDARARARAL------LERVglGHRLDhypAQLSGGEQQRVALARAF 161
|
170
....*....|...
gi 1737198856 149 ASRPRLLILDEPT 161
Cdd:COG4181 162 ATEPAILFADEPT 174
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
27-225 |
7.19e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 93.93 E-value: 7.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 27 GEVTCLLGRNGVGKTTLLRCLMGLI-PVKG----GEVVWQ-GKSITHSKPhqrVQSGVAYVPQgreiFPRL-----TVEE 95
Cdd:PRK13634 33 GSYVAIIGHTGSGKSTLLQHLNGLLqPTSGtvtiGERVITaGKKNKKLKP---LRKKVGIVFQ----FPEHqlfeeTVEK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 96 NLLMGLSRF--SAGNARSVPEEIWQLFPVLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEPTEGIQPSVIKEIG 173
Cdd:PRK13634 106 DICFGPMNFgvSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMM 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1737198856 174 QVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQGRGENMEQEG 225
Cdd:PRK13634 186 EMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
2-216 |
8.46e-23 |
|
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: 91.79 E-value: 8.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGSHILRGVSFEAvvGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRvqsGVAYV 81
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFDLTFAQ--GEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADR---PVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 82 PQGREIFPRLTVEENLLMGLS---RFSAGNARSVPEEIWQLFpvLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILD 158
Cdd:cd03298 76 FQENNLFAHLTVEQNVGLGLSpglKLTAEDRQAIEVALARVG--LAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1737198856 159 EPTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:cd03298 154 EPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-224 |
9.21e-23 |
|
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: 95.66 E-value: 9.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIP--VKGGEVVWQGKSITHSKPHQRVQSGV 78
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 79 AYVPQGREIFPRLTVEENLLMGLSRFSAGNARSVPEEIWQLFPVLKEMK------HRRGGDLSGGQQQQLAIGRALASRP 152
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQldadnvTRPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1737198856 153 RLLILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAeLADSYLVMSRGSIVQQGRGENMEQE 224
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKA-VCDTICVIRDGQHVATKDMSTMSED 231
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-161 |
1.28e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 92.46 E-value: 1.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYG-GS----HILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVq 75
Cdd:COG1101 1 MLELKNLSKTFNpGTvnekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 76 sgvAYVpqGReIF--------PRLTVEENLLMGLSR-----FSAGNARSVPEEIWQLfpvLKEMK----HR---RGGDLS 135
Cdd:COG1101 80 ---KYI--GR-VFqdpmmgtaPSMTIEENLALAYRRgkrrgLRRGLTKKRRELFREL---LATLGlgleNRldtKVGLLS 150
|
170 180
....*....|....*....|....*.
gi 1737198856 136 GGQQQQLAIGRALASRPRLLILDEPT 161
Cdd:COG1101 151 GGQRQALSLLMATLTKPKLLLLDEHT 176
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
3-215 |
1.71e-22 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 92.18 E-value: 1.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 3 QVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQR--VQSGVAY 80
Cdd:TIGR02769 13 RTGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRraFRRDVQL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 81 VPQG--REIFPRLTVEENL---LMGLSRFSAGNARSVPEEIWQLFPVLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLL 155
Cdd:TIGR02769 93 VFQDspSAVNPRMTVRQIIgepLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLI 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 156 ILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQ 215
Cdd:TIGR02769 173 VLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEE 232
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
27-218 |
1.75e-22 |
|
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: 91.08 E-value: 1.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 27 GEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRvqsGVAYVPQGREIFPRLTVEENLLMGLSRFSA 106
Cdd:TIGR01277 24 GEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQR---PVSMLFQENNLFAHLTVRQNIGLGLHPGLK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 107 GNArsvpEEIWQLFPVLKEMK-----HRRGGDLSGGQQQQLAIGRALASRPRLLILDEPTEGIQPSVIKEIGQVIRSLAN 181
Cdd:TIGR01277 101 LNA----EQQEKVVDAAQQVGiadylDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCS 176
|
170 180 190
....*....|....*....|....*....|....*..
gi 1737198856 182 RGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQGRG 218
Cdd:TIGR01277 177 ERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSDC 213
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-216 |
2.18e-22 |
|
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: 95.19 E-value: 2.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYG-GSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQSgVAY 80
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQF-INY 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 81 VPQGREIFPRlTVEENLLMGlsrfsaGNARSVPEEIWQ---LFPVLKEMKH----------RRGGDLSGGQQQQLAIGRA 147
Cdd:TIGR01193 553 LPQEPYIFSG-SILENLLLG------AKENVSQDEIWAaceIAEIKDDIENmplgyqtelsEEGSSISGGQKQRIALARA 625
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1737198856 148 LASRPRLLILDEPTEGIqpSVIKEiGQVIRSLANRGDMAILLVEQFYDFaAELADSYLVMSRGSIVQQG 216
Cdd:TIGR01193 626 LLTDSKVLILDESTSNL--DTITE-KKIVNNLLNLQDKTIIFVAHRLSV-AKQSDKIIVLDHGKIIEQG 690
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-224 |
2.50e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 91.61 E-value: 2.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQSgVAY 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARR-LAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 81 VPQGREIFPRLTVEENLLMGLS-------RFSAGNARSVPEEIWQLFpvLKEMKHRRGGDLSGGQQQQLAIGRALASRPR 153
Cdd:PRK11231 81 LPQHHLTPEGITVRELVAYGRSpwlslwgRLSAEDNARVNQAMEQTR--INHLADRRLTDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1737198856 154 LLILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILLVeqfYDF--AAELADSYLVMSRGSIVQQGR-GENMEQE 224
Cdd:PRK11231 159 VVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVL---HDLnqASRYCDHLVVLANGHVMAQGTpEEVMTPG 229
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-160 |
3.46e-22 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 90.23 E-value: 3.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMG-LIPV--KGGEVVWQGKSITHSKPHQRvqsG 77
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAfsASGEVLLNGRRLTALPAEQR---R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 78 VAYVPQGREIFPRLTVEENLLMGLSRFSAGNARsvPEEIWQlfpVLKE-----MKHRRGGDLSGGQQQQLAIGRALASRP 152
Cdd:COG4136 78 IGILFQDDLLFPHLSVGENLAFALPPTIGRAQR--RARVEQ---ALEEaglagFADRDPATLSGGQRARVALLRALLAEP 152
|
....*...
gi 1737198856 153 RLLILDEP 160
Cdd:COG4136 153 RALLLDEP 160
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
10-216 |
4.08e-22 |
|
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: 90.91 E-value: 4.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 10 YYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIP------------VKGGEVVWQGKS---ITHSKPHQRV 74
Cdd:COG1119 12 RRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPptygndvrlfgeRRGGEDVWELRKrigLVSPALQLRF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 75 QsgvayvpqgreifPRLTVEENLLMGLsrF-SAGNARSVPEEIWQL-FPVLKEM-----KHRRGGDLSGGQQQQLAIGRA 147
Cdd:COG1119 92 P-------------RDETVLDVVLSGF--FdSIGLYREPTDEQRERaRELLELLglahlADRPFGTLSQGEQRRVLIARA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1737198856 148 LASRPRLLILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQfydFAAELADSY---LVMSRGSIVQQG 216
Cdd:COG1119 157 LVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTH---HVEEIPPGIthvLLLKDGRVVAAG 225
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
17-216 |
4.30e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 91.65 E-value: 4.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 17 LRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSK---PHQRVQSGVAYVPQGREIFPRlTV 93
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKvklSDIRKKVGLVFQYPEYQLFEE-TI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 94 EENLLMGLSRFSAGNarsvpEEIWQlfPVLKEM----------KHRRGGDLSGGQQQQLAIGRALASRPRLLILDEPTEG 163
Cdd:PRK13637 102 EKDIAFGPINLGLSE-----EEIEN--RVKRAMnivgldyedyKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1737198856 164 IQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:PRK13637 175 LDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQG 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-161 |
4.98e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.59 E-value: 4.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 4 VSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQgKSIThskphqrvqsgVAYVPQ 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP-KGLR-----------IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 84 GREIFPRLTVEENLLMGLSRFSA------------GNARSVPEEI------------WQL------------FPvlKEMK 127
Cdd:COG0488 69 EPPLDDDLTVLDTVLDGDAELRAleaeleeleaklAEPDEDLERLaelqeefealggWEAearaeeilsglgFP--EEDL 146
|
170 180 190
....*....|....*....|....*....|....
gi 1737198856 128 HRRGGDLSGGQQQQLAIGRALASRPRLLILDEPT 161
Cdd:COG0488 147 DRPVSELSGGWRRRVALARALLSEPDLLLLDEPT 180
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
16-223 |
5.08e-22 |
|
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: 93.66 E-value: 5.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 16 ILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQSgVAYVPQGREIFPRlTVEE 95
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRH-IGYLPQDVELFDG-TIAE 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 96 NLlmglSRFSAGNARSVPE--------EIWQLFP-----VLKEmkhrRGGDLSGGQQQQLAIGRALASRPRLLILDEP-- 160
Cdd:COG4618 425 NI----ARFGDADPEKVVAaaklagvhEMILRLPdgydtRIGE----GGARLSGGQRQRIGLARALYGDPRLVVLDEPns 496
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1737198856 161 ---TEGIQpsvikEIGQVIRSLANRG--------DMAILlveqfydfaaELADSYLVMSRGSIVQQG-RGENMEQ 223
Cdd:COG4618 497 nldDEGEA-----ALAAAIRALKARGatvvvithRPSLL----------AAVDKLLVLRDGRVQAFGpRDEVLAR 556
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-223 |
6.23e-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: 6.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGlIP---VKGGEVVWQGKSITHSKPHQRVQSGV 78
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPkyeVTEGEILFKGEDITDLPPEERARLGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 79 AYVPQGREIFPRLTVEENLlmglsrfsagnaRSVPEeiwqlfpvlkemkhrrggDLSGGQQQQLAIGRALASRPRLLILD 158
Cdd:cd03217 80 FLAFQYPPEIPGVKNADFL------------RYVNE------------------GFSGGEKKRNEILQLLLLEPDLAILD 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1737198856 159 EPTEGIQPSVIKEIGQVIRSLANRGdMAILLV---EQFYDFAAelADSYLVMSRGSIVQQGRGENMEQ 223
Cdd:cd03217 130 EPDSGLDIDALRLVAEVINKLREEG-KSVLIIthyQRLLDYIK--PDRVHVLYDGRIVKSGDKELALE 194
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
17-219 |
6.55e-22 |
|
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: 90.78 E-value: 6.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 17 LRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSIThSKPHQRVQS----GVAYVPQGREIFPRLT 92
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIA-AMSRKELRElrrkKISMVFQSFALLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 93 VEENLLMGLSrfSAGNARSVPEE--IWQLFPV-LKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEPTEGIQPSVI 169
Cdd:cd03294 119 VLENVAFGLE--VQGVPRAEREEraAEALELVgLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIR 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1737198856 170 KEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQGRGE 219
Cdd:cd03294 197 REMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPE 246
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
11-160 |
8.60e-22 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 92.01 E-value: 8.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 11 YGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRvqsGVAYVPQGREIFPR 90
Cdd:PRK11000 13 YGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAER---GVGMVFQSYALYPH 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1737198856 91 LTVEENLLMGLSRFSAGNA---RSVPE--EIWQLFPVLKemkhRRGGDLSGGQQQQLAIGRALASRPRLLILDEP 160
Cdd:PRK11000 90 LSVAENMSFGLKLAGAKKEeinQRVNQvaEVLQLAHLLD----RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
9-183 |
1.89e-21 |
|
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: 88.23 E-value: 1.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 9 QYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSK----PHQRVQSGVAYvpQG 84
Cdd:cd03292 9 TYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraiPYLRRKIGVVF--QD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 85 REIFPRLTVEENLLMGLsRFSAGNARSVPEEIWQLFPV--LKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEPTE 162
Cdd:cd03292 87 FRLLPDRNVYENVAFAL-EVTGVPPREIRKRVPAALELvgLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTG 165
|
170 180
....*....|....*....|.
gi 1737198856 163 GIQPSVIKEIGQVIRSLANRG 183
Cdd:cd03292 166 NLDPDTTWEIMNLLKKINKAG 186
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-226 |
1.94e-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: 92.20 E-value: 1.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 20 VSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVK-GGEVVWQGKSITHSKPHQRVQSGVAYVPQGRE---IFPRLTVEE 95
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKrhgIVPILGVGK 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 96 NL-LMGLSRFSAgnaRSVPEEIWQLFPVLKEMKHRRG---------GDLSGGQQQQLAIGRALASRPRLLILDEPTEGIQ 165
Cdd:TIGR02633 359 NItLSVLKSFCF---KMRIDAAAELQIIGSAIQRLKVktaspflpiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737198856 166 PSVIKEIGQVIRSLANRGdMAILLVEQFYDFAAELADSYLVMSRGSIVQQGRGENMEQEGV 226
Cdd:TIGR02633 436 VGAKYEIYKLINQLAQEG-VAIIVVSSELAEVLGLSDRVLVIGEGKLKGDFVNHALTQEQV 495
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-188 |
3.14e-21 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 87.55 E-value: 3.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKP--HQRV---- 74
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDeyHQDLlylg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 75 -QSGvayvpqgreIFPRLTVEENLlmglsRFSAGNARSV-PEEIWQ-LFPV-LKEMKHRRGGDLSGGQQQQLAIGRALAS 150
Cdd:PRK13538 81 hQPG---------IKTELTALENL-----RFYQRLHGPGdDEALWEaLAQVgLAGFEDVPVRQLSAGQQRRVALARLWLT 146
|
170 180 190
....*....|....*....|....*....|....*...
gi 1737198856 151 RPRLLILDEPTEGIQPSVIKEIGQVIRSLANRGDMAIL 188
Cdd:PRK13538 147 RAPLWILDEPFTAIDKQGVARLEALLAQHAEQGGMVIL 184
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
10-223 |
3.26e-21 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 89.17 E-value: 3.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 10 YYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPhqrvQSGVAYVPQGREI-- 87
Cdd:PRK15056 16 WRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQ----KNLVAYVPQSEEVdw 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 88 -FPRLtVEENLLMG-------LSRFSAGNARSVPEEIWQLfpVLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDE 159
Cdd:PRK15056 92 sFPVL-VEDVVMMGryghmgwLRRAKKRDRQIVTAALARV--DMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 160 PTEGIQPSVIKEIGQVIRSLANRGDmAILLVEQFYDFAAELADsYLVMSRGSIVQQG------RGENMEQ 223
Cdd:PRK15056 169 PFTGVDVKTEARIISLLRELRDEGK-TMLVSTHNLGSVTEFCD-YTVMVKGTVLASGptettfTAENLEL 236
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
17-224 |
4.38e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 88.65 E-value: 4.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 17 LRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITH---SKPHQRVQSGVAYVPQGRE--IFPRl 91
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStskNKDIKQIRKKVGLVFQFPEsqLFEE- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 92 TVEENLLMGLSRF--SAGNARSVPEEIWQLFPVLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEPTEGIQPSVI 169
Cdd:PRK13649 102 TVLKDVAFGPQNFgvSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGR 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1737198856 170 KEIGQVIRSLANRGdMAILLVEQFYDFAAELADSYLVMSRGSIVQQGRGENMEQE 224
Cdd:PRK13649 182 KELMTLFKKLHQSG-MTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-224 |
4.63e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 89.02 E-value: 4.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYG-----GSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLI-PVKG----GEVVWQGKSITHSKP 70
Cdd:PRK13643 1 MIKFEKVNYTYQpnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLqPTEGkvtvGDIVVSSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 71 HQRVQSGVAYVPQGREIFPRlTVEENLLMGLSRF--SAGNARSVPEEIWQLFPVLKEMKHRRGGDLSGGQQQQLAIGRAL 148
Cdd:PRK13643 81 PVRKKVGVVFQFPESQLFEE-TVLKDVAFGPQNFgiPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1737198856 149 ASRPRLLILDEPTEGIQPSVIKEIGQVIRSLANRGDmAILLVEQFYDFAAELADSYLVMSRGSIVQQGRGENMEQE 224
Cdd:PRK13643 160 AMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQ-TVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
16-216 |
5.53e-21 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 86.93 E-value: 5.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 16 ILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKG---GEVVWQGksITHSKPHQRVQSGVAYVPQGREIFPRLT 92
Cdd:cd03233 22 ILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNG--IPYKEFAEKYPGEIIYVSEEDVHFPTLT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 93 VEENLlmglsRFSA---GNARSvpeeiwqlfpvlkemkhrRGgdLSGGQQQQLAIGRALASRPRLLILDEPTEGIQPSVI 169
Cdd:cd03233 100 VRETL-----DFALrckGNEFV------------------RG--ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1737198856 170 KEIGQVIRSLANRGDMAILL-VEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:cd03233 155 LEILKCIRTMADVLKTTTFVsLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
17-216 |
6.37e-21 |
|
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: 90.51 E-value: 6.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 17 LRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPvKGGEVVWQGKSITHSKPHQ------RVQSgvayvpqgreIF-- 88
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRAlrplrrRMQV----------VFqd 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 89 ------PRLTVEENLLMGL-SRFSAGNARSVPEEIWQlfpVLKE------MKHRRGGDLSGGQQQQLAIGRALASRPRLL 155
Cdd:COG4172 371 pfgslsPRMTVGQIIAEGLrVHGPGLSAAERRARVAE---ALEEvgldpaARHRYPHEFSGGQRQRIAIARALILEPKLL 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1737198856 156 ILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILLVEqfYDFA--AELADSYLVMSRGSIVQQG 216
Cdd:COG4172 448 VLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFIS--HDLAvvRALAHRVMVMKDGKVVEQG 508
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
27-216 |
6.53e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 89.39 E-value: 6.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 27 GEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRvqsGVAYVPQGREIFPRLTVEENLLMGLSRFSA 106
Cdd:PRK11432 32 GTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQR---DICMVFQSYALFPHMSLGENVGYGLKMLGV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 107 GNarsvpEEIWQ-----LFPV-LKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEPTEGIQPSVIKEIGQVIRSLA 180
Cdd:PRK11432 109 PK-----EERKQrvkeaLELVdLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQ 183
|
170 180 190
....*....|....*....|....*....|....*...
gi 1737198856 181 NRGDMAILLV--EQFYDFAaeLADSYLVMSRGSIVQQG 216
Cdd:PRK11432 184 QQFNITSLYVthDQSEAFA--VSDTVIVMNKGKIMQIG 219
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
16-226 |
1.32e-20 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 89.78 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 16 ILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKpHQRVQSGVAYVPQGREIFPRlTVEE 95
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYD-HHYLHRQVALVGQEPVLFSG-SVRE 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 96 NLLMGLSRFSAGNARSVPEE------IWQLFPVLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEPTEGIQpsvi 169
Cdd:TIGR00958 574 NIAYGLTDTPDEEIMAAAKAanahdfIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALD---- 649
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1737198856 170 KEIGQVIRSLANRGDMAILLVEQFYDfAAELADSYLVMSRGSIVQQGR-GENMEQEGV 226
Cdd:TIGR00958 650 AECEQLLQESRSRASRTVLLIAHRLS-TVERADQILVLKKGSVVEMGThKQLMEDQGC 706
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-226 |
1.56e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 89.46 E-value: 1.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQSGVAY 80
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 81 VPQGREIFPRLTVEENLLMGlsRFSAGNARSVPEEIWqlfpvlKEMKHRRG----------------GDLSGGQQQQLAI 144
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIG--RHLTKKVCGVNIIDW------REMRVRAAmmllrvglkvdldekvANLSISHKQMLEI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 145 GRALASRPRLLILDEPTEGIQPSVIKEIGQVIRSLANRGDmAILLVEQFYDFAAELADSYLVMSRGSIVQQGRGENMEQE 224
Cdd:PRK09700 157 AKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGT-AIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSND 235
|
..
gi 1737198856 225 GV 226
Cdd:PRK09700 236 DI 237
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-183 |
2.14e-20 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 88.91 E-value: 2.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQSGVAY 80
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGIGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 81 VPQGREIFPRLTVEENLLMG---LSRFSAGNARSVPEEIWQLFPVL--KEMKHRRGGDLSGGQQQQLAIGRALASRPRLL 155
Cdd:PRK10762 84 IHQELNLIPQLTIAENIFLGrefVNRFGRIDWKKMYAEADKLLARLnlRFSSDKLVGELSIGEQQMVEIAKVLSFESKVI 163
|
170 180
....*....|....*....|....*...
gi 1737198856 156 ILDEPTEGIQPSVIKEIGQVIRSLANRG 183
Cdd:PRK10762 164 IMDEPTDALTDTETESLFRVIRELKSQG 191
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
13-225 |
2.67e-20 |
|
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: 86.00 E-value: 2.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 13 GSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSI-THSKPHQRVQSGVayVPQGREIFPRl 91
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLaLADPAWLRRQVGV--VLQENVLFNR- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 92 TVEENLLM---GLSR---FSAGNARSVPEEIWQLFPVLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEPTEGIQ 165
Cdd:cd03252 91 SIRDNIALadpGMSMervIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 166 PSVIKEIGQVIRSLAnRGDMAILLVEQFYdfAAELADSYLVMSRGSIVQQGRGENMEQEG 225
Cdd:cd03252 171 YESEHAIMRNMHDIC-AGRTVIIIAHRLS--TVKNADRIIVMEKGRIVEQGSHDELLAEN 227
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-213 |
3.53e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 88.43 E-value: 3.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 20 VSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQSGVAYVPQGRE---IFPRLTVEEN 96
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMLCPEDRKaegIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 97 LLMGLSRFSAgNARSVPEEIW-----QLFPVLKEMKHRRG----GDLSGGQQQQLAIGRALASRPRLLILDEPTEGIQPS 167
Cdd:PRK11288 352 INISARRHHL-RAGCLINNRWeaenaDRFIRSLNIKTPSReqliMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVG 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1737198856 168 VIKEIGQVIRSLANRGdMAILLVeqfydfAAEL------ADSYLVMSRGSIV 213
Cdd:PRK11288 431 AKHEIYNVIYELAAQG-VAVLFV------SSDLpevlgvADRIVVMREGRIA 475
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-216 |
4.01e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 86.28 E-value: 4.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELN-QYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKP---HQRVQS 76
Cdd:PRK13639 1 ILETRDLKySYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKsllEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 77 GVAYVPQGREIFPRlTVEEN-----LLMGLSRfsagnarsvpEEIWQLfpvLKEMKHRRGGD---------LSGGQQQQL 142
Cdd:PRK13639 81 GIVFQNPDDQLFAP-TVEEDvafgpLNLGLSK----------EEVEKR---VKEALKAVGMEgfenkpphhLSGGQKKRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1737198856 143 AIGRALASRPRLLILDEPTEGIQPSVIKEIGQVIRSLaNRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:PRK13639 147 AIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDL-NKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEG 219
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
21-216 |
4.39e-20 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 85.02 E-value: 4.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 21 SFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRvqsGVAYVPQGREIFPRLTVEENLLMG 100
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRR---PVSMLFQENNLFSHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 101 LS---RFSAGNARSVPEEIWQLFpvLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEPTEGIQPSVIKEIGQVIR 177
Cdd:PRK10771 96 LNpglKLNAAQREKLHAIARQMG--IEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVS 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 1737198856 178 SLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:PRK10771 174 QVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDG 212
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
14-161 |
4.77e-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: 84.83 E-value: 4.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 14 SHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKpHQRVQSGVAYVPQGREIFPRlTV 93
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYE-HKYLHSKVSLVGQEPVLFAR-SL 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1737198856 94 EENLLMGLSRFSAGNARSVPEEiWQLFPVLKEMKH-------RRGGDLSGGQQQQLAIGRALASRPRLLILDEPT 161
Cdd:cd03248 105 QDNIAYGLQSCSFECVKEAAQK-AHAHSFISELASgydtevgEKGSQLSGGQKQRVAIARALIRNPQVLILDEAT 178
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
9-221 |
4.77e-20 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 86.30 E-value: 4.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 9 QYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQ-RVQSGvaYVPQGREI 87
Cdd:COG1125 10 RYPDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElRRRIG--YVIQQIGL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 88 FPRLTVEEN-----LLMGLSRfSAGNARsVPE--EIWQLFPvlKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEP 160
Cdd:COG1125 88 FPHMTVAENiatvpRLLGWDK-ERIRAR-VDEllELVGLDP--EEYRDRYPHELSGGQQQRVGVARALAADPPILLMDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737198856 161 TEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQGRGENM 221
Cdd:COG1125 164 FGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEI 224
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-216 |
5.27e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 85.94 E-value: 5.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYY-GGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSItHSKPHQRVQSGVAY 80
Cdd:PRK13647 5 IEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREV-NAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 81 VPQG--REIFPrLTVEENLlmglsRFSAGNARSVPEEIWQ-----LFPV-LKEMKHRRGGDLSGGQQQQLAIGRALASRP 152
Cdd:PRK13647 84 VFQDpdDQVFS-STVWDDV-----AFGPVNMGLDKDEVERrveeaLKAVrMWDFRDKPPYHLSYGQKKRVAIAGVLAMDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1737198856 153 RLLILDEPTEGIQPSVIKEIGQVIRSLANRGDmAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:PRK13647 158 DVIVLDEPMAYLDPRGQETLMEILDRLHNQGK-TVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
17-216 |
5.62e-20 |
|
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: 84.56 E-value: 5.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 17 LRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPhQRVQSGVAYVPQGREIFPRlTVEEN 96
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDP-ADLRRNIGYVPQDVTLFYG-TLRDN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 97 LLM-----------------GLSRFSAGNARSVPEEIWQlfpvlkemkhrRGGDLSGGQQQQLAIGRALASRPRLLILDE 159
Cdd:cd03245 98 ITLgapladderilraaelaGVTDFVNKHPNGLDLQIGE-----------RGRGLSGGQRQAVALARALLNDPPILLLDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1737198856 160 PTEGIQPSVIKEIGQVIRSLAnrGDMAILLVEQFYDFaAELADSYLVMSRGSIVQQG 216
Cdd:cd03245 167 PTSAMDMNSEERLKERLRQLL--GDKTLIIITHRPSL-LDLVDRIIVMDSGRIVADG 220
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-160 |
6.88e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 85.14 E-value: 6.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVqsgvay 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGV------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 81 VPQGREIFPRLTVEENLLMGLSRfsAGNARSVPEEIWQ--LFPV-LKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLIL 157
Cdd:PRK11248 75 VFQNEGLLPWRNVQDNVAFGLQL--AGVEKMQRLEIAHqmLKKVgLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
...
gi 1737198856 158 DEP 160
Cdd:PRK11248 153 DEP 155
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
28-216 |
7.06e-20 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 88.15 E-value: 7.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 28 EVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKphQRVQSGVAYVPQGREIFPRLTVEENLLMglsrFSAG 107
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNL--DAVRQSLGMCPQHNILFHHLTVAEHILF----YAQL 1030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 108 NARSVPEEIWQLFPVLKE--MKHRR---GGDLSGGQQQQLAIGRALASRPRLLILDEPTEGIQPSVIKEIGQVIrsLANR 182
Cdd:TIGR01257 1031 KGRSWEEAQLEMEAMLEDtgLHHKRneeAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYR 1108
|
170 180 190
....*....|....*....|....*....|....
gi 1737198856 183 GDMAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:TIGR01257 1109 SGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-216 |
7.15e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 85.10 E-value: 7.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQS---- 76
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDAiklr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 77 -GVAYVPQGREIFPRLTVEENLLMGLSRFSAGNARSVP---EEIWQLFPVLKEMKHR---RGGDLSGGQQQQLAIGRALA 149
Cdd:PRK14246 90 kEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKREIKkivEECLRKVGLWKEVYDRlnsPASQLSGGQQQRLTIARALA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1737198856 150 SRPRLLILDEPTEGIQPSVIKEIGQVIRSLANrgDMAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:PRK14246 170 LKPKVLLMDEPTSMIDIVNSQAIEKLITELKN--EIAIVIVSHNPQQVARVADYVAFLYNGELVEWG 234
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-221 |
7.28e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 85.53 E-value: 7.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 11 YGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGL-IPVKG----GEVVWQGKSITHSKPHQRVQSGVAYVPQGR 85
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMnDKVSGyrysGDVLLGGRSIFNYRDVLEFRRRVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 86 EIFPrLTVEENLLMGLSRFS-------AGNARSVPEEIwQLFPVLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILD 158
Cdd:PRK14271 111 NPFP-MSIMDNVLAGVRAHKlvprkefRGVAQARLTEV-GLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1737198856 159 EPTEGIQPSVIKEIGQVIRSLANRgdMAILLVEQFYDFAAELADSYLVMSRGSIVQQGRGENM 221
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-217 |
7.43e-20 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 86.29 E-value: 7.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGS----HILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQ--RV 74
Cdd:COG1135 1 MIELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElrAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 75 QSGVAYVPQGREIFPRLTVEENL-----LMGLSRfSAGNARsVpEEIWQLfpV-LKEMKHRRGGDLSGGQQQQLAIGRAL 148
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENValpleIAGVPK-AEIRKR-V-AELLEL--VgLSDKADAYPSQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1737198856 149 ASRPRLLILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQGR 217
Cdd:COG1135 156 ANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGP 224
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-214 |
9.87e-20 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 85.12 E-value: 9.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGS---------HILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPH 71
Cdd:PRK10419 3 LLNVSGLSHHYAHGglsgkhqhqTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 72 QR--VQSGVAYVPQGR--EIFPRLTVEENL------LMGLSRfsAGNARSVpEEIWQLFPVLKEMKHRRGGDLSGGQQQQ 141
Cdd:PRK10419 83 QRkaFRRDIQMVFQDSisAVNPRKTVREIIreplrhLLSLDK--AERLARA-SEMLRAVDLDDSVLDKRPPQLSGGQLQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 142 LAIGRALASRPRLLILDEPTEGIQPSVIKEIGQVIRSLANRGDMAIL-------LVEQFydfaaelADSYLVMSRGSIVQ 214
Cdd:PRK10419 160 VCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLfithdlrLVERF-------CQRVMVMDNGQIVE 232
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-161 |
1.13e-19 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 85.55 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGS-----------HILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKP 70
Cdd:COG4608 8 LEVRDLKKHFPVRgglfgrtvgvvKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 71 HQ------RVQSgvayvpqgreIF--------PRLTVEENLLMGLSRFSAGNARSVPEEIWQLFPV--LK-EMKHRRGGD 133
Cdd:COG4608 88 RElrplrrRMQM----------VFqdpyaslnPRMTVGDIIAEPLRIHGLASKAERRERVAELLELvgLRpEHADRYPHE 157
|
170 180
....*....|....*....|....*...
gi 1737198856 134 LSGGQQQQLAIGRALASRPRLLILDEPT 161
Cdd:COG4608 158 FSGGQRQRIGIARALALNPKLIVCDEPV 185
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-183 |
1.35e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 86.52 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVK--GGEVVWQGKSITHSKPHQRVQSGV 78
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQASNIRDTERAGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 79 AYVPQGREIFPRLTVEENLLMG--LSRFSAGNARSVPEEIWQLfpvLKEMK-----HRRGGDLSGGQQQQLAIGRALASR 151
Cdd:PRK13549 85 AIIHQELALVKELSVLENIFLGneITPGGIMDYDAMYLRAQKL---LAQLKldinpATPVGNLGLGQQQLVEIAKALNKQ 161
|
170 180 190
....*....|....*....|....*....|..
gi 1737198856 152 PRLLILDEPTEGIQPSVIKEIGQVIRSLANRG 183
Cdd:PRK13549 162 ARLLILDEPTASLTESETAVLLDIIRDLKAHG 193
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
16-216 |
1.38e-19 |
|
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: 83.70 E-value: 1.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 16 ILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSkPHQRVQSGVAYVPQGREIFPRlTVEE 95
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKI-GLHDLRSRISIIPQDPVLFSG-TIRS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 96 NLlMGLSRFSagnarsvPEEIWQ------------LFPVLKEMKHRRGGD-LSGGQQQQLAIGRALASRPRLLILDEPTE 162
Cdd:cd03244 97 NL-DPFGEYS-------DEELWQalervglkefveSLPGGLDTVVEEGGEnLSVGQRQLLCLARALLRKSKILVLDEATA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1737198856 163 GIQPSVIKEIGQVIRSlaNRGDMAILLV----EQFYDFaaelaDSYLVMSRGSIVQQG 216
Cdd:cd03244 169 SVDPETDALIQKTIRE--AFKDCTVLTIahrlDTIIDS-----DRILVLDKGRVVEFD 219
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-210 |
2.26e-19 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 85.94 E-value: 2.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 17 LRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQSGVAYVPQGRE---IFPRLTV 93
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHGFALVTEERRstgIYAYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 94 EENLL----------MGLsrfsAGNARSVPEEIWqlfpVLKEMK-----HRRG-GDLSGGQQQQLAIGRALASRPRLLIL 157
Cdd:PRK10982 344 GFNSLisnirnyknkVGL----LDNSRMKSDTQW----VIDSMRvktpgHRTQiGSLSGGNQQKVIIGRWLLTQPEILML 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1737198856 158 DEPTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAeLADSYLVMSRG 210
Cdd:PRK10982 416 DEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLG-ITDRILVMSNG 467
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
16-216 |
2.54e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 83.19 E-value: 2.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 16 ILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGlIP---VKGGEVVWQGKSITHSKPHQRVQSGVAYVPQGREIFPRLT 92
Cdd:COG0396 15 ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMG-HPkyeVTSGSILLDGEDILELSPDERARAGIFLAFQYPVEIPGVS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 93 VEeNLLMglsrfSAGNARSVPEEIWQLFpvLKEMKH------------RRG--GDLSGGQQQQLAIGRALASRPRLLILD 158
Cdd:COG0396 94 VS-NFLR-----TALNARRGEELSAREF--LKLLKEkmkelgldedflDRYvnEGFSGGEKKRNEILQMLLLEPKLAILD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737198856 159 EPTEGIQPSVIKEIGQVIRSLANRgDMAILLV---EQFYDFAAelADSYLVMSRGSIVQQG 216
Cdd:COG0396 166 ETDSGLDIDALRIVAEGVNKLRSP-DRGILIIthyQRILDYIK--PDFVHVLVDGRIVKSG 223
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-211 |
2.71e-19 |
|
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: 82.87 E-value: 2.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSEL-------NQyyGGSHI--LRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMG---------LIPVKGGEVvwqg 62
Cdd:COG4778 4 LLEVENLsktftlhLQ--GGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGnylpdsgsiLVRHDGGWV---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 63 kSITHSKPHQRV---QSGVAYVPQGREIFPRLT----VEENLL-MGLSRFSA-GNARS------VPEEIWQLFPvlkemk 127
Cdd:COG4778 78 -DLAQASPREILalrRRTIGYVSQFLRVIPRVSaldvVAEPLLeRGVDREEArARAREllarlnLPERLWDLPP------ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 128 hrrgGDLSGGQQQQLAIGRALASRPRLLILDEPTEGIQP---SVIKEIgqvIRSLANRGdMAILLVeqFYD--FAAELAD 202
Cdd:COG4778 151 ----ATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAanrAVVVEL---IEEAKARG-TAIIGI--FHDeeVREAVAD 220
|
....*....
gi 1737198856 203 SYLVMSRGS 211
Cdd:COG4778 221 RVVDVTPFS 229
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
9-212 |
4.78e-19 |
|
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: 81.11 E-value: 4.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 9 QYYGGSH-ILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQSgVAYVPQGREI 87
Cdd:cd03246 9 RYPGAEPpVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDH-VGYLPQDDEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 88 FPRlTVEENLlmglsrfsagnarsvpeeiwqlfpvlkemkhrrggdLSGGQQQQLAIGRALASRPRLLILDEPTEGIQPS 167
Cdd:cd03246 88 FSG-SIAENI------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVE 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1737198856 168 VIKEIGQVIRSLANRGDMAILLVEQfyDFAAELADSYLVMSRGSI 212
Cdd:cd03246 131 GERALNQAIAALKAAGATRIVIAHR--PETLASADRILVLEDGRV 173
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
9-216 |
7.13e-19 |
|
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: 84.92 E-value: 7.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 9 QYYG-GSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQrVQSGVAYVPQGrei 87
Cdd:TIGR03375 472 AYPGqETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPAD-LRRNIGYVPQD--- 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 88 fPRL---TVEENLLM-----------------GLSRFSAGNARSvpeeiwqlfpvLKEMKHRRGGDLSGGQQQQLAIGRA 147
Cdd:TIGR03375 548 -PRLfygTLRDNIALgapyaddeeilraaelaGVTEFVRRHPDG-----------LDMQIGERGRSLSGGQRQAVALARA 615
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1737198856 148 LASRPRLLILDEPTEGIQPSVIKEIGQVIRSLAnrGDMAILLVEQFYDFaAELADSYLVMSRGSIVQQG 216
Cdd:TIGR03375 616 LLRDPPILLLDEPTSAMDNRSEERFKDRLKRWL--AGKTLVLVTHRTSL-LDLVDRIIVMDNGRIVADG 681
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-192 |
1.36e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 80.38 E-value: 1.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSIthSKPHQRVQSGVAY 80
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI--KKDLCTYQKQLCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 81 VPQGREIFPRLTVEENLLMGLsRFSAGNARSvpEEIWQLFPvLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEP 160
Cdd:PRK13540 79 VGHRSGINPYLTLRENCLYDI-HFSPGAVGI--TELCRLFS-LEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEP 154
|
170 180 190
....*....|....*....|....*....|..
gi 1737198856 161 TEGIQPSVIKEIGQVIRSLANRGDMAILLVEQ 192
Cdd:PRK13540 155 LVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
10-221 |
2.23e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 81.57 E-value: 2.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 10 YYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQSGVAYVPQGREI-F 88
Cdd:PRK13644 11 YPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGIVFQNPETqF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 89 PRLTVEENLlmglsRFSAGNARSVPEEIWQLFPV------LKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEPTE 162
Cdd:PRK13644 91 VGRTVEEDL-----AFGPENLCLPPIEIRKRVDRalaeigLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1737198856 163 GIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAelADSYLVMSRGSIVQQGRGENM 221
Cdd:PRK13644 166 MLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD--ADRIIVMDRGKIVLEGEPENV 222
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
16-160 |
2.72e-18 |
|
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: 79.82 E-value: 2.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 16 ILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGksithskphqrvqsGVAYVPQGREIFPRlTVEE 95
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--------------SIAYVSQEPWIQNG-TIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 96 NLLMGlSRFsagnarsvpEEIW--------QLFPVLKEMKHR-------RGGDLSGGQQQQLAIGRALASRPRLLILDEP 160
Cdd:cd03250 85 NILFG-KPF---------DEERyekvikacALEPDLEILPDGdlteigeKGINLSGGQKQRISLARAVYSDADIYLLDDP 154
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
29-220 |
3.11e-18 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 81.84 E-value: 3.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 29 VTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSI--THSK----PHQRvqsGVAYVPQGREIFPRLTVEENLLMGLS 102
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfdAEKGiclpPEKR---RIGYVFQDARLFPHYKVRGNLRYGMA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 103 RFSAGNArsvpEEIWQLF---PVLKemkhRRGGDLSGGQQQQLAIGRALASRPRLLILDEPTEGIQPSVIKEIGQVIRSL 179
Cdd:PRK11144 103 KSMVAQF----DKIVALLgiePLLD----RYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1737198856 180 ANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQGRGEN 220
Cdd:PRK11144 175 AREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEE 215
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-232 |
3.42e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 82.83 E-value: 3.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 15 HILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGgEVVWQGKSITHSKPHQ----RVQSGVAYVPQGREIFPR 90
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQG-EIWFDGQPLHNLNRRQllpvRHRIQVVFQDPNSSLNPR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 91 LTVEENLLMGLSRFSAgnARSVPEEIWQLFPVLKEM------KHRRGGDLSGGQQQQLAIGRALASRPRLLILDEPTEGI 164
Cdd:PRK15134 379 LNVLQIIEEGLRVHQP--TLSAAQREQQVIAVMEEVgldpetRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSL 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1737198856 165 QPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQGRGENM----EQEGVRGLVAI 232
Cdd:PRK15134 457 DKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVfaapQQEYTRQLLAL 528
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
17-216 |
3.85e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 80.83 E-value: 3.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 17 LRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQrVQSGVAYVPQGRE-IFPRLTVEE 95
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWD-VRRQVGMVFQNPDnQFVGATVQD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 96 NLLMGLSRFSAGNARSVPEEIWQLFPV-LKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEPTEGIQPSVIKEIGQ 174
Cdd:PRK13635 102 DVAFGLENIGVPREEMVERVDQALRQVgMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLE 181
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1737198856 175 VIRSLANRGDMAILLVEQFYDFAAElADSYLVMSRGSIVQQG 216
Cdd:PRK13635 182 TVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEG 222
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
16-224 |
4.53e-18 |
|
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: 82.40 E-value: 4.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 16 ILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQSgVAYVPQGREIFPRlTVEE 95
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKH-IGYLPQDVELFPG-TVAE 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 96 NLlmglSRFSAG-NARSVPE--------EIWQLFP-----VLKEmkhrRGGDLSGGQQQQLAIGRALASRPRLLILDEPT 161
Cdd:TIGR01842 411 NI----ARFGENaDPEKIIEaaklagvhELILRLPdgydtVIGP----GGATLSGGQRQRIALARALYGDPKLVVLDEPN 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1737198856 162 EGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYdfAAELADSYLVMSRGSIVQQGRGENMEQE 224
Cdd:TIGR01842 483 SNLDEEGEQALANAIKALKARGITVVVITHRPS--LLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
17-216 |
5.35e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 80.52 E-value: 5.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 17 LRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQSGVAYVPQG--REIFPRLtVE 94
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIRNKAGMVFQNpdNQIVATI-VE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 95 ENLlmglsRFSAGNARSVPEEI-WQLFPVLKEM---KHRRGGD--LSGGQQQQLAIGRALASRPRLLILDEPTEGIQPSV 168
Cdd:PRK13633 105 EDV-----AFGPENLGIPPEEIrERVDESLKKVgmyEYRRHAPhlLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSG 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1737198856 169 IKEIGQVIRSLANRGDMAILLVEQFYDFAAElADSYLVMSRGSIVQQG 216
Cdd:PRK13633 180 RREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEG 226
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-205 |
5.61e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 79.47 E-value: 5.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYG----GSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQ- 75
Cdd:PRK11629 5 LLQCDNLCKRYQegsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAEl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 76 --SGVAYVPQGREIFPRLTVEENLLMGLSRFSAGNARSVPEEIWQLFPV-LKEMKHRRGGDLSGGQQQQLAIGRALASRP 152
Cdd:PRK11629 85 rnQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVgLEHRANHRPSELSGGERQRVAIARALVNNP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1737198856 153 RLLILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAA------ELADSYL 205
Cdd:PRK11629 165 RLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKrmsrqlEMRDGRL 223
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-224 |
5.70e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 80.06 E-value: 5.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKG---------GEVVWQGKSITHSKPH 71
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagshiellGRTVQREGRLARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 72 QRVQSGvaYVPQGREIFPRLTVEENLLMG-----------LSRFSAGNARSVPEEIWQLFpvLKEMKHRRGGDLSGGQQQ 140
Cdd:PRK09984 84 SRANTG--YIFQQFNLVNRLSVLENVLIGalgstpfwrtcFSWFTREQKQRALQALTRVG--MVHFAHQRVSTLSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 141 QLAIGRALASRPRLLILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQGRGEN 220
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
|
....
gi 1737198856 221 MEQE 224
Cdd:PRK09984 240 FDNE 243
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
9-226 |
6.33e-18 |
|
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: 79.58 E-value: 6.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 9 QYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQrVQSGVAYVPQGREIF 88
Cdd:cd03253 9 AYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDS-LRRAIGVVPQDTVLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 89 PRlTVEENLLMGlsRFSAGNarsvpEEIW------QLFPVLKEMKH-------RRGGDLSGGQQQQLAIGRALASRPRLL 155
Cdd:cd03253 88 ND-TIGYNIRYG--RPDATD-----EEVIeaakaaQIHDKIMRFPDgydtivgERGLKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1737198856 156 ILDEPTEGIQPSVIKEIGQVIRSLAnRGDMAILLveqfydfAAEL-----ADSYLVMSRGSIVQQGRGEN-MEQEGV 226
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVS-KGRTTIVI-------AHRLstivnADKIIVLKDGRIVERGTHEElLAKGGL 228
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
5-216 |
1.12e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 79.75 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 5 SELNQyyggshiLRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKP-HQRVQSGVAYVPQ 83
Cdd:PRK13642 18 SDVNQ-------LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVwNLRRKIGMVFQNP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 84 GREiFPRLTVEENLLMGLSRFSAGNARSVPEEIWQLFPV-LKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEPTE 162
Cdd:PRK13642 91 DNQ-FVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVnMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1737198856 163 GIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAElADSYLVMSRGSIVQQG 216
Cdd:PRK13642 170 MLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEA 222
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-216 |
1.36e-17 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 79.10 E-value: 1.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKG--------GEVVWQGKSItHSKPHQ 72
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGEPL-AAIDAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 73 RVQSGVAYVPQ-GREIFPrLTVEENLLMGL---SRFSAGNARSVPEEIWQLFPV--LKEMKHRRGGDLSGGQQQQLAIGR 146
Cdd:PRK13547 80 RLARLRAVLPQaAQPAFA-FSAREIVLLGRyphARRAGALTHRDGEIAWQALALagATALVGRDVTTLSGGELARVQFAR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1737198856 147 ALA---------SRPRLLILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:PRK13547 159 VLAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHG 237
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-202 |
1.77e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 78.67 E-value: 1.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRC---LMGLIPV--KGGEVVWQGKSI--THSKPHQrV 74
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGfrVEGKVTFHGKNLyaPDVDPVE-V 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 75 QSGVAYVPQGREIFPRlTVEENLLMGlSRFSA--GNARSVPEEIWQLFPVLKEMKHR---RGGDLSGGQQQQLAIGRALA 149
Cdd:PRK14243 90 RRRIGMVFQKPNPFPK-SIYDNIAYG-ARINGykGDMDELVERSLRQAALWDEVKDKlkqSGLSLSGGQQQRLCIARAIA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1737198856 150 SRPRLLILDEPTEGIQPSVIKEIGQVIRSLANRgdMAILLVEQFYDFAAELAD 202
Cdd:PRK14243 168 VQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSD 218
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-161 |
2.00e-17 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 75.95 E-value: 2.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWqGKSIThskphqrvqsgVAYV 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-GSTVK-----------IGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 82 PQgreifprltveenllmglsrfsagnarsvpeeiwqlfpvlkemkhrrggdLSGGQQQQLAIGRALASRPRLLILDEPT 161
Cdd:cd03221 69 EQ--------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPT 98
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-212 |
2.11e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 78.57 E-value: 2.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVvwqgksITHSKPHQRVQSGVAYV 81
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL------LAGTAPLAEAREDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 82 PQGREIFPRLTVEENLLMGLSrfsaGNARsvPEEIWQLFPV-LKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEP 160
Cdd:PRK11247 87 FQDARLLPWKKVIDNVGLGLK----GQWR--DAALQALAAVgLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1737198856 161 TEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSI 212
Cdd:PRK11247 161 LGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
13-223 |
2.55e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 78.29 E-value: 2.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 13 GSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSIT--HSKPHQRvqsGVAYVPQGREIFPR 90
Cdd:PRK10575 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLEswSSKAFAR---KVAYLPQQLPAAEG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 91 LTVEENLLMG-------LSRFSAGNARSVPEEIwqLFPVLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEPTEG 163
Cdd:PRK10575 100 MTVRELVAIGrypwhgaLGRFGAADREKVEEAI--SLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSA 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1737198856 164 IQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADsYLVMSR-GSIVQQG------RGENMEQ 223
Cdd:PRK10575 178 LDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCD-YLVALRgGEMIAQGtpaelmRGETLEQ 243
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
13-226 |
2.76e-17 |
|
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: 77.66 E-value: 2.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 13 GSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQrVQSGVAYVPQGREIFPRlT 92
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLAS-LRRQIGLVSQDVFLFND-T 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 93 VEENLLMGLSRFSAGNARSVPEeIWQLFPVLKEMKH-------RRGGDLSGGQQQQLAIGRALASRPRLLILDEPTEGIQ 165
Cdd:cd03251 92 VAENIAYGRPGATREEVEEAAR-AANAHEFIMELPEgydtvigERGVKLSGGQRQRIAIARALLKDPPILILDEATSALD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1737198856 166 PSVIKEIGQVIRSL-ANRGDMAIllveqfydfAAEL-----ADSYLVMSRGSIVQQGRGEN-MEQEGV 226
Cdd:cd03251 171 TESERLVQAALERLmKNRTTFVI---------AHRLstienADRIVVLEDGKIVERGTHEElLAQGGV 229
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
16-217 |
3.01e-17 |
|
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: 77.07 E-value: 3.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 16 ILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSkPHQRVQSGVAYVPQgreifprltvEE 95
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTI-PLEDLRSSLTIIPQ----------DP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 96 NLLMGLSRFSAGNARSVPEEiwQLFPVLKEmkhRRGGD-LSGGQQQQLAIGRALASRPRLLILDEPTEGIQPSVIKEIGQ 174
Cdd:cd03369 92 TLFSGTIRSNLDPFDEYSDE--EIYGALRV---SEGGLnLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQK 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1737198856 175 VIRSLANRGDMAILL--VEQFYDFaaelaDSYLVMSRGSIVQQGR 217
Cdd:cd03369 167 TIREEFTNSTILTIAhrLRTIIDY-----DKILVMDAGEVKEYDH 206
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-216 |
3.46e-17 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 78.98 E-value: 3.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 19 GVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQR--VQSGVAYVPQG--REIFPRLTV- 93
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWraVRSDIQMIFQDplASLNPRMTIg 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 94 ---EENLLMGLSRFSAGNARSVPEEIWQLFPVLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEPTEGIQPSVIK 170
Cdd:PRK15079 119 eiiAEPLRTYHPKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQA 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1737198856 171 EIGQVIRSLanRGDMAILLVEQFYDFAA--ELADSYLVMSRGSIVQQG 216
Cdd:PRK15079 199 QVVNLLQQL--QREMGLSLIFIAHDLAVvkHISDRVLVMYLGHAVELG 244
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-216 |
4.87e-17 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 79.34 E-value: 4.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELN----QYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIP----VKGGEVVWQGKSITHSKPHQ 72
Cdd:COG4172 6 LLSVEDLSvafgQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPdpaaHPSGSILFDGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 73 --RVQsgvayvpqGREI---F--------PRLTVE----ENLL--MGLSRfSAGNARSV----------PEEIWQLFPvl 123
Cdd:COG4172 86 lrRIR--------GNRIamiFqepmtslnPLHTIGkqiaEVLRlhRGLSG-AAARARALellervgipdPERRLDAYP-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 124 kemkHRrggdLSGGQQQQLAIGRALASRPRLLILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILLVEqfYDFA--AELA 201
Cdd:COG4172 155 ----HQ----LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLIT--HDLGvvRRFA 224
|
250
....*....|....*
gi 1737198856 202 DSYLVMSRGSIVQQG 216
Cdd:COG4172 225 DRVAVMRQGEIVEQG 239
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
9-216 |
8.15e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 77.10 E-value: 8.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 9 QYYG-GSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSIThSKPHQRVQSGVAYVPQGRE- 86
Cdd:PRK13648 16 QYQSdASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAIT-DDNFEKLRKHIGIVFQNPDn 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 87 IFPRLTVEENLLMGLSRFSAGN---ARSVPEEIWQLfpvlkEMKHRRGGD---LSGGQQQQLAIGRALASRPRLLILDEP 160
Cdd:PRK13648 95 QFVGSIVKYDVAFGLENHAVPYdemHRRVSEALKQV-----DMLERADYEpnaLSGGQKQRVAIAGVLALNPSVIILDEA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1737198856 161 TEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAElADSYLVMSRGSIVQQG 216
Cdd:PRK13648 170 TSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEG 224
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
17-221 |
9.27e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 77.18 E-value: 9.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 17 LRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSI---THSKPHQRVQSGVAYVPQgreiFPRL-- 91
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpeTGNKNLKKLRKKVSLVFQ----FPEAql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 92 ---TVEENLLMGLSRFSAGNARSVPEEIWQLFPV-LKE-MKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEPTEGIQP 166
Cdd:PRK13641 99 fenTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVgLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1737198856 167 SVIKEIGQVIRSLANRGDMAILLVEQFYDfAAELADSYLVMSRGSIVQQGRGENM 221
Cdd:PRK13641 179 EGRKEMMQLFKDYQKAGHTVILVTHNMDD-VAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-198 |
9.82e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 75.97 E-value: 9.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYG-GSH---ILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQ- 75
Cdd:PRK10584 6 IVEVHHLKKSVGqGEHelsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 76 --SGVAYVPQGREIFPRLTVEEN-----LLMGLS-RFSAGNARSVPEEIWqlfpvLKEMKHRRGGDLSGGQQQQLAIGRA 147
Cdd:PRK10584 86 raKHVGFVFQSFMLIPTLNALENvelpaLLRGESsRQSRNGAKALLEQLG-----LGKRLDHLPAQLSGGEQQRVALARA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1737198856 148 LASRPRLLILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAA 198
Cdd:PRK10584 161 FNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAA 211
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
32-216 |
1.15e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 78.22 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 32 LLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSIThSKPHQRVQSGVAYVPQGREIFPRlTVEENLLMGlsrfsagnaRS 111
Cdd:PRK10790 372 LVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLS-SLSHSVLRQGVAMVQQDPVVLAD-TFLANVTLG---------RD 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 112 VPEE-IW------QLFPVLKEMK---HRR----GGDLSGGQQQQLAIGRALASRPRLLILDEPTEGIQPSVIKEIGQVIR 177
Cdd:PRK10790 441 ISEEqVWqaletvQLAELARSLPdglYTPlgeqGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALA 520
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1737198856 178 SLANRGDMAIL------LVEqfydfaaelADSYLVMSRGSIVQQG 216
Cdd:PRK10790 521 AVREHTTLVVIahrlstIVE---------ADTILVLHRGQAVEQG 556
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-217 |
1.28e-16 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 77.15 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQ-YYGGS---HILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKP----HQ 72
Cdd:PRK11153 1 MIELKNISKvFPQGGrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEkelrKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 73 RVQSGVayvpqgreIFPRLtveeNLLMglSRFSAGN-------ARSVPEEIWQ----LFPV--LKEMKHRRGGDLSGGQQ 139
Cdd:PRK11153 81 RRQIGM--------IFQHF----NLLS--SRTVFDNvalplelAGTPKAEIKArvteLLELvgLSDKADRYPAQLSGGQK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1737198856 140 QQLAIGRALASRPRLLILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQGR 217
Cdd:PRK11153 147 QRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGT 224
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
9-160 |
1.40e-16 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 77.19 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 9 QYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRvqsGVAYVPQGREIF 88
Cdd:PRK11650 12 SYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADR---DIAMVFQNYALY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 89 PRLTVEENLLMGLsrfsagNARSVPEE-----------IWQLFPVLKemkhRRGGDLSGGQQQQLAIGRALASRPRLLIL 157
Cdd:PRK11650 89 PHMSVRENMAYGL------KIRGMPKAeieervaeaarILELEPLLD----RKPRELSGGQRQRVAMGRAIVREPAVFLF 158
|
...
gi 1737198856 158 DEP 160
Cdd:PRK11650 159 DEP 161
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
15-216 |
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 1737198856 15 HILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVvwqgksITHSKPHQRVQSGVAYVPQgreifprLTVE 94
Cdd:cd03220 36 WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV------TVRGRVSSLLGLGGGFNPE-------LTGR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 95 EN-----LLMGLSRfsaGNARSVPEEIWQlFPVLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEPTEGIQPSVI 169
Cdd:cd03220 103 ENiylngRLLGLSR---KEIDEKIDEIIE-FSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1737198856 170 KEIGQVIRSLANRGdMAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:cd03220 179 EKCQRRLRELLKQG-KTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
17-214 |
1.48e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 78.03 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 17 LRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQSGVAYVPQGREIFPRLTVEEN 96
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGVAIIYQELHLVPEMTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 97 LLMGL--SRFSAGNARSVPEEiwqlfpVLKEMKH--------RRGGDLSGGQQQQLAIGRALASRPRLLILDEPTEGIQP 166
Cdd:PRK11288 100 LYLGQlpHKGGIVNRRLLNYE------AREQLEHlgvdidpdTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1737198856 167 SVIKEIGQVIRSLANRGdMAILLVEQFYDFAAELADSYLVMSRGSIVQ 214
Cdd:PRK11288 174 REIEQLFRVIRELRAEG-RVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-166 |
1.57e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 77.86 E-value: 1.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 3 QVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQSGVAYVP 82
Cdd:NF033858 3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCPRIAYMP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 83 Q--GREIFPRLTVEENL-----LMGLSRfSAGNARsvpeeIWQL--------FPvlkemkHRRGGDLSGGQQQQLAIGRA 147
Cdd:NF033858 83 QglGKNLYPTLSVFENLdffgrLFGQDA-AERRRR-----IDELlratglapFA------DRPAGKLSGGMKQKLGLCCA 150
|
170
....*....|....*....
gi 1737198856 148 LASRPRLLILDEPTEGIQP 166
Cdd:NF033858 151 LIHDPDLLILDEPTTGVDP 169
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
14-212 |
1.68e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 76.31 E-value: 1.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 14 SHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKP-HQRVQSGVAYV-PQGReiFPRL 91
Cdd:PRK13650 20 KYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVwDIRHKIGMVFQnPDNQ--FVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 92 TVEENLLMGLSR--FSAGNARSVPEEIWQLFPvLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEPTEGIQPSVI 169
Cdd:PRK13650 98 TVEDDVAFGLENkgIPHEEMKERVNEALELVG-MQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1737198856 170 KEIGQVIRSLANRGDMAILLVEQFYDFAAeLADSYLVMSRGSI 212
Cdd:PRK13650 177 LELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQV 218
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
16-210 |
1.98e-16 |
|
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: 74.59 E-value: 1.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 16 ILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCL-----MGLIpvkGGEVVWQGKSIThsKPHQRVqsgVAYVPQGREIFPR 90
Cdd:cd03232 22 LLNNISGYVKPGTLTALMGESGAGKTTLLDVLagrktAGVI---TGEILINGRPLD--KNFQRS---TGYVEQQDVHSPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 91 LTVEENLlmglsRFSAGNarsvpeeiwqlfpvlkemkhrRGgdLSGGQQQQLAIGRALASRPRLLILDEPTEGIQPSVIK 170
Cdd:cd03232 94 LTVREAL-----RFSALL---------------------RG--LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAY 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1737198856 171 EIGQVIRSLANRGdMAIL---------LVEQFydfaaelaDSYLVMSRG 210
Cdd:cd03232 146 NIVRFLKKLADSG-QAILctihqpsasIFEKF--------DRLLLLKRG 185
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-225 |
2.24e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 77.58 E-value: 2.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 20 VSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVwQGKSITHSKPHQ-RVQsgVAYVPQGreifPRL---TVEE 95
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQGSLKI-NGIELRELDPESwRKH--LSWVGQN----PQLphgTLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 96 NLLMGlsrfsagNARSVPEEIWQL--------FpvLKEMKH-------RRGGDLSGGQQQQLAIGRALASRPRLLILDEP 160
Cdd:PRK11174 442 NVLLG-------NPDASDEQLQQAlenawvseF--LPLLPQgldtpigDQAAGLSVGQAQRLALARALLQPCQLLLLDEP 512
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1737198856 161 TEGIQPSVIKeigQVIRSL--ANRGDMAILLVEQFYDFAAelADSYLVMSRGSIVQQGRGENMEQEG 225
Cdd:PRK11174 513 TASLDAHSEQ---LVMQALnaASRRQTTLMVTHQLEDLAQ--WDQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
16-216 |
2.25e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 75.99 E-value: 2.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 16 ILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMG-LIPVKGGEVVWQGKSIT-HSKPHQRVQSGVAYVPQGRE-IFPRLT 92
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlLLPDDNPNSKITVDGITlTAKTVWDIREKVGIVFQNPDnQFVGAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 93 VEENLLMGLSRfsagnaRSVPEEiwQLFPVLKEMKHRRG---------GDLSGGQQQQLAIGRALASRPRLLILDEPTEG 163
Cdd:PRK13640 102 VGDDVAFGLEN------RAVPRP--EMIKIVRDVLADVGmldyidsepANLSGGQKQRVAIAGILAVEPKIIILDESTSM 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1737198856 164 IQPSVIKEIGQVIRSLANRGDMAILLVEQFYDfAAELADSYLVMSRGSIVQQG 216
Cdd:PRK13640 174 LDPAGKEQILKLIRKLKKKNNLTVISITHDID-EANMADQVLVLDDGKLLAQG 225
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-216 |
2.47e-16 |
|
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: 73.89 E-value: 2.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGS--HILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSIthSKPHQRVQSGVA 79
Cdd:cd03247 1 LSINNVSFSYPEQeqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPV--SDLEKALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 80 YVPQGREIFPRlTVEENLlmglsrfsagnarsvpeeiwqlfpvlkemkhrrGGDLSGGQQQQLAIGRALASRPRLLILDE 159
Cdd:cd03247 79 VLNQRPYLFDT-TLRNNL---------------------------------GRRFSGGERQRLALARILLQDAPIVLLDE 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1737198856 160 PTEGIQPSVIKEIGQVIRSLANrgDMAILLVEQFYDfAAELADSYLVMSRGSIVQQG 216
Cdd:cd03247 125 PTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLT-GIEHMDKILFLENGKIIMQG 178
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
16-218 |
2.54e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 77.23 E-value: 2.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 16 ILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGgevvWQGKSITHS-KPHQRVQSGVAYVPQGREIFPRLTVE 94
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNN----FTGTILANNrKPTKQILKRTGFVTQDDILYPHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 95 ENLLMgLSRFSAGNARSVPEEIWQLFPVLKEMKHRRGGD----------LSGGQQQQLAIGRALASRPRLLILDEPTEGI 164
Cdd:PLN03211 159 ETLVF-CSLLRLPKSLTKQEKILVAESVISELGLTKCENtiignsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGL 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1737198856 165 QPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQGRG 218
Cdd:PLN03211 238 DATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKG 291
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-211 |
1.19e-15 |
|
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: 75.82 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGS------HILRGVSfeavVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKphQRV 74
Cdd:TIGR01257 1937 ILRLNELTKVYSGTsspavdRLCVGVR----PGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNI--SDV 2010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 75 QSGVAYVPQGREIFPRLTVEENLLMglsrfsAGNARSVP-EEI-----WQLFPV-LKEMKHRRGGDLSGGQQQQLAIGRA 147
Cdd:TIGR01257 2011 HQNMGYCPQFDAIDDLLTGREHLYL------YARLRGVPaEEIekvanWSIQSLgLSLYADRLAGTYSGGNKRKLSTAIA 2084
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1737198856 148 LASRPRLLILDEPTEGIQPSVIKEIGQVIRSLANRGdMAILLVEQFYDFAAELADSYLVMSRGS 211
Cdd:TIGR01257 2085 LIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREG-RAVVLTSHSMEECEALCTRLAIMVKGA 2147
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
17-216 |
1.24e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 74.05 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 17 LRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHS---KPHQRVQSGVAYVPQgreiFPRL-- 91
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKtkdKYIRPVRKRIGMVFQ----FPESql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 92 ---TVEENLLMGLSRFSAgNARSVPEEIWQL-----FPvlKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEPTEG 163
Cdd:PRK13646 99 fedTVEREIIFGPKNFKM-NLDEVKNYAHRLlmdlgFS--RDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1737198856 164 IQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:PRK13646 176 LDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQT 228
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
12-190 |
3.01e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 72.05 E-value: 3.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 12 GGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQSgVAYVPQGREIFPRl 91
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQ-VSYCAQTPTLFGD- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 92 TVEENLLM---------GLSRFSAGNAR-SVPEEIWQlfpvlkemkhRRGGDLSGGQQQQLAIGRALASRPRLLILDEPT 161
Cdd:PRK10247 96 TVYDNLIFpwqirnqqpDPAIFLDDLERfALPDTILT----------KNIAELSGGEKQRISLIRNLQFMPKVLLLDEIT 165
|
170 180
....*....|....*....|....*....
gi 1737198856 162 EGIQPSVIKEIGQVIRSLANRGDMAILLV 190
Cdd:PRK10247 166 SALDESNKHNVNEIIHRYVREQNIAVLWV 194
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
28-216 |
7.80e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 71.96 E-value: 7.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 28 EVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHS----KPHQRVQSGVAYVPQgreiFPRL-----TVEENLL 98
Cdd:PRK13645 38 KVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANlkkiKEVKRLRKEIGLVFQ----FPEYqlfqeTIEKDIA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 99 MGLSRFSAGNA---RSVPEeIWQLFPVLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEPTEGIQPSVIKEIGQV 175
Cdd:PRK13645 114 FGPVNLGENKQeayKKVPE-LLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINL 192
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1737198856 176 IRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:PRK13645 193 FERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIG 233
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-210 |
1.12e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 72.83 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 16 ILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCL-----MGLIpvKGGEVVWQGKSITHSkphqrVQSGVAYVPQGREIFPR 90
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLaervtTGVI--TGGDRLVNGRPLDSS-----FQRSIGYVQQQDLHLPT 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 91 LTVEENLlmglsRFSAG--NARSVP--------EEIWQLFpvlkEMKHRR-------GGDLSGGQQQQLAIGRALASRPR 153
Cdd:TIGR00956 851 STVRESL-----RFSAYlrQPKSVSksekmeyvEEVIKLL----EMESYAdavvgvpGEGLNVEQRKRLTIGVELVAKPK 921
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1737198856 154 LLI-LDEPTEGIQPSVIKEIGQVIRSLANRGDmAIL---------LVEQFydfaaelaDSYLVMSRG 210
Cdd:TIGR00956 922 LLLfLDEPTSGLDSQTAWSICKLMRKLADHGQ-AILctihqpsaiLFEEF--------DRLLLLQKG 979
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
16-216 |
1.40e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 71.42 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 16 ILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVvwQGKSItHSKPHQRVQSGVAYVPQgREI--FPRL-- 91
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTI--QVGDI-YIGDKKNNHELITNPYS-KKIknFKELrr 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 92 ----------------TVEENLLMGlsRFSAGNARSVPEEIWQLFPVLKEMKH----RRGGDLSGGQQQQLAIGRALASR 151
Cdd:PRK13631 117 rvsmvfqfpeyqlfkdTIEKDIMFG--PVALGVKKSEAKKLAKFYLNKMGLDDsyleRSPFGLSGGQKRRVAIAGILAIQ 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1737198856 152 PRLLILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFyDFAAELADSYLVMSRGSIVQQG 216
Cdd:PRK13631 195 PEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTM-EHVLEVADEVIVMDKGKILKTG 258
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-224 |
1.56e-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: 72.14 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYY-----GGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEV-VWQGKS-ITHSKP--- 70
Cdd:TIGR03269 279 IIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnVRVGDEwVDMTKPgpd 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 71 -HQRVQSGVAYVPQGREIFPRLTVEENLLMGLSrfsagnaRSVPEEIWQLFPVL------------KEMKHRRGGDLSGG 137
Cdd:TIGR03269 359 gRGRAKRYIGILHQEYDLYPHRTVLDNLTEAIG-------LELPDELARMKAVItlkmvgfdeekaEEILDKYPDELSEG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 138 QQQQLAIGRALASRPRLLILDEPTEGIQPSVIKEIGQVIrsLANRGDM--AILLVEQFYDFAAELADSYLVMSRGSIVQQ 215
Cdd:TIGR03269 432 ERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSI--LKAREEMeqTFIIVSHDMDFVLDVCDRAALMRDGKIVKI 509
|
....*....
gi 1737198856 216 GRGENMEQE 224
Cdd:TIGR03269 510 GDPEEIVEE 518
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
16-230 |
1.86e-14 |
|
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: 69.88 E-value: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 16 ILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSItHSKPHQRVQSGVAYVPQGREIFPRlTVEE 95
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDI-RDLNLRWLRSQIGLVSQEPVLFDG-TIAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 96 NLLMGLsrfsagNARSVPEE------------IWQLFPVLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEPTEG 163
Cdd:cd03249 96 NIRYGK------PDATDEEVeeaakkanihdfIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1737198856 164 IQPSVIKEIGQVIRSLAnRGDMAILLveqfydfAAEL-----ADSYLVMSRGSIVQQGR-GENMEQEGV-RGLV 230
Cdd:cd03249 170 LDAESEKLVQEALDRAM-KGRTTIVI-------AHRLstirnADLIAVLQNGQVVEQGThDELMAQKGVyAKLV 235
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
15-207 |
3.13e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.22 E-value: 3.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 15 HILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLI---PVKGGEVVWQGKSithskphQRVQSGVAYVPQGREIfprL 91
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgtPVAGCVDVPDNQF-------GREASLIDAIGRKGDF---K 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 92 TVEENL-LMGLSrfSAGNARSVPEEiwqlfpvlkemkhrrggdLSGGQQQQLAIGRALASRPRLLILDEPTEGIQPSVIK 170
Cdd:COG2401 114 DAVELLnAVGLS--DAVLWLRRFKE------------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAK 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 1737198856 171 EIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVM 207
Cdd:COG2401 174 RVARNLQKLARRAGITLVVATHHYDVIDDLQPDLLIF 210
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
11-209 |
3.38e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 69.37 E-value: 3.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 11 YGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGksithskphqrvQSGVAYVPQgreifpR 90
Cdd:PRK09544 14 FGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG------------KLRIGYVPQ------K 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 91 LTVEENLLMGLSRFSAGNARSVPEEIwqlFPVLKEMKHRRGGD-----LSGGQQQQLAIGRALASRPRLLILDEPTEGIQ 165
Cdd:PRK09544 76 LYLDTTLPLTVNRFLRLRPGTKKEDI---LPALKRVQAGHLIDapmqkLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1737198856 166 PSVIKEIGQVIRSLANRGDMAILLVEQfydfaaelaDSYLVMSR 209
Cdd:PRK09544 153 VNGQVALYDLIDQLRRELDCAVLMVSH---------DLHLVMAK 187
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
27-216 |
3.86e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 70.83 E-value: 3.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 27 GEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQG---KSITHSKPHQRVQSGVAYVPQGREIFPRLTVEENLLMGLSR 103
Cdd:PRK10070 54 GEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMEL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 104 FSAGNARSVPEEIWQLFPV-LKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEPTEGIQPSVIKEIGQVIRSLANR 182
Cdd:PRK10070 134 AGINAEERREKALDALRQVgLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAK 213
|
170 180 190
....*....|....*....|....*....|....
gi 1737198856 183 GDMAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:PRK10070 214 HQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVG 247
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-226 |
6.62e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 70.39 E-value: 6.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 17 LRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMG-LIPVKGGEVVWQGKsithskphqrvqsgVAYVPQGREIFpRLTVEE 95
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRGS--------------VAYVPQVSWIF-NATVRE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 96 NLLMGLSRFSAGNARSVPEEIWQ----LFPV--LKEMKHRrGGDLSGGQQQQLAIGRALASRPRLLILDEPTEGIQPSVI 169
Cdd:PLN03232 698 NILFGSDFESERYWRAIDVTALQhdldLLPGrdLTEIGER-GVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVA 776
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1737198856 170 KEIGQVIRSLANRGDMAILLVEQFYDFAaeLADSYLVMSRGSIVQQGRGENMEQEGV 226
Cdd:PLN03232 777 HQVFDSCMKDELKGKTRVLVTNQLHFLP--LMDRIILVSEGMIKEEGTFAELSKSGS 831
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-216 |
7.67e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 70.14 E-value: 7.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 16 ILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIP----VKGGEVVWQGKSITHSKPHQRVQsgVAYVPQGREIFPRL 91
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDgfhiGVEGVITYDGITPEEIKKHYRGD--VVYNAETDVHFPHL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 92 TVEENL------------LMGLSRFS-AGNARSVPEEIWQLfpvlkemKHRR----GGDL----SGGQQQQLAIGRALAS 150
Cdd:TIGR00956 154 TVGETLdfaarcktpqnrPDGVSREEyAKHIADVYMATYGL-------SHTRntkvGNDFvrgvSGGERKRVSIAEASLG 226
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1737198856 151 RPRLLILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILL-VEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:TIGR00956 227 GAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVaIYQCSQDAYELFDKVIVLYEGYQIYFG 293
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
17-216 |
9.56e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 68.96 E-value: 9.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 17 LRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQSGVAYVPQGREIFPRL----- 91
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEKVLEKLVIQKTRFKKIkkike 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 92 -------------------TVEENLLMGLSRF--SAGNARSVPEEIWQLFPVLKEMKHRRGGDLSGGQQQQLAIGRALAS 150
Cdd:PRK13651 103 irrrvgvvfqfaeyqlfeqTIEKDIIFGPVSMgvSKEEAKKRAAKYIELVGLDESYLQRSPFELSGGQKRRVALAGILAM 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1737198856 151 RPRLLILDEPTEGIQPSVIKEIGQVIRSLANRGDmAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:PRK13651 183 EPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVLEWTKRTIFFKDGKIIKDG 247
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
11-226 |
1.81e-13 |
|
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: 68.97 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 11 YGGSHI--LRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKpHQRVQSGVAYVPQGREIF 88
Cdd:TIGR02203 340 YPGRDRpaLDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT-LASLRRQVALVSQDVVLF 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 89 PRlTVEENLLMG----------LSRFSAGNARSVpeeIWQLFPVLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILD 158
Cdd:TIGR02203 419 ND-TIANNIAYGrteqadraeiERALAAAYAQDF---VDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILD 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1737198856 159 EPTEGIQPSVIKEIGQVIRSLAnRGDMAILLVEQFYdfAAELADSYLVMSRGSIVQQG-RGENMEQEGV 226
Cdd:TIGR02203 495 EATSALDNESERLVQAALERLM-QGRTTLVIAHRLS--TIEKADRIVVMDDGRIVERGtHNELLARNGL 560
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-221 |
1.82e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.11 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELN----QYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVwQGKSITHSKPHQRVQS 76
Cdd:PRK10261 12 VLAVENLNiafmQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQ-CDKMLLRRRSRQVIEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 77 GVAYVPQGRE--------IF--------PRLTVEEN------LLMGLSRFSA-GNARSVPEEIwqLFPVLKEMKHRRGGD 133
Cdd:PRK10261 91 SEQSAAQMRHvrgadmamIFqepmtslnPVFTVGEQiaesirLHQGASREEAmVEAKRMLDQV--RIPEAQTILSRYPHQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 134 LSGGQQQQLAIGRALASRPRLLILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIV 213
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
....*...
gi 1737198856 214 QQGRGENM 221
Cdd:PRK10261 249 ETGSVEQI 256
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-219 |
1.85e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 68.23 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGSHI-LRGV---SFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIP----VKGGEVVWQGKSITHSKPHQ 72
Cdd:PRK11022 3 LLNVDKLSVHFGDESApFRAVdriSYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 73 R---VQSGVAYVPQG--REIFPRLTVEENLLMGLSRFSAGNARSVPEEIWQLFPV---------LKEMKHRrggdLSGGQ 138
Cdd:PRK11022 83 RrnlVGAEVAMIFQDpmTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQvgipdpasrLDVYPHQ----LSGGM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 139 QQQLAIGRALASRPRLLILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQGRG 218
Cdd:PRK11022 159 SQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKA 238
|
.
gi 1737198856 219 E 219
Cdd:PRK11022 239 H 239
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-216 |
3.62e-13 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 67.91 E-value: 3.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGL--IPVKGGEVVWQ------------------ 61
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 62 -----GKSITH--------SKP-HQRVQSGVAYVPQGR-EIFPRLTVEENLLMGLSR--FSAGNARSVPEEIWQLFPVLK 124
Cdd:TIGR03269 81 pcpvcGGTLEPeevdfwnlSDKlRRRIRKRIAIMLQRTfALYGDDTVLDNVLEALEEigYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 125 EMKHRrGGDLSGGQQQQLAIGRALASRPRLLILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSY 204
Cdd:TIGR03269 161 RITHI-ARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKA 239
|
250
....*....|..
gi 1737198856 205 LVMSRGSIVQQG 216
Cdd:TIGR03269 240 IWLENGEIKEEG 251
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
15-216 |
3.62e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 67.96 E-value: 3.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 15 HILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPH--QRVQSGVAYVPQG--REIFPR 90
Cdd:PRK10261 338 HAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGklQALRRDIQFIFQDpyASLDPR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 91 LTVEENLLMGLSRFSAGNARSVPEEI-WQLFPV--LKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEPTEGIQPS 167
Cdd:PRK10261 418 QTVGDSIMEPLRVHGLLPGKAAAARVaWLLERVglLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVS 497
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1737198856 168 VIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:PRK10261 498 IRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-219 |
4.61e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 66.05 E-value: 4.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQ-YYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSK----PHQRVQ 75
Cdd:PRK10908 1 MIRFEHVSKaYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKnrevPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 76 SGVAYvpQGREIFPRLTVEENLLMGL-----------SRFSAGNARSVPEEIWQLFPVlkemkhrrggDLSGGQQQQLAI 144
Cdd:PRK10908 81 IGMIF--QDHHLLMDRTVYDNVAIPLiiagasgddirRRVSAALDKVGLLDKAKNFPI----------QLSGGEQQRVGI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1737198856 145 GRALASRPRLLILDEPTEGIQPSVIKEIGQVIRSLaNRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQGRGE 219
Cdd:PRK10908 149 ARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEF-NRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGVGGE 222
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-224 |
4.73e-13 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 67.45 E-value: 4.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTllrclmGLIPVK-----GGEVVWQGKSITHSKPHQRVQS 76
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**R------GALPAHv*gpdAGRRPWRF*TWCANRRALRRTI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 77 GVAY-VPQGREifPRLTVEENLLMgLSR---FSAGNARSVPEEIWQLFPvLKEMKHRRGGDLSGGQQQQLAIGRALASRP 152
Cdd:NF000106 88 G*HRpVR*GRR--ESFSGRENLYM-IGR*ldLSRKDARARADELLERFS-LTEAAGRAAAKYSGGMRRRLDLAASMIGRP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1737198856 153 RLLILDEPTEGIQPSVIKEIGQVIRSLANRGdMAILLVEQFYDFAAELADSYLVMSRGSIVQQGRGENMEQE 224
Cdd:NF000106 164 AVLYLDEPTTGLDPRTRNEVWDEVRSMVRDG-ATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTK 234
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
16-161 |
4.91e-13 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 65.90 E-value: 4.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 16 ILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRV---QSGVAYVPQGREIFPRLT 92
Cdd:NF038007 20 VLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIilrRELIGYIFQSFNLIPHLS 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1737198856 93 VEENLLMGLSRfsagnaRSVP--EEIWQLFPVLK--EMKHRRG---GDLSGGQQQQLAIGRALASRPRLLILDEPT 161
Cdd:NF038007 100 IFDNVALPLKY------RGVAkkERIERVNQVLNlfGIDNRRNhkpMQLSGGQQQRVAIARAMVSNPALLLADEPT 169
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
27-161 |
8.77e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.90 E-value: 8.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 27 GEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQgKSITHSKPHQR------------VQSGVAYVPQGREIFPRLT-- 92
Cdd:PRK11147 29 NERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE-QDLIVARLQQDpprnvegtvydfVAEGIEEQAEYLKRYHDIShl 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 93 VE----ENLLMGLSRfsagnarsVPEEI-----WQL----FPVLKEMK---HRRGGDLSGGQQQQLAIGRALASRPRLLI 156
Cdd:PRK11147 108 VEtdpsEKNLNELAK--------LQEQLdhhnlWQLenriNEVLAQLGldpDAALSSLSGGWLRKAALGRALVSNPDVLL 179
|
....*
gi 1737198856 157 LDEPT 161
Cdd:PRK11147 180 LDEPT 184
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
16-226 |
1.09e-12 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 66.77 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 16 ILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQ-RVQSGVayVPQGREIFPRlTVE 94
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASlRAAIGI--VPQDTVLFND-TIA 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 95 ENLLMGlsRFSAGnarsvPEEIW------QLFPVLKEMKH-------RRGGDLSGGQQQQLAIGRALASRPRLLILDE-- 159
Cdd:COG5265 450 YNIAYG--RPDAS-----EEEVEaaaraaQIHDFIESLPDgydtrvgERGLKLSGGEKQRVAIARTLLKNPPILIFDEat 522
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1737198856 160 -----PTEgiqpsviKEIGQVIRSLA-NRGDMAIllveqfydfAAEL-----ADSYLVMSRGSIVQQGR-GENMEQEGV 226
Cdd:COG5265 523 saldsRTE-------RAIQAALREVArGRTTLVI---------AHRLstivdADEILVLEAGRIVERGThAELLAQGGL 585
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-216 |
1.15e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 65.43 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLiP---VKGGEVVWQGKSITHSKPHQRVQSG 77
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH-PaykILEGDILFKGESILDLEPEERAHLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 78 VAYVPQgreiFPrltVE------ENLLMgLSRFSAGNARSVPE-EIWQLFPVLKE------MK----HRRGGD-LSGGQQ 139
Cdd:CHL00131 86 IFLAFQ----YP---IEipgvsnADFLR-LAYNSKRKFQGLPElDPLEFLEIINEklklvgMDpsflSRNVNEgFSGGEK 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1737198856 140 QQLAIGRALASRPRLLILDEPTEGIQPSVIKEIGQVIRSLANRgDMAILLVEQFYDFAAELADSYL-VMSRGSIVQQG 216
Cdd:CHL00131 158 KRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTS-ENSIILITHYQRLLDYIKPDYVhVMQNGKIIKTG 234
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
15-216 |
1.28e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 65.10 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 15 HILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGksithskphqRVQS----GVAYVPQgreifpr 90
Cdd:COG1134 40 WALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG----------RVSAllelGAGFHPE------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 91 LTVEEN-----LLMGLSRfsagnarsvpEEIWQLFPVLKE-----------MKHrrggdLSGGQQQQLAIGRALASRPRL 154
Cdd:COG1134 103 LTGRENiylngRLLGLSR----------KEIDEKFDEIVEfaelgdfidqpVKT-----YSSGMRARLAFAVATAVDPDI 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737198856 155 LILDEPTegiqpSVikeiG---------QVIRSLANRGdMAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:COG1134 168 LLVDEVL-----AV----GdaafqkkclARIRELRESG-RTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDG 228
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
17-216 |
1.84e-12 |
|
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: 64.28 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 17 LRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQSGVAYvPQGREIFPRLTVEEN 96
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVF-GQKTQLWWDLPVIDS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 97 LLM-----GLSRFSAGNARSVPEEIWQLFPVLKEMKHRrggdLSGGQQQQLAIGRALASRPRLLILDEPTEGIQPSVIKE 171
Cdd:cd03267 116 FYLlaaiyDLPPARFKKRLDELSELLDLEELLDTPVRQ----LSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQEN 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1737198856 172 IGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:cd03267 192 IRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
32-179 |
2.39e-12 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 62.94 E-value: 2.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 32 LLGRNGVGKTTLLRCLMGLIPVKGGEVvwqgksithSKPhqrVQSGVAYVPQgREIFPRLTVEENLLmglsrfsagnars 111
Cdd:cd03223 32 ITGPSGTGKSSLFRALAGLWPWGSGRI---------GMP---EGEDLLFLPQ-RPYLPLGTLREQLI------------- 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1737198856 112 vpeeiwqlFPVLKEmkhrrggdLSGGQQQQLAIGRALASRPRLLILDEPTEGIQPSVIKEIGQVIRSL 179
Cdd:cd03223 86 --------YPWDDV--------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKEL 137
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-161 |
4.83e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 64.53 E-value: 4.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKsithskphqrvqSGVAYV 81
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSEN------------ANIGYY 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 82 PQGREI-FPRltvEENLL--MGLSRFSAGNARSVPEEIWQ-LFP---VLKEMKhrrggDLSGGQQQQLAIGRALASRPRL 154
Cdd:PRK15064 388 AQDHAYdFEN---DLTLFdwMSQWRQEGDDEQAVRGTLGRlLFSqddIKKSVK-----VLSGGEKGRMLFGKLMMQKPNV 459
|
....*..
gi 1737198856 155 LILDEPT 161
Cdd:PRK15064 460 LVMDEPT 466
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-206 |
6.74e-12 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 63.20 E-value: 6.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 27 GEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSithskphqrvqsgVAYVPQGREIFPRLTVEEnLLMGLSRfSA 106
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT-------------VSYKPQYIKADYEGTVRD-LLSSITK-DF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 107 GNARSVPEEI---WQLFPVLKemkhRRGGDLSGGQQQQLAIGRALASRPRLLILDEPTEGIQPSVIKEIGQVIRSLANRG 183
Cdd:cd03237 90 YTHPYFKTEIakpLQIEQILD----REVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENN 165
|
170 180
....*....|....*....|...
gi 1737198856 184 DMAILLVEQFYDFAAELADSYLV 206
Cdd:cd03237 166 EKTAFVVEHDIIMIDYLADRLIV 188
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
12-216 |
7.17e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 64.08 E-value: 7.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 12 GGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSIThSKPHQRVQSGVAYVPQGREIFPRl 91
Cdd:PRK11160 351 QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIA-DYSEAALRQAISVVSQRVHLFSA- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 92 TVEENLLMGLSRFSagnarsvpEEiwQLFPVLKEM---KHRRGGD------------LSGGQQQQLAIGRALASRPRLLI 156
Cdd:PRK11160 429 TLRDNLLLAAPNAS--------DE--ALIEVLQQVgleKLLEDDKglnawlgeggrqLSGGEQRRLGIARALLHDAPLLL 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1737198856 157 LDEPTEGIQPSVIKEIGQVIRSLAnrGDMAILLV-------EQFydfaaelaDSYLVMSRGSIVQQG 216
Cdd:PRK11160 499 LDEPTEGLDAETERQILELLAEHA--QNKTVLMIthrltglEQF--------DRICVMDNGQIIEQG 555
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-221 |
8.04e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 63.96 E-value: 8.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 19 GVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVK-----GGEVVWQGKSITH-SKPHQRVQSG--VAYVPQGREIF-- 88
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHaSEQTLRGVRGnkIAMIFQEPMVSln 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 89 PRLTVEENLLMGLS-----RFSAgnARSvpEEIWQLFPVLKEMKHRRGGD----LSGGQQQQLAIGRALASRPRLLILDE 159
Cdd:PRK15134 107 PLHTLEKQLYEVLSlhrgmRREA--ARG--EILNCLDRVGIRQAAKRLTDyphqLSGGERQRVMIAMALLTRPELLIADE 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1737198856 160 PTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQGRGENM 221
Cdd:PRK15134 183 PTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATL 244
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
12-166 |
9.50e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 62.86 E-value: 9.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 12 GGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSI---THSKPHQrVQSGVAYVPQGREIF 88
Cdd:PRK11831 18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamSRSRLYT-VRKRMSMLFQSGALF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 89 PRLTVEENLLMGLSRFSAgnarsVPEEIWQLFPVLK-EMKHRRGG------DLSGGQQQQLAIGRALASRPRLLILDEPT 161
Cdd:PRK11831 97 TDMNVFDNVAYPLREHTQ-----LPAPLLHSTVMMKlEAVGLRGAaklmpsELSGGMARRAALARAIALEPDLIMFDEPF 171
|
....*
gi 1737198856 162 EGIQP 166
Cdd:PRK11831 172 VGQDP 176
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
15-225 |
1.00e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 63.99 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 15 HILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMG-LIPVKGGEVVWQGKsithskphqrvqsgVAYVPQGREIFpRLTV 93
Cdd:PLN03130 631 PTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRGT--------------VAYVPQVSWIF-NATV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 94 EENLLMGlSRFSagnarsvPEEIWQLFPVlKEMKH--------------RRGGDLSGGQQQQLAIGRALASRPRLLILDE 159
Cdd:PLN03130 696 RDNILFG-SPFD-------PERYERAIDV-TALQHdldllpggdlteigERGVNISGGQKQRVSMARAVYSNSDVYIFDD 766
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1737198856 160 PTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYdFAAELaDSYLVMSRGSIVQQGRGENMEQEG 225
Cdd:PLN03130 767 PLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLH-FLSQV-DRIILVHEGMIKEEGTYEELSNNG 830
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
27-160 |
1.66e-11 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 61.58 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 27 GEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGK---SITHSKPHQRVQSGVAYVPQgREIFPRLTVEENLLMGlSR 103
Cdd:cd03290 27 GQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKnesEPSFEATRSRNRYSVAYAAQ-KPWLLNATVEENITFG-SP 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1737198856 104 FSAGNARSVPEEIwQLFPVLKEMKH-------RRGGDLSGGQQQQLAIGRALASRPRLLILDEP 160
Cdd:cd03290 105 FNKQRYKAVTDAC-SLQPDIDLLPFgdqteigERGINLSGGQRQRICVARALYQNTNIVFLDDP 167
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
27-223 |
1.82e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.82 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 27 GEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQSGVAYVPQGREIFPRLTVEENLLMGlsRFSA 106
Cdd:PRK10982 24 HSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQELNLVLQRSVMDNMWLG--RYPT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 107 G----NARSVPEEIWQLFPVLK-EMKHR-RGGDLSGGQQQQLAIGRALASRPRLLILDEPTEGIQPSVIKEIGQVIRSLA 180
Cdd:PRK10982 102 KgmfvDQDKMYRDTKAIFDELDiDIDPRaKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLK 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1737198856 181 NRGdMAILLVEQFYDFAAELADSYLVMSRGSIV--QQGRGENMEQ 223
Cdd:PRK10982 182 ERG-CGIVYISHKMEEIFQLCDEITILRDGQWIatQPLAGLTMDK 225
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-188 |
5.39e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 61.72 E-value: 5.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 27 GEVTCLLGRNGVGKTTLLRCLMG-LIPVKG---GEVVW-------QGKSIthsKPH-QRVQSG---VAYVPQGREIFPRL 91
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGeLKPNLGdydEEPSWdevlkrfRGTEL---QDYfKKLANGeikVAHKPQYVDLIPKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 92 ---TVEEnLLMGLsrfsagNARSVPEEIWQLFPvLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEPTegiqpSV 168
Cdd:COG1245 176 fkgTVRE-LLEKV------DERGKLDELAEKLG-LENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPS-----SY 242
|
170 180 190
....*....|....*....|....*....|...
gi 1737198856 169 --IKE---IGQVIRSLANRG--------DMAIL 188
Cdd:COG1245 243 ldIYQrlnVARLIRELAEEGkyvlvvehDLAIL 275
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
17-219 |
6.97e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 60.75 E-value: 6.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 17 LRGVSFE-------AVVGEVTCllgrngvGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPH------QRVQSgVAYVPQ 83
Cdd:PRK11308 31 LDGVSFTlergktlAVVGESGC-------GKSTLARLLTMIETPTGGELYYQGQDLLKADPEaqkllrQKIQI-VFQNPY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 84 GrEIFPRLTV----EENLLMGLSrFSAGNARSVPEEIWQLFPVLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDE 159
Cdd:PRK11308 103 G-SLNPRKKVgqilEEPLLINTS-LSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADE 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 160 PTEGIQPSVikeIGQVIRSLANrgdmailLVEQF---YDFAAE-------LADSYLVMSRGSIVQQGRGE 219
Cdd:PRK11308 181 PVSALDVSV---QAQVLNLMMD-------LQQELglsYVFISHdlsvvehIADEVMVMYLGRCVEKGTKE 240
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-177 |
7.23e-11 |
|
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: 61.46 E-value: 7.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYY--GGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKgGEVVWQGKSiTHSKPHQRVQSGVA 79
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVS-WNSVTLQTWRKAFG 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 80 YVPQGREIFPRlTVEENLlmglsrfsAGNARSVPEEIWQL------------FPVLKEMKHRRGG-DLSGGQQQQLAIGR 146
Cdd:TIGR01271 1296 VIPQKVFIFSG-TFRKNL--------DPYEQWSDEEIWKVaeevglksvieqFPDKLDFVLVDGGyVLSNGHKQLMCLAR 1366
|
170 180 190
....*....|....*....|....*....|.
gi 1737198856 147 ALASRPRLLILDEPTEGIQPSVIkeigQVIR 177
Cdd:TIGR01271 1367 SILSKAKILLLDEPSAHLDPVTL----QIIR 1393
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-206 |
9.27e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 60.95 E-value: 9.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 27 GEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKsithskphqrvqsgVAYVPQGREIFPRLTVEENLlmglsrfSA 106
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK--------------ISYKPQYISPDYDGTVEEFL-------RS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 107 GNARSVPEEIWQ---LFPV-LKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEPT------EGIqpsvikEIGQVI 176
Cdd:COG1245 425 ANTDDFGSSYYKteiIKPLgLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSahldveQRL------AVAKAI 498
|
170 180 190
....*....|....*....|....*....|...
gi 1737198856 177 RSLANRGDMAILLVE---QFYDFaaeLADSYLV 206
Cdd:COG1245 499 RRFAENRGKTAMVVDhdiYLIDY---ISDRLMV 528
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-214 |
9.70e-11 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 60.25 E-value: 9.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYY--GGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKgGEVVWQGKSiTHSKPHQRVQSGVA 79
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVS-WNSVPLQKWRKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 80 YVPQGREIFPRlTVEENLlmglsrfsAGNARSVPEEIWQL------------FPVLKEMKHRRGG-DLSGGQQQQLAIGR 146
Cdd:cd03289 81 VIPQKVFIFSG-TFRKNL--------DPYGKWSDEEIWKVaeevglksvieqFPGQLDFVLVDGGcVLSHGHKQLMCLAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1737198856 147 ALASRPRLLILDEPTEGIQPSVIKEIGQVIRSlaNRGDMAILLVEQFYDFAAElADSYLVMSRGSIVQ 214
Cdd:cd03289 152 SVLSKAKILLLDEPSAHLDPITYQVIRKTLKQ--AFADCTVILSEHRIEAMLE-CQRFLVIEENKVRQ 216
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
17-161 |
1.73e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 60.19 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 17 LRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPvKG---GEVVWQGKSITHSKPHQRVQSGVAYVPQGREIFPRLTV 93
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYP-HGsyeGEILFDGEVCRFKDIRDSEALGIVIIHQELALIPYLSI 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1737198856 94 EENLLMGLSRFSAG-------NARSvpEEIwqLFPV-LKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEPT 161
Cdd:NF040905 96 AENIFLGNERAKRGvidwnetNRRA--REL--LAKVgLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPT 167
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
13-161 |
1.73e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 60.21 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 13 GSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVwqgksithsKPH--------QRvqsgvAYVPQG 84
Cdd:COG4178 375 GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIA---------RPAgarvlflpQR-----PYLPLG 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 85 --REI---------FPRLTVEENL-LMGLSRFSAgnaRSVPEEIWQlfpvlkemkHRrggdLSGGQQQQLAIGRALASRP 152
Cdd:COG4178 441 tlREAllypataeaFSDAELREALeAVGLGHLAE---RLDEEADWD---------QV----LSLGEQQRLAFARLLLHKP 504
|
....*....
gi 1737198856 153 RLLILDEPT 161
Cdd:COG4178 505 DWLFLDEAT 513
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
13-172 |
1.96e-10 |
|
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: 60.31 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 13 GSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMG-LIPVKGgevvwqgkSITHSkphqrvqSGVAYVPQGREIFPRl 91
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGeLEPSEG--------KIKHS-------GRISFSPQTSWIMPG- 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 92 TVEENLLMGLS----RF-SAGNARSVPEEIwQLFPVLKEMKHRRGG-DLSGGQQQQLAIGRALASRPRLLILDEPTEGIQ 165
Cdd:TIGR01271 502 TIKDNIIFGLSydeyRYtSVIKACQLEEDI-ALFPEKDKTVLGEGGiTLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
....*..
gi 1737198856 166 PSVIKEI 172
Cdd:TIGR01271 581 VVTEKEI 587
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
15-224 |
2.09e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 59.80 E-value: 2.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 15 HILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGL-----IpvkGGEVVWQGKSITHSKPHQRVQSGVAYVPQGREifp 89
Cdd:NF040905 274 KVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRsygrnI---SGTVFKDGKEVDVSTVSDAIDAGLAYVTEDRK--- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 90 RL------TVEENL-LMGLSRFSAGNA------RSVPEEIwqlfpvLKEMKHR------RGGDLSGGQQQQLAIGRALAS 150
Cdd:NF040905 348 GYglnlidDIKRNItLANLGKVSRRGVideneeIKVAEEY------RKKMNIKtpsvfqKVGNLSGGNQQKVVLSKWLFT 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 151 RPRLLILDEPTEGIQPSVIKEIGQVIRSLANRGdMAILLVeqfydfAAEL------ADSYLVMSRGSIVQQGRGENMEQE 224
Cdd:NF040905 422 DPDVLILDEPTRGIDVGAKYEIYTIINELAAEG-KGVIVI------SSELpellgmCDRIYVMNEGRITGELPREEASQE 494
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
23-161 |
2.45e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.82 E-value: 2.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 23 EAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKsithskphqrvqsgVAYVPQGREIFPRLTVEENLlmgls 102
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK--------------ISYKPQYIKPDYDGTVEDLL----- 421
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1737198856 103 RFSAGNARSVP--EEIwqLFPV-LKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEPT 161
Cdd:PRK13409 422 RSITDDLGSSYykSEI--IKPLqLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPS 481
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
6-220 |
3.63e-10 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 58.76 E-value: 3.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 6 ELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIP----VKGGEVVWQGKSITHSKPHQRVQSgvayv 81
Cdd:COG4170 12 EIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDLLKLSPRERRKI----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 82 pQGRE---IF--------PRLTVEENLLMGLSrfsagnARSVPEEIWQLF----PVLKEMKHRRG------------GDL 134
Cdd:COG4170 87 -IGREiamIFqepsscldPSAKIGDQLIEAIP------SWTFKGKWWQRFkwrkKRAIELLHRVGikdhkdimnsypHEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 135 SGGQQQQLAIGRALASRPRLLILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQ 214
Cdd:COG4170 160 TEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVE 239
|
....*.
gi 1737198856 215 QGRGEN 220
Cdd:COG4170 240 SGPTEQ 245
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-166 |
5.66e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 58.60 E-value: 5.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 20 VSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSIThskPH-----QRVqsgvAYVPQGREIFPRLTVE 94
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD---AGdiatrRRV----GYMSQAFSLYGELTVR 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 95 ENLLMglsrfsagNAR--SVPEEIWQlfPVLKEMKHRRG---------GDLSGGQQQQLAIGRALASRPRLLILDEPTEG 163
Cdd:NF033858 358 QNLEL--------HARlfHLPAAEIA--ARVAEMLERFDladvadalpDSLPLGIRQRLSLAVAVIHKPELLILDEPTSG 427
|
...
gi 1737198856 164 IQP 166
Cdd:NF033858 428 VDP 430
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-216 |
8.93e-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: 58.42 E-value: 8.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 17 LRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKsithskphqrvqsgVAYVPQGREIfPRLTVEEN 96
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--------------VAYVPQQAWI-QNDSLREN 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 97 LLMGlSRFSAGNARSVPEEIwQLFPVLKEMKH-------RRGGDLSGGQQQQLAIGRALASRPRLLILDEPTEGIQPSVI 169
Cdd:TIGR00957 719 ILFG-KALNEKYYQQVLEAC-ALLPDLEILPSgdrteigEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVG 796
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1737198856 170 KEI-GQVIRSLANRGDMAILLVEQFYDFAAELaDSYLVMSRGSIVQQG 216
Cdd:TIGR00957 797 KHIfEHVIGPEGVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMG 843
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
22-219 |
8.95e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 57.43 E-value: 8.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 22 FEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKG---GEVVWQGKSITHSKPHQ--RVQSgvayvPQGREIF-------- 88
Cdd:PRK09473 37 FSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPEKElnKLRA-----EQISMIFqdpmtsln 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 89 PRLTVEENL---LM---GLSRfsagnARSVPEEIWQLFPV-LKEMKHRRG---GDLSGGQQQQLAIGRALASRPRLLILD 158
Cdd:PRK09473 112 PYMRVGEQLmevLMlhkGMSK-----AEAFEESVRMLDAVkMPEARKRMKmypHEFSGGMRQRVMIAMALLCRPKLLIAD 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737198856 159 EPTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQGRGE 219
Cdd:PRK09473 187 EPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNAR 247
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
20-225 |
1.12e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 56.86 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 20 VSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKgGEVVWQGKSI----THSKPHQRvqsgvAYVPQGREIFPRLTVEE 95
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGS-GSIQFAGQPLeawsAAELARHR-----AYLSQQQTPPFAMPVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 96 NLLMGL-SRFSAGNARSVPEEIWQLFPVLKEMkHRRGGDLSGGQQQQ-------LAIGRALASRPRLLILDEPTEGIQPS 167
Cdd:PRK03695 89 YLTLHQpDKTRTEAVASALNEVAEALGLDDKL-GRSVNQLSGGEWQRvrlaavvLQVWPDINPAGQLLLLDEPMNSLDVA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1737198856 168 VIKEIGQVIRSLANRGdMAILLVEQFYDFAAELADSYLVMSRGSIVQQGRGEN-MEQEG 225
Cdd:PRK03695 168 QQAALDRLLSELCQQG-IAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEvLTPEN 225
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
20-216 |
1.16e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 56.72 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 20 VSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQsgvayvpQGREIF--------PRL 91
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQ-------RIRMIFqdpstslnPRQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 92 TVEENLLMGLSRFSAGNARSVPEEIWQLFP---VLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEPTEGIQPSV 168
Cdd:PRK15112 105 RISQILDFPLRLNTDLEPEQREKQIIETLRqvgLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSM 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1737198856 169 IKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:PRK15112 185 RSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERG 232
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-191 |
1.19e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.51 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 27 GEVTCLLGRNGVGKTTLLRCLMG-LIPVKG---GEVVW-------QGKSI-THSKphqRVQSG---VAYVPQGREIFPRL 91
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGeLIPNLGdyeEEPSWdevlkrfRGTELqNYFK---KLYNGeikVVHKPQYVDLIPKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 92 ---TVEEnLLMGLsrfsagNARSVPEEIWQLFPvLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEPTEGIQpsv 168
Cdd:PRK13409 176 fkgKVRE-LLKKV------DERGKLDEVVERLG-LENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD--- 244
|
170 180
....*....|....*....|....*.
gi 1737198856 169 IKE---IGQVIRSLANrgDMAILLVE 191
Cdd:PRK13409 245 IRQrlnVARLIRELAE--GKYVLVVE 268
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
10-161 |
1.46e-09 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 57.28 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 10 YYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSIThSKPHQRVQSGVAYVPQGREIFP 89
Cdd:PRK13657 344 YDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIR-TVTRASLRRNIAVVFQDAGLFN 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 90 RlTVEENLLMGlsRFSAGNARSV-PEEIWQL--FPVLKEMKH-----RRGGDLSGGQQQQLAIGRALASRPRLLILDEPT 161
Cdd:PRK13657 423 R-SIEDNIRVG--RPDATDEEMRaAAERAQAhdFIERKPDGYdtvvgERGRQLSGGERQRLAIARALLKDPPILILDEAT 499
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-216 |
1.89e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.48 E-value: 1.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 16 ILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEvVWQGKSIthskphqrvqsgvAYVPQGREIFpRLTVEE 95
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGR-VWAERSI-------------AYVPQQAWIM-NATVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 96 NLLMGLSRFSAGNARSV-----PEEIWQLFPVLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEPTEGIQPSVIK 170
Cdd:PTZ00243 740 NILFFDEEDAARLADAVrvsqlEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGE 819
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1737198856 171 EIGQVIRSLANRGDMAILLVEQFYDFAaeLADSYLVMSRGSIVQQG 216
Cdd:PTZ00243 820 RVVEECFLGALAGKTRVLATHQVHVVP--RADYVVALGDGRVEFSG 863
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
16-216 |
2.27e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 55.86 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 16 ILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIP----VKGGEVVWQGKSITHSKPHQRVqsgVAYVPQG-REIF-P 89
Cdd:PRK10418 18 LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPagvrQTAGRVLLDGKPVAPCALRGRK---IATIMQNpRSAFnP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 90 RLT-----VEENLLMGLSRFSAGNARSV-------PEEIWQLFPVlkEMkhrrggdlSGGQQQQLAIGRALASRPRLLIL 157
Cdd:PRK10418 95 LHTmhthaRETCLALGKPADDATLTAALeavglenAARVLKLYPF--EM--------SGGMLQRMMIALALLCEAPFIIA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1737198856 158 DEPTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQG 216
Cdd:PRK10418 165 DEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQG 223
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-178 |
2.93e-09 |
|
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: 56.88 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 16 ILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQrVQSGVAYVPQGREIFprltvEE 95
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHD-LRFKITIIPQDPVLF-----SG 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 96 NLLMGLSRFSAGNarsvPEEIWQLFpvlkEMKHRR-----------------GGDLSGGQQQQLAIGRALASRPRLLILD 158
Cdd:TIGR00957 1375 SLRMNLDPFSQYS----DEEVWWAL----ELAHLKtfvsalpdkldhecaegGENLSVGQRQLVCLARALLRKTKILVLD 1446
|
170 180
....*....|....*....|
gi 1737198856 159 EPTEGIQPSVIKEIGQVIRS 178
Cdd:TIGR00957 1447 EATAAVDLETDNLIQSTIRT 1466
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-178 |
3.76e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 56.33 E-value: 3.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 16 ILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSIThSKPHQRVQSGVAYVPQGREIFPRlTVEE 95
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIG-AYGLRELRRQFSMIPQDPVLFDG-TVRQ 1402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 96 NllmgLSRFSagnaRSVPEEIWQLFPvLKEMKHR--------------RGGDLSGGQQQQLAIGRALASRPRLLIL-DEP 160
Cdd:PTZ00243 1403 N----VDPFL----EASSAEVWAALE-LVGLRERvasesegidsrvleGGSNYSVGQRQLMCMARALLKKGSGFILmDEA 1473
|
170
....*....|....*...
gi 1737198856 161 TEGIQPSVIKEIGQVIRS 178
Cdd:PTZ00243 1474 TANIDPALDRQIQATVMS 1491
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-216 |
3.77e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 55.18 E-value: 3.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGL--IPVKGGEVVWQGKSITHSKPHQRVQSGV 78
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 79 AYVPQGREIFPrlTVEENLLMGLSRFSAGNARSVP-----------EEIWQLFPVLKEMKHRR-GGDLSGGQQQQLAIGR 146
Cdd:PRK09580 81 FMAFQYPVEIP--GVSNQFFLQTALNAVRSYRGQEpldrfdfqdlmEEKIALLKMPEDLLTRSvNVGFSGGEKKRNDILQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737198856 147 ALASRPRLLILDEPTEGIQPSVIKEIGQVIRSLANrGDMAILLVEQFYDFAAELADSYL-VMSRGSIVQQG 216
Cdd:PRK09580 159 MAVLEPELCILDESDSGLDIDALKIVADGVNSLRD-GKRSFIIVTHYQRILDYIKPDYVhVLYQGRIVKSG 228
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-161 |
4.28e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.11 E-value: 4.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 3 QVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMG-LIPVKGgevvwqgksithskphqRVQSG---- 77
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGqLQADSG-----------------RIHCGtkle 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 78 VAYVPQGREIF-PRLTVEENLLMGLSRFSA-GNARSVPEEIwQ--LFPVLKEMKHRRGgdLSGGQQQQLAIGRALASRPR 153
Cdd:PRK11147 384 VAYFDQHRAELdPEKTVMDNLAEGKQEVMVnGRPRHVLGYL-QdfLFHPKRAMTPVKA--LSGGERNRLLLARLFLKPSN 460
|
....*...
gi 1737198856 154 LLILDEPT 161
Cdd:PRK11147 461 LLILDEPT 468
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-216 |
4.54e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 55.38 E-value: 4.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPhQRVQSGVAYV 81
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYAS-KEVARRIGLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 82 PQGREIFPRLTVEENLLMG-------LSRFSAGNARSVPEEIWQlfPVLKEMKHRRGGDLSGGQQQQLAIGRALASRPRL 154
Cdd:PRK10253 87 AQNATTPGDITVQELVARGryphqplFTRWRKEDEEAVTKAMQA--TGITHLADQSVDTLSGGQRQRAWIAMVLAQETAI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737198856 155 LILDEPTEGIQPSVIKEIGQVIRSLaNRgdmaillvEQFYDFAAELAD--------SYLVMSR-GSIVQQG 216
Cdd:PRK10253 165 MLLDEPTTWLDISHQIDLLELLSEL-NR--------EKGYTLAAVLHDlnqacryaSHLIALReGKIVAQG 226
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
10-161 |
8.46e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 54.94 E-value: 8.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 10 YYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEvVWQGKSIThskphqrvqsgVAYVPQGREIFP 89
Cdd:TIGR03719 14 VPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE-ARPQPGIK-----------VGYLPQEPQLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 90 RLTVEENLLMG-------LSRFSAGNAR----------------SVPEEI-----WQLFPVLK-EMKHRR--GGD----- 133
Cdd:TIGR03719 82 TKTVRENVEEGvaeikdaLDRFNEISAKyaepdadfdklaaeqaELQEIIdaadaWDLDSQLEiAMDALRcpPWDadvtk 161
|
170 180
....*....|....*....|....*...
gi 1737198856 134 LSGGQQQQLAIGRALASRPRLLILDEPT 161
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPT 189
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
2-225 |
9.37e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 55.10 E-value: 9.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGSH--ILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQrVQSGVA 79
Cdd:PRK10789 314 LDVNIRQFTYPQTDhpALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDS-WRSRLA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 80 YVPQGREIFPRlTVEENLLMGlsRFSAGN------AR--SVPEEIWQLFPVLKEMKHRRGGDLSGGQQQQLAIGRALASR 151
Cdd:PRK10789 393 VVSQTPFLFSD-TVANNIALG--RPDATQqeiehvARlaSVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLN 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1737198856 152 PRLLILDEPTEGIQPSVIKEIgqvIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSIVQQGRGENM-EQEG 225
Cdd:PRK10789 470 AEILILDDALSAVDGRTEHQI---LHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLaQQSG 541
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
13-211 |
9.94e-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: 9.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 13 GSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMG-LIPVKGgevvwqgkSITHSkphqrvqSGVAYVPQGREIFPRl 91
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGeLEPSEG--------KIKHS-------GRISFSSQFSWIMPG- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 92 TVEENLLMGLS----RF-SAGNARSVPEEIWQlFPVLKEMKHRRGG-DLSGGQQQQLAIGRALASRPRLLILDEPTEGIQ 165
Cdd:cd03291 113 TIKENIIFGVSydeyRYkSVVKACQLEEDITK-FPEKDNTVLGEGGiTLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1737198856 166 PSVIKEIGQ--VIRSLANRgdMAILLVEQFYDFaaELADSYLVMSRGS 211
Cdd:cd03291 192 VFTEKEIFEscVCKLMANK--TRILVTSKMEHL--KKADKILILHEGS 235
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
133-221 |
1.59e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 54.04 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 133 DLSGGQQQQLAIGRALASRPRLLILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILLVEQFYDFAAELADSYLVMSRGSI 212
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQT 237
|
....*....
gi 1737198856 213 VQQGRGENM 221
Cdd:PRK15093 238 VETAPSKEL 246
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-161 |
3.66e-08 |
|
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: 53.02 E-value: 3.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGSHILRGVSFE----AVVGevtcLLGRNGVGKTTLLRCLMGLIPVKGGEVVWqGKSithskphqrVQsg 77
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKlppgGIVG----VIGPNGAGKSTLFRMITGQEQPDSGTIEI-GET---------VK-- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 78 VAYVPQGRE-IFPRLTVEENLLMGLSRFSAGNaRSVPEEIW-QLFPVLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLL 155
Cdd:TIGR03719 387 LAYVDQSRDaLDPNKTVWEEISGGLDIIKLGK-REIPSRAYvGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVL 465
|
....*.
gi 1737198856 156 ILDEPT 161
Cdd:TIGR03719 466 LLDEPT 471
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
16-188 |
9.37e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 51.00 E-value: 9.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 16 ILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKsitHSKPHQRVQSgVAYVPQGREIFPRLTVEE 95
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGK---TATRGDRSRF-MAYLGHLPGLKADLSTLE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 96 NLLMgLSRFSAGNARSVPEEIWQLFPvLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEPTEGIQPSVIKEIGQV 175
Cdd:PRK13543 102 NLHF-LCGLHGRRAKQMPGSALAIVG-LAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRM 179
|
170
....*....|...
gi 1737198856 176 IRSLANRGDMAIL 188
Cdd:PRK13543 180 ISAHLRGGGAALV 192
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
17-226 |
9.38e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 51.94 E-value: 9.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 17 LRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSK-PHQRVQsgVAYVPQGREIFPRlTVEE 95
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTlASLRNQ--VALVSQNVHLFND-TIAN 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 96 NLLMGLS-RFS------AGNARSVPEEIWQLFPVLKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEPTEGIQPSV 168
Cdd:PRK11176 436 NIAYARTeQYSreqieeAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTES 515
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1737198856 169 IKEIGQVIRSL-ANRGDMAIL----LVEQfydfaaelADSYLVMSRGSIVQQGR-GENMEQEGV 226
Cdd:PRK11176 516 ERAIQAALDELqKNRTSLVIAhrlsTIEK--------ADEILVVEDGEIVERGThAELLAQNGV 571
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
21-168 |
1.08e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 51.67 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 21 SFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGevvwqgksiTHSKPHQrvqSGVAYVPQgREIFPRLTVEENLLMG 100
Cdd:TIGR00954 472 SFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGG---------RLTKPAK---GKLFYVPQ-RPYMTLGTLRDQIIYP 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 101 LSR---FSAGNARSVPEEIWQLFPvLKEMKHRRGG---------DLSGGQQQQLAIGRALASRPRLLILDEPTEGIQPSV 168
Cdd:TIGR00954 539 DSSedmKRRGLSDKDLEQILDNVQ-LTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDV 617
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-161 |
1.63e-07 |
|
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: 49.29 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 27 GEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVwqgksithskphqrvqsgvayvpqgreifprltveenllmglsRFSA 106
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVI-------------------------------------------YIDG 38
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1737198856 107 GNARSVPEEIWQLFPVlkemkHRRGGDLSGGQQQQLAIGRALASRPRLLILDEPT 161
Cdd:smart00382 39 EDILEEVLDQLLLIIV-----GGKKASGSGELRLRLALALARKLKPDVLILDEIT 88
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
16-214 |
1.69e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.52 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 16 ILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQrVQSGVAYVPQGREIFPRlTVEE 95
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTD-LRRVLSIIPQSPVLFSG-TVRF 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 96 NLlmglSRFSAGNarsvPEEIWQLFPV--LKEMKHRR-----------GGDLSGGQQQQLAIGRALASRPRLLILDEPTE 162
Cdd:PLN03232 1329 NI----DPFSEHN----DADLWEALERahIKDVIDRNpfgldaevsegGENFSVGQRQLLSLARALLRRSKILVLDEATA 1400
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1737198856 163 GIQPSVIKEIGQVIRSLANRGDMAILL--VEQFYDfaaelADSYLVMSRGSIVQ 214
Cdd:PLN03232 1401 SVDVRTDSLIQRTIREEFKSCTMLVIAhrLNTIID-----CDKILVLSSGQVLE 1449
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
131-190 |
1.82e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.18 E-value: 1.82e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 131 GGDLSGGQQQQLAIGRALASRPRLLILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILLV 190
Cdd:PTZ00265 1356 GKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITI 1415
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
21-226 |
3.92e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.01 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 21 SFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITH----------SKPHQRVQSGVayVPQGREIFPR 90
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRlsfeqlqklvSDEWQRNNTDM--LSPGEDDTGR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 91 lTVEENLLMGLSRfsagNARSvpEEIWQLFPVlKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEPTEGIQPSVIK 170
Cdd:PRK10938 101 -TTAEIIQDEVKD----PARC--EQLAQQFGI-TALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQ 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1737198856 171 EIGQVIRSLANRGdMAILLV-------EQFYDFAAELADSYLvmsrgsiVQQGRGENMEQEGV 226
Cdd:PRK10938 173 QLAELLASLHQSG-ITLVLVlnrfdeiPDFVQFAGVLADCTL-------AETGEREEILQQAL 227
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-161 |
1.13e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.58 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 2 LQVSELNQYYGGSHILRGVSFE----AVVGevtcLLGRNGVGKTTLLRCLMGLIPVKGGEVVwQGKSithskphqrVQsg 77
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSlppgGIVG----IIGPNGAGKSTLFKMITGQEQPDSGTIK-IGET---------VK-- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 78 VAYVPQGRE-IFPRLTVEENLLMGLSRFSAGNarsvpeeiwqlfpvlKEMKHR--------RGGD-------LSGGQQQQ 141
Cdd:PRK11819 389 LAYVDQSRDaLDPNKTVWEEISGGLDIIKVGN---------------REIPSRayvgrfnfKGGDqqkkvgvLSGGERNR 453
|
170 180
....*....|....*....|
gi 1737198856 142 LAIGRALASRPRLLILDEPT 161
Cdd:PRK11819 454 LHLAKTLKQGGNVLLLDEPT 473
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-161 |
1.30e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.58 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELnqYYGGSHILRGV--SF--EAVVGevtcLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQgKSIThskphqrvqs 76
Cdd:PRK11819 9 MNRVSKV--VPPKKQILKDIslSFfpGAKIG----VLGLNGAGKSTLLRIMAGVDKEFEGEARPA-PGIK---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 77 gVAYVPQGREIFPRLTVEENLLMGLSRFSAGNARSvpEEIWQLF--------PVLKEM-------KHRRGGD-------- 133
Cdd:PRK11819 72 -VGYLPQEPQLDPEKTVRENVEEGVAEVKAALDRF--NEIYAAYaepdadfdALAAEQgelqeiiDAADAWDldsqleia 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1737198856 134 ---------------LSGGQQQQLAIGRALASRPRLLILDEPT 161
Cdd:PRK11819 149 mdalrcppwdakvtkLSGGERRRVALCRLLLEKPDMLLLDEPT 191
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
16-188 |
1.32e-06 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 48.57 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 16 ILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITHSKPHQRVQ---SGVAYVPQGREIFPRLT 92
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQlrrEHFGFIFQRYHLLSHLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 93 VEENLlmGLSRFSAGNARSVPEEIWQLFPV---LKEMKHRRGGDLSGGQQQQLAIGRALASRPRLLILDEPTEGIQPSVI 169
Cdd:PRK10535 103 AAQNV--EVPAVYAGLERKQRLLRAQELLQrlgLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSG 180
|
170
....*....|....*....
gi 1737198856 170 KEIGQVIRSLANRGDMAIL 188
Cdd:PRK10535 181 EEVMAILHQLRDRGHTVII 199
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-161 |
4.80e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.70 E-value: 4.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 1 MLQVSELNQYYGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMG-LIPVKGGEVVWQGKSITHSKPHQrvqsgva 79
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGeLAPVSGEIGLAKGIKLGYFAQHQ------- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 80 yvpqgreiFPRLTVEENLLMGLSRFSagnarsvPEEIWQlfpvlkEMKHRRGG-------------DLSGGQQQQLAIGR 146
Cdd:PRK10636 385 --------LEFLRADESPLQHLARLA-------PQELEQ------KLRDYLGGfgfqgdkvteetrRFSGGEKARLVLAL 443
|
170
....*....|....*
gi 1737198856 147 ALASRPRLLILDEPT 161
Cdd:PRK10636 444 IVWQRPNLLLLDEPT 458
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
11-190 |
6.92e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.16 E-value: 6.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 11 YGGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPvKG--------------GEVVWQGKSitH-----SKPH 71
Cdd:PRK10938 270 YNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHP-QGysndltlfgrrrgsGETIWDIKK--HigyvsSSLH 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 72 Q--RVQSGVAYVPqgreifprltveenllmgLSRF--SAGNARSVPEEIWQLfpvLKEMKHRRGGD----------LSGG 137
Cdd:PRK10938 347 LdyRVSTSVRNVI------------------LSGFfdSIGIYQAVSDRQQKL---AQQWLDILGIDkrtadapfhsLSWG 405
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1737198856 138 QQQQLAIGRALASRPRLLILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILLV 190
Cdd:PRK10938 406 QQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFV 458
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
29-159 |
1.68e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 44.09 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 29 VTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSITH-SKPHqrvqsgVAYVPQGREIFPRLTVEENLLMGLSRFSAg 107
Cdd:PRK13541 28 ITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNiAKPY------CTYIGHNLGLKLEMTVFENLKFWSEIYNS- 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1737198856 108 nARSVPEEI--WQLFPVLKEMKHRrggdLSGGQQQQLAIGRALASRPRLLILDE 159
Cdd:PRK13541 101 -AETLYAAIhyFKLHDLLDEKCYS----LSSGMQKIVAIARLIACQSDLWLLDE 149
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
12-161 |
1.76e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.24 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 12 GGSHILRGVSFEAVVGEVTCLLGRNGVGKTTLLRcLMGLIPVKG-----------GEVVWQGKSI------THSKPHQRV 74
Cdd:PLN03073 188 GGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLR-YMAMHAIDGipkncqilhveQEVVGDDTTAlqcvlnTDIERTQLL 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 75 QSGVAYVPQGREI-FPRLTVE------------------ENLLMGLSRFSAGNARSVPEEIWQLFPVLKEMKHRRGGDLS 135
Cdd:PLN03073 267 EEEAQLVAQQRELeFETETGKgkgankdgvdkdavsqrlEEIYKRLELIDAYTAEARAASILAGLSFTPEMQVKATKTFS 346
|
170 180
....*....|....*....|....*.
gi 1737198856 136 GGQQQQLAIGRALASRPRLLILDEPT 161
Cdd:PLN03073 347 GGWRMRIALARALFIEPDLLLLDEPT 372
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
134-202 |
2.67e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.82 E-value: 2.67e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1737198856 134 LSGGQQQQLAIGRALASRPR--LLILDEPTEGIQPSVIKEIGQVIRSLANRGDmAILLVE---QFYDFAAELAD 202
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGN-TVLLVEhdeQMISLADRIID 549
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
134-189 |
9.58e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 41.54 E-value: 9.58e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1737198856 134 LSGGQQQQLAIGRALASRPR--LLILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILL 189
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILI 145
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
134-164 |
1.95e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 42.32 E-value: 1.95e-04
10 20 30
....*....|....*....|....*....|.
gi 1737198856 134 LSGGQQQQLAIGRALASRPRLLILDEPTEGI 164
Cdd:PTZ00265 580 LSGGQKQRISIARAIIRNPKILILDEATSSL 610
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
27-206 |
2.19e-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: 40.63 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 27 GEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSIthskphqrvqsgvAYVPQGReifprltveenllmglsrfsa 106
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITP-------------VYKPQYI--------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 107 gnarsvpeeiwqlfpvlkemkhrrggDLSGGQQQQLAIGRALASRPRLLILDEPTEGIQPSVIKEIGQVIRSLANRGDMA 186
Cdd:cd03222 71 --------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKT 124
|
170 180
....*....|....*....|
gi 1737198856 187 ILLVEQFYDFAAELADSYLV 206
Cdd:cd03222 125 ALVVEHDLAVLDYLSDRIHV 144
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
134-189 |
3.35e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 3.35e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1737198856 134 LSGGQQQQLAIGRALAS---RPRLLILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILL 189
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVII 868
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
27-221 |
4.05e-04 |
|
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: 40.66 E-value: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 27 GEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSIThSKPHQRVQSGVAYVPQGREIFPrltveenllmGLSRFSA 106
Cdd:cd03288 47 GQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDIS-KLPLHTLRSRLSIILQDPILFS----------GSIRFNL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737198856 107 GNARSVPEE-IWQLFPV--LKEM-KHRRGG----------DLSGGQQQQLAIGRALASRPRLLILDEPTEGIQPSViKEI 172
Cdd:cd03288 116 DPECKCTDDrLWEALEIaqLKNMvKSLPGGldavvteggeNFSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT-ENI 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1737198856 173 GQ--VIRSLANRGDMAIL-LVEQFYDfaaelADSYLVMSRGSIVQQGRGENM 221
Cdd:cd03288 195 LQkvVMTAFADRTVVTIAhRVSTILD-----ADLVLVLSRGILVECDTPENL 241
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
134-188 |
4.58e-04 |
|
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: 40.29 E-value: 4.58e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1737198856 134 LSGGQQQQLAIGRALASRPR---LLILDEPTEGIQPSVIKEIGQVIRSLANRGDMAIL 188
Cdd:cd03271 170 LSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVV 227
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
134-189 |
5.60e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.77 E-value: 5.60e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1737198856 134 LSGGQQQQLAIGRALASR---PRLLILDEPTEGIQPSVIKEIGQVIRSLANRGDMAILL 189
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVI 888
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-58 |
9.95e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 39.30 E-value: 9.95e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1737198856 17 LRGVSFEAVVGEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEV 58
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEV 79
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
27-66 |
1.17e-03 |
|
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: 39.40 E-value: 1.17e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1737198856 27 GEVTCLLGRNGVGKTTLLRCLMGLIPVKGGEVVWQGKSIT 66
Cdd:COG4615 358 GELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT 397
|
|
| |
