|
Name |
Accession |
Description |
Interval |
E-value |
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
2-233 |
1.26e-114 |
|
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: 327.32 E-value: 1.26e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 2 AAMLEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKYGI 81
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 82 GFVPEERGIFATLSVEENLKLP----PVVASGGMTLDEIYELFPNLYERRTSPGTKLSGGEQQMLAMARILRTGVKVLLL 157
Cdd:COG0410 81 GYVPEGRRIFPSLTVEENLLLGayarRDRAEVRADLERVYELFPRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1610782141 158 DEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPVSELSGRMGELNKVLGV 233
Cdd:COG0410 161 DEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEVREAYLGV 236
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-227 |
2.82e-104 |
|
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: 300.50 E-value: 2.82e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKYGIGFV 84
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 85 PEERGIFATLSVEENLKL---PPVVASGGMTLDEIYELFPNLYERRTSPGTKLSGGEQQMLAMARILRTGVKVLLLDEPT 161
Cdd:cd03224 81 PEGRRIFPELTVEENLLLgayARRRAKRKARLERVYELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1610782141 162 EGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVsnfpvseLSGRMGEL 227
Cdd:cd03224 161 EGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVV-------LEGTAAEL 219
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
5-221 |
5.00e-84 |
|
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: 249.36 E-value: 5.00e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKYGIGFV 84
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 85 PEERGIFATLSVEENLK--LPPVVASGGMTLDEIYELFPNLYERRTSPGTKLSGGEQQMLAMARILRTGVKVLLLDEPTE 162
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLtgLAALPRRSRKIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 163 GLAPVIVQRIGEVLQKL-KSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPVSELS 221
Cdd:TIGR03410 161 GIQPSIIKDIGRVIRRLrAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELD 220
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-212 |
8.63e-60 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 188.16 E-value: 8.63e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 1 MAAMLEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKYG 80
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 81 IGFVPEERGIFATLSVEENLKLPPVVASGGMTLDEI---YELFPNLYERRTSPGTKLSGGEQQMLAMARILRTGVKVLLL 157
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIkwvYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1610782141 158 DEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMV 212
Cdd:PRK11614 162 DEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-224 |
1.43e-49 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 161.77 E-value: 1.43e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDlmPVPLHRTAKYGIGFV 84
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGED--VARDPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 85 PEERGIFATLSVEENLK-------LPPVVASGgmTLDEIYELFpNLYERRTSPGTKLSGGEQQMLAMARILRTGVKVLLL 157
Cdd:COG1131 79 PQEPALYPDLTVRENLRffarlygLPRKEARE--RIDELLELF-GLTDAADRKVGTLSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1610782141 158 DEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPVSELSGRM 224
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-211 |
1.03e-48 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 157.56 E-value: 1.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDlmPVPLHRTAKYGIGFV 84
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKD--IKKEPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 85 PEERGIFATLSVEENLKLppvvaSGGMtldeiyelfpnlyerrtspgtklsggeQQMLAMARILRTGVKVLLLDEPTEGL 164
Cdd:cd03230 79 PEEPSLYENLTVRENLKL-----SGGM---------------------------KQRLALAQALLHDPELLILDEPTSGL 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1610782141 165 APVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQM 211
Cdd:cd03230 127 DPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
3-210 |
9.99e-48 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 157.11 E-value: 9.99e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 3 AMLEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKYGIG 82
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 83 FVPEERGIFATLSVEENLKLppVVASGGMT-------LDEIYELFpNLYERRTSPGTKLSGGEQQMLAMARILRTGVKVL 155
Cdd:COG1137 82 YLPQEASIFRKLTVEDNILA--VLELRKLSkkereerLEELLEEF-GITHLRKSKAYSLSGGERRRVEIARALATNPKFI 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1610782141 156 LLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQ 210
Cdd:COG1137 159 LLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGK 213
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-226 |
1.01e-46 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 155.02 E-value: 1.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 4 MLEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPlhRTAKYGIGF 83
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP--REARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 84 VPEERGIFATLSVEENLKL-----PPVVASGGMTLDEIYELF--PNLYERRTSpgtKLSGGEQQMLAMARILRTGVKVLL 156
Cdd:COG4555 79 LPDERGLYDRLTVRENIRYfaelyGLFDEELKKRIEELIELLglEEFLDRRVG---ELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 157 LDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPVSELSGRMGE 226
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-229 |
1.71e-45 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 151.33 E-value: 1.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLK-SWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKYgIGF 83
Cdd:COG1122 1 IELENLSfSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRK-VGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 84 V---PEeRGIFATlSVEE-------NLKLPPvvasggmtlDEIY-------ELFpNLYERRTSPGTKLSGGEQQMLAMAR 146
Cdd:COG1122 80 VfqnPD-DQLFAP-TVEEdvafgpeNLGLPR---------EEIRerveealELV-GLEHLADRPPHELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 147 ILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPVSELSGRMGE 226
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYEL 227
|
...
gi 1610782141 227 LNK 229
Cdd:COG1122 228 LEE 230
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-212 |
2.16e-45 |
|
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: 151.05 E-value: 2.16e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKYGIG-- 82
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGrt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 83 F-VPEergIFATLSVEENLKLPPVVASGGMTL---------------DEIYELFpNLYERRTSPGTKLSGGEQQMLAMAR 146
Cdd:cd03219 81 FqIPR---LFPELTVLENVMVAAQARTGSGLLlararreereareraEELLERV-GLADLADRPAGELSYGQQRRLEIAR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1610782141 147 ILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMV 212
Cdd:cd03219 157 ALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVI 222
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-210 |
5.29e-45 |
|
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: 150.00 E-value: 5.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKYGIGFV 84
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 85 PEERGIFATLSVEENLKLppVVASGGMT-------LDEIYELFpNLYERRTSPGTKLSGGEQQMLAMARILRTGVKVLLL 157
Cdd:cd03218 81 PQEASIFRKLTVEENILA--VLEIRGLSkkereekLEELLEEF-HITHLRKSKASSLSGGERRRVEIARALATNPKFLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1610782141 158 DEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQ 210
Cdd:cd03218 158 DEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGK 210
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
5-210 |
6.15e-44 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 147.42 E-value: 6.15e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKYGIGFV 84
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLGIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 85 PEERGIFATLSVEENLKLPpVVASGGMTLDEIYELFPNLYER------RTSPGTKLSGGEQQMLAMARILRTGVKVLLLD 158
Cdd:TIGR04406 82 PQEASIFRKLTVEENIMAV-LEIRKDLDRAEREERLEALLEEfqishlRDNKAMSLSGGERRRVEIARALATNPKFILLD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1610782141 159 EPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQ 210
Cdd:TIGR04406 161 EPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGK 212
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-210 |
1.20e-42 |
|
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: 143.38 E-value: 1.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 6 EVSNLKSWY--GESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKYgIGF 83
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRK-VGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 84 V---PEeRGIFATlSVEE-------NLKLPPVVASggMTLDEIYELFpNLYERRTSPGTKLSGGEQQMLAMARILRTGVK 153
Cdd:cd03225 80 VfqnPD-DQFFGP-TVEEevafgleNLGLPEEEIE--ERVEEALELV-GLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1610782141 154 VLLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQ 210
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-212 |
1.27e-40 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 139.40 E-value: 1.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 1 MAAMLEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKYG 80
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 81 IG--F-VPEergIFATLSVEEN-----------------LKLPPVVASGGMTLDEIYEL--FPNLYERRTSPGTKLSGGE 138
Cdd:COG0411 81 IArtFqNPR---LFPELTVLENvlvaaharlgrgllaalLRLPRARREEREARERAEELleRVGLADRADEPAGNLSYGQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1610782141 139 QQMLAMARILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLK-SRGMTVVLVEQNFRFASRIADRFYLMDHGQMV 212
Cdd:COG0411 158 QRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRdERGITILLIEHDMDLVMGLADRIVVLDFGRVI 232
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-210 |
1.41e-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: 136.93 E-value: 1.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMP----VPLHRTAkyg 80
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDledeLPPLRRR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 81 IGFVPEERGIFATLSVEENLKLPpvvasggmtldeiyelfpnlyerrtspgtkLSGGEQQMLAMARILRTGVKVLLLDEP 160
Cdd:cd03229 78 IGMVFQDFALFPHLTVLENIALG------------------------------LSGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1610782141 161 TEGLAPVIVQRIGEVLQKLKSR-GMTVVLVEQNFRFASRIADRFYLMDHGQ 210
Cdd:cd03229 128 TSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-212 |
4.58e-39 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 135.12 E-value: 4.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 4 MLEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPvPLHRTAKY--GI 81
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD-SKKDINKLrrKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 82 GFVPEERGIFATLSVEENLKLPPVVAsGGMTLDEIYELFPNLYER-------RTSPGTkLSGGEQQMLAMARILRTGVKV 154
Cdd:COG1126 80 GMVFQQFNLFPHLTVLENVTLAPIKV-KKMSKAEAEERAMELLERvgladkaDAYPAQ-LSGGQQQRVAIARALAMEPKV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1610782141 155 LLLDEPTEGLAPvivQRIGEVLQ---KLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMV 212
Cdd:COG1126 158 MLFDEPTSALDP---ELVGEVLDvmrDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIV 215
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-212 |
6.18e-39 |
|
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: 133.80 E-value: 6.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTakyGIGFV 84
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERR---NIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 85 PEERGIFATLSVEENLKLPPVVASGGMT-----LDEIYELFPNLYERRTSPGTkLSGGEQQMLAMARILRTGVKVLLLDE 159
Cdd:cd03259 78 FQDYALFPHLTVAENIAFGLKLRGVPKAeirarVRELLELVGLEGLLNRYPHE-LSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1610782141 160 PTEGLAPVIVQRIGEVLQKL-KSRGMTVVLVEQNFRFASRIADRFYLMDHGQMV 212
Cdd:cd03259 157 PLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-210 |
1.18e-38 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 131.60 E-value: 1.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 6 EVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRtAKYGIGFVP 85
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEE-LRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 86 EergifatlsveenlklppvvasggmtldeiyelfpnlyerrtspgtkLSGGEQQMLAMARILRTGVKVLLLDEPTEGLA 165
Cdd:cd00267 80 Q-----------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLD 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1610782141 166 PVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQ 210
Cdd:cd00267 113 PASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-211 |
1.78e-38 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 132.63 E-value: 1.78e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDL--MPVPLHRTAkygIG 82
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLsaMPPPEWRRQ---VA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 83 FVPEERGIFATlSVEENLKLPPVVASGGMTLDEIYELFPNLY------ERRTSpgtKLSGGEQQMLAMARILRTGVKVLL 156
Cdd:COG4619 78 YVPQEPALWGG-TVRDNLPFPFQLRERKFDRERALELLERLGlppdilDKPVE---RLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1610782141 157 LDEPTEGLAPVIVQRIGEVLQKL-KSRGMTVVLVEQNFRFASRIADRFYLMDHGQM 211
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-225 |
6.40e-38 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 133.70 E-value: 6.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 4 MLEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKdlmpvPLHRTAKYGIGF 83
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGE-----PLDPEDRRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 84 VPEERGIFATLSVEEN------LKlppvvasgGMT-------LDEIYELFpNLYERRTSPGTKLSGGEQQMLAMArilrT 150
Cdd:COG4152 76 LPEERGLYPKMKVGEQlvylarLK--------GLSkaeakrrADEWLERL-GLGDRANKKVEELSKGNQQKVQLI----A 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1610782141 151 GV----KVLLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPVSELSGRMG 225
Cdd:COG4152 143 ALlhdpELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFG 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-210 |
7.06e-38 |
|
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: 131.11 E-value: 7.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLM--PVPLHRTAKYgIG 82
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddKKNINELRQK-VG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 83 FVPEERGIFATLSVEENLKLPPVVASGgMTLDEIYELFPNLYER-------RTSPGTkLSGGEQQMLAMARILRTGVKVL 155
Cdd:cd03262 80 MVFQQFNLFPHLTVLENITLAPIKVKG-MSKAEAEERALELLEKvgladkaDAYPAQ-LSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1610782141 156 LLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQ 210
Cdd:cd03262 158 LFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-212 |
6.86e-37 |
|
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: 129.16 E-value: 6.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 4 MLEVSNLKSWY----GESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKY 79
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 80 G--IGFVPEErgIFATL----SVEENLKLPPVVASGGMTLDEIYELFPNLYERRTSPGT-------KLSGGEQQMLAMAR 146
Cdd:cd03257 81 RkeIQMVFQD--PMSSLnprmTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEvlnryphELSGGQRQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1610782141 147 ILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKS-RGMTVVLVEQNFRFASRIADRFYLMDHGQMV 212
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEeLGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-224 |
1.07e-36 |
|
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: 129.15 E-value: 1.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 4 MLEVSNLKSWYGES----QALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKy 79
Cdd:COG1124 1 MLEVRNLSVSYGQGgrrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 80 GIGFVPEErgIFATL----SVEENLKLPPVVASGGMTLDEIYELF------PNLYERRtsPGtKLSGGEQQMLAMARILR 149
Cdd:COG1124 80 RVQMVFQD--PYASLhprhTVDRILAEPLRIHGLPDREERIAELLeqvglpPSFLDRY--PH-QLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1610782141 150 TGVKVLLLDEPTEGLaPVIVQ-RIGEVLQKLK-SRGMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPVSELSGRM 224
Cdd:COG1124 155 LEPELLLLDEPTSAL-DVSVQaEILNLLKDLReERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGP 230
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-212 |
2.92e-36 |
|
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: 127.01 E-value: 2.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRtakygIGFV 84
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNR-----IGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 85 PEERGIFATLSVEENLK-------LPPVVASGgmTLDEIYELFpNLYERRTSPGTKLSGGEQQMLAMARILRTGVKVLLL 157
Cdd:cd03269 76 PEERGLYPKMKVIDQLVylaqlkgLKKEEARR--RIDEWLERL-ELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1610782141 158 DEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMV 212
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-230 |
7.54e-36 |
|
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: 132.33 E-value: 7.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 1 MAAMLEVSNLKSWY--GESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNR---KGVIKLGGKDLMPVPLHR 75
Cdd:COG1123 1 MTPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 76 TAKYgIGFVPEE-RGIFATLSVEENLKLPPVVasGGMTLDEIYELFPNLYE------RRTSPGTKLSGGEQQMLAMARIL 148
Cdd:COG1123 81 RGRR-IGMVFQDpMTQLNPVTVGDQIAEALEN--LGLSRAEARARVLELLEavglerRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 149 RTGVKVLLLDEPTEGLAPVIVQRIGEVLQKL-KSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPVSELSGRMGEL 227
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQAL 237
|
...
gi 1610782141 228 NKV 230
Cdd:COG1123 238 AAV 240
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-213 |
7.96e-36 |
|
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: 124.86 E-value: 7.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 6 EVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKYgIGFVP 85
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARK-IAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 86 EergifatlsveenlklppVVASGGMTldeiyelfpNLYERRTspgTKLSGGEQQMLAMARILRTGVKVLLLDEPTEGLA 165
Cdd:cd03214 80 Q------------------ALELLGLA---------HLADRPF---NELSGGERQRVLLARALAQEPPILLLDEPTSHLD 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1610782141 166 PVIVQRIGEVLQKL-KSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVS 213
Cdd:cd03214 130 IAHQIELLELLRRLaRERGKTVVMVLHDLNLAARYADRVILLKDGRIVA 178
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-212 |
8.19e-36 |
|
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: 127.08 E-value: 8.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 4 MLEVSNLkSW-YGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKYgIG 82
Cdd:COG1120 1 MLEAENL-SVgYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARR-IA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 83 FVPEERGIFATLSVEEnlklppVVASG---------GMT------LDEIYELFpNLYERRTSPGTKLSGGEQQMLAMARI 147
Cdd:COG1120 79 YVPQEPPAPFGLTVRE------LVALGryphlglfgRPSaedreaVEEALERT-GLEHLADRPVDELSGGERQRVLIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1610782141 148 LRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKL-KSRGMTVVLVEQNFRFASRIADRFYLMDHGQMV 212
Cdd:COG1120 152 LAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIV 217
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-220 |
1.80e-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: 125.37 E-value: 1.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGII-----RNRKGVIKLGGKDLM-----PVPLH 74
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYdldvdVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 75 RTakygIGFVPEERGIFAtLSVEENLKLPPVVA--SGGMTLDEIYE-------LFPNLYERrtSPGTKLSGGEQQMLAMA 145
Cdd:cd03260 81 RR----VGMVFQKPNPFP-GSIYDNVAYGLRLHgiKLKEELDERVEealrkaaLWDEVKDR--LHALGLSGGQQQRLCLA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1610782141 146 RILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSRgMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPVSEL 220
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
3-214 |
5.64e-35 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 124.62 E-value: 5.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 3 AMLEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKYGIG 82
Cdd:PRK10895 2 ATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 83 FVPEERGIFATLSVEENLkLPPVVASGGMT-------LDEIYELFpNLYERRTSPGTKLSGGEQQMLAMARILRTGVKVL 155
Cdd:PRK10895 82 YLPQEASIFRRLSVYDNL-MAVLQIRDDLSaeqredrANELMEEF-HIEHLRDSMGQSLSGGERRRVEIARALAANPKFI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1610782141 156 LLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVSN 214
Cdd:PRK10895 160 LLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAH 218
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-210 |
6.18e-35 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 124.43 E-value: 6.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 1 MAAMLEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLmpvplhRTAKYG 80
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP------RRARRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 81 IGFVPEERGIFAT--LSVEEnlklppVVASG-----GMTL----------DEIYELFpNLYERRTSPGTKLSGGEQQMLA 143
Cdd:COG1121 77 IGYVPQRAEVDWDfpITVRD------VVLMGrygrrGLFRrpsradreavDEALERV-GLEDLADRPIGELSGGQQQRVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1610782141 144 MARILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQ 210
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGL 216
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-220 |
8.62e-35 |
|
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: 129.64 E-value: 8.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 2 AAMLEVSNLKSWY-----GESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRT 76
Cdd:COG1123 258 EPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSL 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 77 AKYG--IGFVPE--ERGIFATLSVEENLKLPPVVAsGGMTLDEIYE----------LFPNLYERRtsPGTkLSGGEQQML 142
Cdd:COG1123 338 RELRrrVQMVFQdpYSSLNPRMTVGDIIAEPLRLH-GLLSRAERRErvaellervgLPPDLADRY--PHE-LSGGQRQRV 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1610782141 143 AMARILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSR-GMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPVSEL 220
Cdd:COG1123 414 AIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEV 492
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-210 |
1.82e-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: 122.60 E-value: 1.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYG----ESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKY- 79
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 80 --GIGFVPEERGIFATLSVEENLKLPPVVA--SGGMTLDEIYELFP--NLYERRTSPGTKLSGGEQQMLAMARILRTGVK 153
Cdd:cd03255 81 rrHIGFVFQSFNLLPDLTALENVELPLLLAgvPKKERRERAEELLErvGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1610782141 154 VLLLDEPTEGLAPVIVQRIGEVLQKL-KSRGMTVVLVEQNFRFASRiADRFYLMDHGQ 210
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHDPELAEY-ADRIIELRDGK 217
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-209 |
8.77e-34 |
|
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: 120.72 E-value: 8.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 6 EVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHrtakygIGFVP 85
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR------IGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 86 EERGIFAT--LSVEEnlklppVVASGGMT---------------LDEIYELFpNLYERRTSPGTKLSGGEQQMLAMARIL 148
Cdd:cd03235 75 QRRSIDRDfpISVRD------VVLMGLYGhkglfrrlskadkakVDEALERV-GLSELADRQIGELSGGQQQRVLLARAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1610782141 149 RTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHG 209
Cdd:cd03235 148 VQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
3-188 |
1.86e-33 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 119.51 E-value: 1.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 3 AMLEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKygIG 82
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRR--LA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 83 FVPEERGIFATLSVEENL----KLPPVVASGgMTLDEIYELFpNLYERRTSPGTKLSGGEQQMLAMARILRTGVKVLLLD 158
Cdd:COG4133 79 YLGHADGLKPELTVRENLrfwaALYGLRADR-EAIDEALEAV-GLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLD 156
|
170 180 190
....*....|....*....|....*....|
gi 1610782141 159 EPTEGLAPVIVQRIGEVLQKLKSRGMTVVL 188
Cdd:COG4133 157 EPFTALDAAGVALLAELIAAHLARGGAVLL 186
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-212 |
2.23e-33 |
|
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: 117.91 E-value: 2.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKYGIGFV 84
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 85 PEergifatlsveenlklppvvasggmtldeiyelfpnlyerrtspgtkLSGGEQQMLAMARILRTGVKVLLLDEPTEGL 164
Cdd:cd03216 81 YQ-----------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAAL 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1610782141 165 APVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMV 212
Cdd:cd03216 114 TPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-220 |
8.02e-33 |
|
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: 118.76 E-value: 8.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLmpVPLHRTAKYGI--- 81
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDI--SGLSEAELYRLrrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 82 -GFVPEERGIFATLSVEENLKLPpvvasggmtLDEIYELFPNLYERRTS--------PGTK------LSGGEQQMLAMAR 146
Cdd:cd03261 79 mGMLFQSGALFDSLTVFENVAFP---------LREHTRLSEEEIREIVLekleavglRGAEdlypaeLSGGMKKRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1610782141 147 ILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLK-SRGMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPVSEL 220
Cdd:cd03261 150 ALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKkELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-212 |
1.22e-32 |
|
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: 117.85 E-value: 1.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 4 MLEVSNLKSWY----GESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPlhRTAKY 79
Cdd:cd03266 1 MITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEP--AEARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 80 GIGFVPEERGIFATLSVEENLK-------LPPVVASGgmTLDEIYELF--PNLYERRTSpgtKLSGGEQQMLAMARILRT 150
Cdd:cd03266 79 RLGFVSDSTGLYDRLTARENLEyfaglygLKGDELTA--RLEELADRLgmEELLDRRVG---GFSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1610782141 151 GVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMV 212
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
12-212 |
1.71e-32 |
|
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: 116.97 E-value: 1.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 12 SWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTakygIGFVPEERG-I 90
Cdd:cd03226 8 SYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKS----IGYVMQDVDyQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 91 FATLSVEENLKLP-PVVASGGMTLDEIYELFpNLYERRTSPGTKLSGGEQQMLAMARILRTGVKVLLLDEPTEGLAPVIV 169
Cdd:cd03226 84 LFTDSVREELLLGlKELDAGNEQAETVLKDL-DLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNM 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1610782141 170 QRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMV 212
Cdd:cd03226 163 ERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-221 |
2.40e-32 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 122.43 E-value: 2.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 1 MAAMLEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKdlmPVPLHRTA--- 77
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGE---PVRFRSPRdaq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 78 KYGIGFVPEERGIFATLSVEENLKLPPVVASGGMtLD--EIYELFPNLYER---RTSPGTK---LSGGEQQMLAMARILR 149
Cdd:COG1129 78 AAGIAIIHQELNLVPNLSVAENIFLGREPRRGGL-IDwrAMRRRARELLARlglDIDPDTPvgdLSVAQQQLVEIARALS 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1610782141 150 TGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLV----EQNFrfasRIADRFYLMDHGQMVSNFPVSELS 221
Cdd:COG1129 157 RDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYIshrlDEVF----EIADRVTVLRDGRLVGTGPVAELT 228
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-212 |
5.14e-32 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 117.06 E-value: 5.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 1 MAAMLEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTImgiirNR----------KGVIKLGGKDL-- 68
Cdd:COG1117 8 LEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCL-----NRmndlipgarvEGEILLDGEDIyd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 69 --MPVPLHRTAkygIGFVPEERGIFATlSVEENlklppvVASG----GMT----LDEIYE-------LFPNLYERRTSPG 131
Cdd:COG1117 83 pdVDVVELRRR---VGMVFQKPNPFPK-SIYDN------VAYGlrlhGIKskseLDEIVEeslrkaaLWDEVKDRLKKSA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 132 TKLSGGEQQMLAMARILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSRgMTVVLVEQNFRFASRIADRFYLMDHGQM 211
Cdd:COG1117 153 LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGEL 231
|
.
gi 1610782141 212 V 212
Cdd:COG1117 232 V 232
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-211 |
3.88e-31 |
|
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: 112.91 E-value: 3.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 2 AAMLEVSNLKSWYgesqALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKYGI 81
Cdd:cd03215 2 EPVLEVRGLSVKG----AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 82 GFVPEER---GIFATLSVEENLKLPPVvasggmtldeiyelfpnlyerrtspgtkLSGGEQQMLAMARILRTGVKVLLLD 158
Cdd:cd03215 78 AYVPEDRkreGLVLDLSVAENIALSSL----------------------------LSGGNQQKVVLARWLARDPRVLILD 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1610782141 159 EPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQM 211
Cdd:cd03215 130 EPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-161 |
4.01e-31 |
|
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: 111.97 E-value: 4.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 20 LHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKyGIGFVPEERGIFATLSVEEN 99
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRK-EIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 100 LKLPPVV-----ASGGMTLDEIYELFPNLYERRT---SPGTKLSGGEQQMLAMARILRTGVKVLLLDEPT 161
Cdd:pfam00005 80 LRLGLLLkglskREKDARAEEALEKLGLGDLADRpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-212 |
4.25e-31 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 117.12 E-value: 4.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 1 MAAMLEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHrtaKYG 80
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE---KRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 81 IGFVPEERGIFATLSVEENlklppvVASG----GMTLDEIY-------ELF--PNLYERRtsPGTkLSGGEQQMLAMARI 147
Cdd:COG3842 79 VGMVFQDYALFPHLTVAEN------VAFGlrmrGVPKAEIRarvaellELVglEGLADRY--PHQ-LSGGQQQRVALARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 148 LRTGVKVLLLDEPTEGL-APVIVQRIGEVLQKLKSRGMTVVLV----EQNFRFASRIAdrfyLMDHGQMV 212
Cdd:COG3842 150 LAPEPRVLLLDEPLSALdAKLREEMREELRRLQRELGITFIYVthdqEEALALADRIA----VMNDGRIE 215
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-214 |
6.78e-31 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 113.60 E-value: 6.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 1 MAAMLEVSNLKSWYG----ESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLmpvplhrt 76
Cdd:COG1136 1 MSPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDI-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 77 AKYG-----------IGFVPEERGIFATLSVEENLKLPPVVAsgGMT-------LDEIYELFpNLYERRTSPGTKLSGGE 138
Cdd:COG1136 73 SSLSerelarlrrrhIGFVFQFFNLLPELTALENVALPLLLA--GVSrkerrerARELLERV-GLGDRLDHRPSQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1610782141 139 QQMLAMARILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKL-KSRGMTVVLVEQNFRFASRiADRFYLMDHGQMVSN 214
Cdd:COG1136 150 QQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnRELGTTIVMVTHDPELAAR-ADRVIRLRDGRIVSD 225
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-220 |
1.31e-30 |
|
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: 113.06 E-value: 1.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 4 MLEVSNLKSWYGES----QALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDL--MPVPLHRTA 77
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtlLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 78 KYGIGFVPEERGIFATLSVEENLKLPPVVAsgGMTLDEI----YEL--FPNLYERRTSPGTKLSGGEQQMLAMARILRTG 151
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIA--GVPKAEIeervLELleLVGLEDKADAYPAQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 152 VKVLLLDEPTEGLAPVIVQRIGEVLQKL-KSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPVSEL 220
Cdd:cd03258 159 PKVLLCDEATSALDPETTQSILALLRDInRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-212 |
1.72e-30 |
|
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: 117.94 E-value: 1.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 2 AAMLEVSNLK-SWYGESQ-ALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVP---LHRT 76
Cdd:COG4987 331 GPSLELEDVSfRYPGAGRpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDeddLRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 77 akygIGFVPEERGIFATlSVEENLKLppvvASGGMTLDEIYEL------------FPN-----LYERrtspGTKLSGGEQ 139
Cdd:COG4987 411 ----IAVVPQRPHLFDT-TLRENLRL----ARPDATDEELWAAlervglgdwlaaLPDgldtwLGEG----GRRLSGGER 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1610782141 140 QMLAMARILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLkSRGMTVVLVEQNFRFASRiADRFYLMDHGQMV 212
Cdd:COG4987 478 RRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEA-LAGRTVLLITHRLAGLER-MDRILVLEDGRIV 548
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-212 |
8.55e-30 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 111.24 E-value: 8.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNL-KSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLM---PVPLHRTakyg 80
Cdd:cd03295 1 IEFENVtKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIReqdPVELRRK---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 81 IGFVPEERGIFATLSVEENLKLPPVV-----ASGGMTLDEIYELF---PNLYERRTSpgTKLSGGEQQMLAMARILRTGV 152
Cdd:cd03295 77 IGYVIQQIGLFPHMTVEENIALVPKLlkwpkEKIRERADELLALVgldPAEFADRYP--HELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1610782141 153 KVLLLDEPTEGLAPVIVQRIGEVLQKLKSR-GMTVVLVEQNFRFASRIADRFYLMDHGQMV 212
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIV 215
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-213 |
1.10e-29 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 110.14 E-value: 1.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 4 MLEVSNL-KSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDL--MP---VPLHRTa 77
Cdd:COG2884 1 MIRFENVsKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLsrLKrreIPYLRR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 78 kyGIGFVPEERGIFATLSVEENLKLPPVVAsgGMTLDEIYELFP------NLYERRTSPGTKLSGGEQQMLAMARILRTG 151
Cdd:COG2884 80 --RIGVVFQDFRLLPDRTVYENVALPLRVT--GKSRKEIRRRVRevldlvGLSDKAKALPHELSGGEQQRVAIARALVNR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1610782141 152 VKVLLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVS 213
Cdd:COG2884 156 PELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-220 |
2.45e-29 |
|
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: 109.97 E-value: 2.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNL-KSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLH--RTAKYGI 81
Cdd:cd03256 1 IEVENLsKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKalRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 82 GFVPEERGIFATLSVEENL---KLPPV----VASGGMTLDEIYELFPNL--------YERRTSpgtKLSGGEQQMLAMAR 146
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVlsgRLGRRstwrSLFGLFPKEEKQRALAALervglldkAYQRAD---QLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1610782141 147 ILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKL-KSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPVSEL 220
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-220 |
3.18e-29 |
|
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: 109.00 E-value: 3.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPlhRTAKYGIGFV 84
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP--REVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 85 PEERGIFATLSVEENLKLPPVVAS-GGMTLDE-IYEL--FPNLYERRTSPGTKLSGGEQQMLAMARILRTGVKVLLLDEP 160
Cdd:cd03265 79 FQDLSVDDELTGWENLYIHARLYGvPGAERRErIDELldFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1610782141 161 TEGLAPVIVQRIGEVLQKLKSR-GMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPVSEL 220
Cdd:cd03265 159 TIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
15-210 |
3.82e-29 |
|
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: 107.47 E-value: 3.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 15 GESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKYgIGFVPEERGIFATl 94
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN-IAYVPQDPFLFSG- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 95 SVEENLklppvvasggmtldeiyelfpnlyerrtspgtkLSGGEQQMLAMARILRTGVKVLLLDEPTEGLAPVIVQRIGE 174
Cdd:cd03228 91 TIRENI---------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILE 137
|
170 180 190
....*....|....*....|....*....|....*..
gi 1610782141 175 VLQKLkSRGMTVVLVEQnfRFAS-RIADRFYLMDHGQ 210
Cdd:cd03228 138 ALRAL-AKGKTVIVIAH--RLSTiRDADRIIVLDDGR 171
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-221 |
6.71e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 113.19 E-value: 6.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 4 MLEVSNLKSwygeSQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKdlmPVPLHRTA---KYG 80
Cdd:COG1129 256 VLEVEGLSV----GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGK---PVRIRSPRdaiRAG 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 81 IGFVPEER---GIFATLSVEENLKLP--PVVASGG-MTLDEIYELFPNLYER---RT-SPGTK---LSGGEQQMLAMARI 147
Cdd:COG1129 329 IAYVPEDRkgeGLVLDLSIRENITLAslDRLSRGGlLDRRRERALAEEYIKRlriKTpSPEQPvgnLSGGNQQKVVLAKW 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 148 LRTGVKVLLLDEPTEGlapVIV---QRIGEVLQKLKSRGMTVVLVeqnfrfaS-------RIADRFYLMDHGQMVSNFPV 217
Cdd:COG1129 409 LATDPKVLILDEPTRG---IDVgakAEIYRLIRELAAEGKAVIVI-------SselpellGLSDRILVMREGRIVGELDR 478
|
....
gi 1610782141 218 SELS 221
Cdd:COG1129 479 EEAT 482
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
5-212 |
7.47e-29 |
|
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: 108.58 E-value: 7.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGESQaLHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPlhrTAKYGIGFV 84
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLP---PEKRDISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 85 PEERGIFATLSVEENLKLppvvasgGMTL------------DEIYELF--PNLYERRtsPGTkLSGGEQQMLAMARILRT 150
Cdd:cd03299 77 PQNYALFPHMTVYKNIAY-------GLKKrkvdkkeierkvLEIAEMLgiDHLLNRK--PET-LSGGEQQRVAIARALVV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1610782141 151 GVKVLLLDEPTEGLAPVIVQRIGEVLQKL-KSRGMTVVLVEQNFRFASRIADRFYLMDHGQMV 212
Cdd:cd03299 147 NPKILLLDEPFSALDVRTKEKLREELKKIrKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLI 209
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-220 |
1.07e-28 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 109.89 E-value: 1.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 1 MAAMLEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKdlmPVPLH-RTAKY 79
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGE---PVPSRaRHARQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 80 GIGFVPEERGIFATLSVEENLKLppVVASGGMTLDEIYELFPNLYE------RRTSPGTKLSGGEQQMLAMARILRTGVK 153
Cdd:PRK13537 81 RVGVVPQFDNLDPDFTVRENLLV--FGRYFGLSAAAARALVPPLLEfaklenKADAKVGELSGGMKRRLTLARALVNDPD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1610782141 154 VLLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPVSEL 220
Cdd:PRK13537 159 VLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-220 |
1.89e-28 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 107.49 E-value: 1.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 4 MLEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLM-PVPLHRTAKYGIG 82
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdPKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 83 FVPEERGIFATLSVEENLKLPPVV---ASGGMTLDEIYELFPN--LYERRTSPGTKLSGGEQQMLAMARILRTGVKVLLL 157
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFGPLRvrgASKEEAEKQARELLAKvgLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1610782141 158 DEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPVSEL 220
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVL 223
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
4-210 |
3.23e-28 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 106.18 E-value: 3.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 4 MLEVSNL-KSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKY--G 80
Cdd:TIGR02673 1 MIEFHNVsKAYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 81 IGFVPEERGIFATLSVEENLKLPPVVA-----SGGMTLDEIYELFPNLYERRTSPGTkLSGGEQQMLAMARILRTGVKVL 155
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVALPLEVRgkkerEIQRRVGAALRQVGLEHKADAFPEQ-LSGGEQQRVAIARAIVNSPPLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1610782141 156 LLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQ 210
Cdd:TIGR02673 160 LADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
3-220 |
1.42e-27 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 105.60 E-value: 1.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 3 AMLEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLG------GKDLMPVP-LHR 75
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGditidtARSLSQQKgLIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 76 TAKYGIGFVPEERGIFATLSVEENLKLPPVVASGgMTLDEIYELFPNLYER------RTSPGTKLSGGEQQMLAMARILR 149
Cdd:PRK11264 82 QLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKG-EPKEEATARARELLAKvglagkETSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1610782141 150 TGVKVLLLDEPTEGLAPVIVqriGEVL---QKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPVSEL 220
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELV---GEVLntiRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
19-212 |
8.92e-27 |
|
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: 107.61 E-value: 8.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 19 ALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKYgIGFVPEERGIFATlSVEE 98
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQ-IGVVLQDVFLFSG-TIRE 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 99 NLKLppvvASGGMTLDEIYEL------------FPNLYERRTSP-GTKLSGGEQQMLAMARILRTGVKVLLLDEPTEGLA 165
Cdd:COG2274 568 NITL----GDPDATDEEIIEAarlaglhdfieaLPMGYDTVVGEgGSNLSGGQRQRLAIARALLRNPRILILDEATSALD 643
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1610782141 166 PVIVQRIGEVLQKLKsRGMTVVLVEQnfRFAS-RIADRFYLMDHGQMV 212
Cdd:COG2274 644 AETEAIILENLRRLL-KGRTVIIIAH--RLSTiRLADRIIVLDKGRIV 688
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-212 |
9.28e-27 |
|
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: 102.58 E-value: 9.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGESQ--ALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHrtAKYGIG 82
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKA--ARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 83 FVPEERGIFATLSVEENLK----LPPVVASGGMTLDEIYELFPNLYERRTSPGTKLSGGEQQMLAMARILRTGVKVLLLD 158
Cdd:cd03263 79 YCPQFDALFDELTVREHLRfyarLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1610782141 159 EPTEGLAPVIVQRIGEVLQKLKsRGMTVVLVEQNFRFASRIADRFYLMDHGQMV 212
Cdd:cd03263 159 EPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-212 |
1.15e-26 |
|
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: 101.91 E-value: 1.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDlmpvPLHRTAKYG-IGF 83
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKS----YQKNIEALRrIGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 84 VPEERGIFATLSVEENLKLPPVVASGG-----MTLDEIyelfpNLYERRTSPGTKLSGGEQQMLAMARILRTGVKVLLLD 158
Cdd:cd03268 77 LIEAPGFYPNLTARENLRLLARLLGIRkkridEVLDVV-----GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1610782141 159 EPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMV 212
Cdd:cd03268 152 EPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-209 |
1.42e-26 |
|
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: 102.32 E-value: 1.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHrtaKYGIGFV 84
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH---KRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 85 PEERGIFATLSVEENLKLPPVVAsgGMTLDEIYELFPNL--------YERRtSPgTKLSGGEQQMLAMARILRTGVKVLL 156
Cdd:cd03300 78 FQNYALFPHLTVFENIAFGLRLK--KLPKAEIKERVAEAldlvqlegYANR-KP-SQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1610782141 157 LDEPTEGLAPVIVQRIGEVLQKL-KSRGMTVVLVEQNFRFASRIADRFYLMDHG 209
Cdd:cd03300 154 LDEPLGALDLKLRKDMQLELKRLqKELGITFVFVTHDQEEALTMSDRIAVMNKG 207
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-220 |
2.86e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 102.46 E-value: 2.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 4 MLEVSNLKSWYGE-SQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGG-------KDLMPVplhr 75
Cdd:PRK13639 1 ILETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepikydkKSLLEV---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 76 TAKYGIGFVPEERGIFATlSVEENLKLPPVvaSGGMTLDEIYELFPNL--------YERRtsPGTKLSGGEQQMLAMARI 147
Cdd:PRK13639 77 RKTVGIVFQNPDDQLFAP-TVEEDVAFGPL--NLGLSKEEVEKRVKEAlkavgmegFENK--PPHHLSGGQKKRVAIAGI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1610782141 148 LRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPVSEL 220
Cdd:PRK13639 152 LAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
5-212 |
3.90e-26 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 99.69 E-value: 3.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGES--QALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDlmPVPLHRTAKYGIG 82
Cdd:cd03247 1 LSINNVSFSYPEQeqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVP--VSDLEKALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 83 FVPEERGIFATlSVEENLklppvvasggmtldeiyelfpnlyerrtspGTKLSGGEQQMLAMARILRTGVKVLLLDEPTE 162
Cdd:cd03247 79 VLNQRPYLFDT-TLRNNL------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTV 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1610782141 163 GLAPVIVQRIGEVLQKLkSRGMTVVLVEQNFRFASRiADRFYLMDHGQMV 212
Cdd:cd03247 128 GLDPITERQLLSLIFEV-LKDKTLIWITHHLTGIEH-MDKILFLENGKII 175
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-209 |
6.17e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 102.99 E-value: 6.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGkdlMPVPLH-RTAKYGIGF 83
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG---VPVPARaRLARARIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 84 VPEERGIFATLSVEENLklppvVASG---GMTLDEIYELFPNLYE------RRTSPGTKLSGGEQQMLAMARILRTGVKV 154
Cdd:PRK13536 119 VPQFDNLDLEFTVRENL-----LVFGryfGMSTREIEAVIPSLLEfarlesKADARVSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1610782141 155 LLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHG 209
Cdd:PRK13536 194 LILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAG 248
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
3-212 |
6.79e-26 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 102.84 E-value: 6.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 3 AMLEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPlhrtakygig 82
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLP---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 83 fvPEERGI------FA---TLSVEENLKLPPVVAsgGMTLDEIYEL---------FPNLYERRtsPGTkLSGGEQQMLAM 144
Cdd:COG3839 72 --PKDRNIamvfqsYAlypHMTVYENIAFPLKLR--KVPKAEIDRRvreaaellgLEDLLDRK--PKQ-LSGGQRQRVAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1610782141 145 ARILRTGVKVLLLDEPTEGL-APVIVQRIGEvLQKL-KSRGMTVVLV--EQN--FRFASRIAdrfyLMDHGQMV 212
Cdd:COG3839 145 GRALVREPKVFLLDEPLSNLdAKLRVEMRAE-IKRLhRRLGTTTIYVthDQVeaMTLADRIA----VMNDGRIQ 213
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
5-212 |
7.11e-26 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 100.86 E-value: 7.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGK--DLMPVPLHRTA---KY 79
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSEKAIrllRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 80 GIGFVPEERGIFATLSVEENLKLPPV-VAsgGMT----------------LDEIYELFPNLyerrtspgtkLSGGEQQML 142
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENLIEAPCkVL--GLSkeqarekamkllarlrLTDKADRFPLH----------LSGGQQQRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 143 AMARILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMV 212
Cdd:COG4161 151 AIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRII 220
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
5-189 |
7.85e-26 |
|
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: 104.75 E-value: 7.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLK-SWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKYgIGF 83
Cdd:TIGR02868 335 LELRDLSaGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRR-VSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 84 VPEERGIFATlSVEENLKLppvvASGGMTLDEIY-------------ELFPNLYERRTSPGTKLSGGEQQMLAMARILRT 150
Cdd:TIGR02868 414 CAQDAHLFDT-TVRENLRL----ARPDATDEELWaalervgladwlrALPDGLDTVLGEGGARLSGGERQRLALARALLA 488
|
170 180 190
....*....|....*....|....*....|....*....
gi 1610782141 151 GVKVLLLDEPTEGLAPVIVQRIGEVLQKlKSRGMTVVLV 189
Cdd:TIGR02868 489 DAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLI 526
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
5-210 |
1.51e-25 |
|
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: 99.72 E-value: 1.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTakyGIGFV 84
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER---NVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 85 PEERGIFATLSVEEN----LKLPPVVASGG--------------MTLDEIYELFPNlyerrtspgtKLSGGEQQMLAMAR 146
Cdd:cd03296 80 FQHYALFRHMTVFDNvafgLRVKPRSERPPeaeirakvhellklVQLDWLADRYPA----------QLSGGQRQRVALAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1610782141 147 ILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSR-GMTVVLVEQNFRFASRIADRFYLMDHGQ 210
Cdd:cd03296 150 ALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGR 214
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-212 |
1.93e-25 |
|
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: 103.68 E-value: 1.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 2 AAMLEVSNLK-SWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKYg 80
Cdd:COG4988 334 PPSIELEDVSfSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQ- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 81 IGFVPEERGIFATlSVEENLKLppvvASGGMT------------LDEIYELFPNLYERR-TSPGTKLSGGEQQMLAMARI 147
Cdd:COG4988 413 IAWVPQNPYLFAG-TIRENLRL----GRPDASdeeleaaleaagLDEFVAALPDGLDTPlGEGGRGLSGGQAQRLALARA 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1610782141 148 LRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLkSRGMTVVLV---EQNFRFASRIadrfYLMDHGQMV 212
Cdd:COG4988 488 LLRDAPLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILIthrLALLAQADRI----LVLDDGRIV 550
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
15-212 |
7.28e-25 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 102.17 E-value: 7.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 15 GESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLH--RTAkygIGFVPEERGIFA 92
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLEslRRQ---IGVVPQDTFLFS 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 93 TlSVEENLKLppvvASGGMTLDEIYE------------LFPNLY-----ERrtspGTKLSGGEQQMLAMARILRTGVKVL 155
Cdd:COG1132 428 G-TIRENIRY----GRPDATDEEVEEaakaaqahefieALPDGYdtvvgER----GVNLSGGQRQRIAIARALLKDPPIL 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1610782141 156 LLDEPTEGLAPVIVQRIGEVLQKLkSRGMTVVLVEQnfRFAS-RIADRFYLMDHGQMV 212
Cdd:COG1132 499 ILDEATSALDTETEALIQEALERL-MKGRTTIVIAH--RLSTiRNADRILVLDDGRIV 553
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-209 |
1.07e-24 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 97.85 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 1 MAAMLEVSNL----KSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRt 76
Cdd:COG1116 4 AAPALELRGVskrfPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDR- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 77 akygiGFVPEERGIFATLSVEENLKLPPVVAsgGMTLDEIYEL------------FPNLYerrtsPGTkLSGGEQQMLAM 144
Cdd:COG1116 83 -----GVVFQEPALLPWLTVLDNVALGLELR--GVPKAERRERarellelvglagFEDAY-----PHQ-LSGGMRQRVAI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1610782141 145 ARILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKL-KSRGMTVVLVEQNFRFASRIADRFYLMDHG 209
Cdd:COG1116 150 ARALANDPEVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-206 |
1.18e-24 |
|
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: 97.16 E-value: 1.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGESQ----ALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRtakyg 80
Cdd:cd03293 1 LEVRNVSKTYGGGGgavtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDR----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 81 iGFVPEERGIFATLSVEENLKLPPVVAsgGMTLDEIYELFPNL--------YERRTsPGTkLSGGEQQMLAMARILRTGV 152
Cdd:cd03293 76 -GYVFQQDALLPWLTVLDNVALGLELQ--GVPKAEARERAEELlelvglsgFENAY-PHQ-LSGGMRQRVALARALAVDP 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1610782141 153 KVLLLDEPTEGLAPVIVQRIGEVLQKL-KSRGMTVVLVEQNFRFASRIADRFYLM 206
Cdd:cd03293 151 DVLLLDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-212 |
1.96e-24 |
|
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: 96.17 E-value: 1.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPlhrTAKYGIGFV 84
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLP---PKDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 85 PEERGIFATLSVEENLKLPpvVASGGMTLDEIYEL---------FPNLYERRTSpgtKLSGGEQQMLAMARILRTGVKVL 155
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFG--LKLRKVPKDEIDERvrevaellqIEHLLDRKPK---QLSGGQRQRVALGRAIVREPKVF 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1610782141 156 LLDEPTEGL-APVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMV 212
Cdd:cd03301 153 LMDEPLSNLdAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
5-212 |
2.27e-24 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 96.62 E-value: 2.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGK--DLMPVPLH---RTAKY 79
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSDkaiRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 80 GIGFVPEERGIFATLSVEENLKLPPVVASGgMTLDEIYELFPNLYER-RTSPGT-----KLSGGEQQMLAMARILRTGVK 153
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLIEAPCRVLG-LSKDQALARAEKLLERlRLKPYAdrfplHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1610782141 154 VLLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMV 212
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIV 220
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-220 |
3.43e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 96.52 E-value: 3.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 3 AMLEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIR-----NRKGVIKLGGKDL--MPVPLHR 75
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIfkMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 76 TAKYGIGFVPEErgiFATLSVEENLKLPPVVASGGMTLDEIYE----------LFPNLYERRTSPGTKLSGGEQQMLAMA 145
Cdd:PRK14247 82 RRVQMVFQIPNP---IPNLSIFENVALGLKLNRLVKSKKELQErvrwalekaqLWDEVKDRLDAPAGKLSGGQQQRLCIA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1610782141 146 RILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKsRGMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPVSEL 220
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLDPENTAKIESLFLELK-KDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
7-202 |
5.05e-24 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 94.99 E-value: 5.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 7 VSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKY---GIGF 83
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFrreKLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 84 VPEERGIFATLSVEENLKLPPVVA--SGGMTLDEIYEL--FPNLYERRTSPGTKLSGGEQQMLAMARILRTGVKVLLLDE 159
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGLKYKklSKKEKREKKKEAleKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1610782141 160 PTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRiADR 202
Cdd:TIGR03608 161 PTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAKQ-ADR 202
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
5-212 |
1.05e-23 |
|
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: 99.04 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYG-ESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKYgIGF 83
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQF-INY 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 84 VPEERGIFATlSVEENLKLPpvvASGGMTLDEIY------------ELFPNLYERRTSP-GTKLSGGEQQMLAMARILRT 150
Cdd:TIGR01193 553 LPQEPYIFSG-SILENLLLG---AKENVSQDEIWaaceiaeikddiENMPLGYQTELSEeGSSISGGQKQRIALARALLT 628
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1610782141 151 GVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSRgmTVVLVEQNFRFASRiADRFYLMDHGQMV 212
Cdd:TIGR01193 629 DSKVLILDESTSNLDTITEKKIVNNLLNLQDK--TIIFVAHRLSVAKQ-SDKIIVLDHGKII 687
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
12-212 |
1.77e-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: 93.71 E-value: 1.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 12 SWYGESQALHgVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPlhrTAKYGIGFVPEERGIF 91
Cdd:cd03298 7 RFSYGEQPMH-FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAP---PADRPVSMLFQENNLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 92 ATLSVEEN--------LKLPPV------VASGGMTLDeiyelfpNLYERRtsPGTkLSGGEQQMLAMARILRTGVKVLLL 157
Cdd:cd03298 83 AHLTVEQNvglglspgLKLTAEdrqaieVALARVGLA-------GLEKRL--PGE-LSGGERQRVALARVLVRDKPVLLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1610782141 158 DEPTEGLAPVIVQRIGEVLQKL-KSRGMTVVLVEQNFRFASRIADRFYLMDHGQMV 212
Cdd:cd03298 153 DEPFAALDPALRAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-221 |
2.17e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 97.40 E-value: 2.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 1 MAAMLEVSNL-KSwYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKdlmPVPLH--RTA 77
Cdd:COG3845 2 MPPALELRGItKR-FGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGK---PVRIRspRDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 78 -KYGIGFVPEERGIFATLSVEENLKL--PPvVASGGMTLDEIYELFPNLYER---RTSPGTK---LSGGEQQMLAMARIL 148
Cdd:COG3845 78 iALGIGMVHQHFMLVPNLTVAENIVLglEP-TKGGRLDRKAARARIRELSERyglDVDPDAKvedLSVGEQQRVEILKAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1610782141 149 RTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPVSELS 221
Cdd:COG3845 157 YRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETS 229
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-219 |
3.61e-23 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 94.07 E-value: 3.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 3 AMLEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKYgig 82
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 83 fvpeeRGI---FATLS----VEEnlklppVVASGGMTLDEIYELFPNLYER----------RTSPGTKLSGGEQQMLAMA 145
Cdd:PRK13548 78 -----RAVlpqHSSLSfpftVEE------VVAMGRAPHGLSRAEDDALVAAalaqvdlahlAGRDYPQLSGGEQQRVQLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 146 RIL------RTGVKVLLLDEPTEGLAPVIVQRIGEVLQKL-KSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPVS 218
Cdd:PRK13548 147 RVLaqlwepDGPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPA 226
|
.
gi 1610782141 219 E 219
Cdd:PRK13548 227 E 227
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-229 |
4.05e-23 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 97.04 E-value: 4.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 1 MAAMLEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKYG 80
Cdd:PRK15439 8 APPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 81 IGFVPEERGIFATLSVEEN--LKLP-PVVASGGMTlDEIYELfpNLYERRTSPGTKLSGGEQQMLAMARILRTGVKVLLL 157
Cdd:PRK15439 88 IYLVPQEPLLFPNLSVKENilFGLPkRQASMQKMK-QLLAAL--GCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILIL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1610782141 158 DEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVsnfpvseLSGRMGELNK 229
Cdd:PRK15439 165 DEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIA-------LSGKTADLST 229
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-205 |
5.43e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 93.30 E-value: 5.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 1 MAAMLEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTImgiirNRKGviklggkDLMP-VPLHRTAKY 79
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSI-----NRMN-------DLNPeVTITGSIVY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 80 G-----------------IGFVPEERGIFAtLSVEEN----LKLPPVvaSGGMTLDEIYE-------LFPNLYERRTSPG 131
Cdd:PRK14239 70 NghniysprtdtvdlrkeIGMVFQQPNPFP-MSIYENvvygLRLKGI--KDKQVLDEAVEkslkgasIWDEVKDRLHDSA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1610782141 132 TKLSGGEQQMLAMARILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSRgMTVVLVEQNFRFASRIADR--FYL 205
Cdd:PRK14239 147 LGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRtgFFL 221
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
23-213 |
8.60e-23 |
|
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: 91.97 E-value: 8.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 23 VDLTVgEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDL------MPVPLHRTakyGIGFVPEERGIFATLSV 96
Cdd:cd03297 17 IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrkkINLPPQQR---KIGLVFQQYALFPHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 97 EENLKLP-PVVASGGMTL--DEIYELF--PNLYERRTSpgtKLSGGEQQMLAMARILRTGVKVLLLDEPTEGL-APVIVQ 170
Cdd:cd03297 93 RENLAFGlKRKRNREDRIsvDELLDLLglDHLLNRYPA---QLSGGEKQRVALARALAAQPELLLLDEPFSALdRALRLQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1610782141 171 RIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVS 213
Cdd:cd03297 170 LLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQY 212
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
5-212 |
1.10e-22 |
|
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: 91.88 E-value: 1.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGESQ--ALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKD---LMPVPLHRtaky 79
Cdd:cd03245 3 IEFRNVSFSYPNQEipALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDirqLDPADLRR---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 80 GIGFVPEERGIFATlSVEENLKLPPVVASGGMTL--------DEIYELFPNLYERRTSP-GTKLSGGEQQMLAMARILRT 150
Cdd:cd03245 79 NIGYVPQDVTLFYG-TLRDNITLGAPLADDERILraaelagvTDFVNKHPNGLDLQIGErGRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1610782141 151 GVKVLLLDEPTEGLAPVIVQRIGEVLQKLKsRGMTVVLVEQNFRFASrIADRFYLMDHGQMV 212
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRPSLLD-LVDRIIVMDSGRIV 217
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
19-211 |
1.88e-22 |
|
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: 90.93 E-value: 1.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 19 ALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKY--GIGFVPEERGIFATLSV 96
Cdd:cd03292 16 ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLrrKIGVVFQDFRLLPDRNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 97 EENLKLPPVVAsgGMTLDEIYELFPNLYER-------RTSPgTKLSGGEQQMLAMARILRTGVKVLLLDEPTEGLAPVIV 169
Cdd:cd03292 96 YENVAFALEVT--GVPPREIRKRVPAALELvglshkhRALP-AELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1610782141 170 QRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQM 211
Cdd:cd03292 173 WEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-220 |
2.39e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 91.83 E-value: 2.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 1 MAAMLEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIR-----NRKGVIKLGGK-----DLMP 70
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRniyspDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 71 VPLHRTakygIGFVPEERGIFATLSVEEN----LKLPPVVASGGmTLDEIYE-------LFPNLYERRTSPGTKLSGGEQ 139
Cdd:PRK14267 81 IEVRRE----VGMVFQYPNPFPHLTIYDNvaigVKLNGLVKSKK-ELDERVEwalkkaaLWDEVKDRLNDYPSNLSGGQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 140 QMLAMARILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSRgMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPVSE 219
Cdd:PRK14267 156 QRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRK 234
|
.
gi 1610782141 220 L 220
Cdd:PRK14267 235 V 235
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-209 |
2.50e-22 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 91.59 E-value: 2.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 1 MAAMLEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKYG 80
Cdd:PRK11300 2 SQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 81 IGFVPEERGIFATLSVEENL-----------------KLPPVVASGGMTLDE-IYEL-FPNLYERRTSPGTKLSGGEQQM 141
Cdd:PRK11300 82 VVRTFQHVRLFREMTVIENLlvaqhqqlktglfsgllKTPAFRRAESEALDRaATWLeRVGLLEHANRQAGNLAYGQQRR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1610782141 142 LAMARILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSR-GMTVVLVEQNFRFASRIADRFYLMDHG 209
Cdd:PRK11300 162 LEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
2-209 |
3.04e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 93.75 E-value: 3.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 2 AAMLEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPlHRTAKYGI 81
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALS-ARAASRRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 82 GFVPEERGIFATLSVEENLKL---PPVVASGGMTLDEiyelfPNLYER---RTS-------PGTKLSGGEQQMLAMARIL 148
Cdd:PRK09536 80 ASVPQDTSLSFEFDVRQVVEMgrtPHRSRFDTWTETD-----RAAVERameRTGvaqfadrPVTSLSGGERQRVLLARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1610782141 149 RTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHG 209
Cdd:PRK09536 155 AQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADG 215
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-212 |
3.65e-22 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 91.33 E-value: 3.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 4 MLEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKYgigf 83
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARR---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 84 vpeeRGI--------FAtLSVEEnlklppVVASGGMTLDEIYELFPNL------------YERRTSPGtkLSGGEQQMLA 143
Cdd:COG4559 77 ----RAVlpqhsslaFP-FTVEE------VVALGRAPHGSSAAQDRQIvrealalvglahLAGRSYQT--LSGGEQQRVQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1610782141 144 MARIL-------RTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMV 212
Cdd:COG4559 144 LARVLaqlwepvDGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLV 219
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
5-224 |
7.54e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 93.17 E-value: 7.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLkSWYGES--QALHGVDLTVGEGEtitILGRNGV---GKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKY 79
Cdd:COG3845 258 LEVENL-SVRDDRgvPALKDVSLEVRAGE---ILGIAGVagnGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 80 GIGFVPEER---GIFATLSVEENLKL-----PPVVASGGMTLDEIYELFPNLYER---RT-SPGTK---LSGGEQQMLAM 144
Cdd:COG3845 334 GVAYIPEDRlgrGLVPDMSVAENLILgryrrPPFSRGGFLDRKAIRAFAEELIEEfdvRTpGPDTParsLSGGNQQKVIL 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 145 ARILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPVSELS--- 221
Cdd:COG3845 414 ARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEATree 493
|
....
gi 1610782141 222 -GRM 224
Cdd:COG3845 494 iGLL 497
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-220 |
1.33e-21 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 89.04 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 4 MLEVSNLKSWYGEsQALHgVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPlhrtakygigf 83
Cdd:COG3840 1 MLRLDDLTYRYGD-FPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 84 vPEERGI---------FATLSVEEN--LKLPPvvasgGMTLDE--------------IYELFpnlyERRtsPGTkLSGGE 138
Cdd:COG3840 68 -PAERPVsmlfqennlFPHLTVAQNigLGLRP-----GLKLTAeqraqveqalervgLAGLL----DRL--PGQ-LSGGQ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 139 QQMLAMARILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKL-KSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPV 217
Cdd:COG3840 135 RQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELcRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPT 214
|
...
gi 1610782141 218 SEL 220
Cdd:COG3840 215 AAL 217
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
5-227 |
1.43e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 89.84 E-value: 1.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTImgiirNR----------KGVIKLGGKDLM----- 69
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCF-----NRlndlipgfrvEGKVTFHGKNLYapdvd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 70 PVPLHRTakygIGFVPEERGIFATlSVEENLKLPPVVASGGMTLDEIYE-------LFPNLYERRTSPGTKLSGGEQQML 142
Cdd:PRK14243 86 PVEVRRR----IGMVFQKPNPFPK-SIYDNIAYGARINGYKGDMDELVErslrqaaLWDEVKDKLKQSGLSLSGGQQQRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 143 AMARILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSRgMTVVLVEQNFRFASRIADR--FYlmdhgqmvsNFPVSEL 220
Cdd:PRK14243 161 CIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSDMtaFF---------NVELTEG 230
|
....*..
gi 1610782141 221 SGRMGEL 227
Cdd:PRK14243 231 GGRYGYL 237
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
5-188 |
1.52e-21 |
|
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: 88.18 E-value: 1.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAkyGIGFV 84
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHE--NILYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 85 PEERGIFATLSVEENLK-LPPVVASGGMTLDEIYELFpNLYERRTSPGTKLSGGEQQMLAMARILRTGVKVLLLDEPTEG 163
Cdd:TIGR01189 79 GHLPGLKPELSALENLHfWAAIHGGAQRTIEDALAAV-GLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170 180
....*....|....*....|....*
gi 1610782141 164 LAPVIVQRIGEVLQKLKSRGMTVVL 188
Cdd:TIGR01189 158 LDKAGVALLAGLLRAHLARGGIVLL 182
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
12-213 |
2.50e-21 |
|
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: 88.44 E-value: 2.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 12 SWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKyGIGFVPEERGIF 91
Cdd:cd03254 11 SYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRS-MIGVVLQDTFLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 92 ATlSVEENLKLPP--------VVASGGMTLDEIYELFPNLYERRTSP-GTKLSGGEQQMLAMARILRTGVKVLLLDEPTE 162
Cdd:cd03254 90 SG-TIMENIRLGRpnatdeevIEAAKEAGAHDFIMKLPNGYDTVLGEnGGNLSQGERQLLAIARAMLRDPKILILDEATS 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1610782141 163 GLAPVIVQRIGEVLQKLKsRGMTVVLVeqnfrfASRI-----ADRFYLMDHGQMVS 213
Cdd:cd03254 169 NIDTETEKLIQEALEKLM-KGRTSIII------AHRLstiknADKILVLDDGKIIE 217
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
5-189 |
2.70e-21 |
|
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: 91.58 E-value: 2.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWY-GESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKyGIGF 83
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRD-QIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 84 VPEERGIFATlSVEENLKLPPVVASGGMT--------LDEIYELFPNLYERRTSP-GTKLSGGEQQMLAMARILRTGVKV 154
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENIRLARPDASDAEIrealeragLDEFVAALPQGLDTPIGEgGAGLSGGQAQRLALARAFLRDAPL 479
|
170 180 190
....*....|....*....|....*....|....*
gi 1610782141 155 LLLDEPTEGLAPVIVQRIGEVLQKLkSRGMTVVLV 189
Cdd:TIGR02857 480 LLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLV 513
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-221 |
4.20e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 91.00 E-value: 4.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 1 MAAMLEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKYG 80
Cdd:PRK09700 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 81 IGFVPEERGIFATLSVEENL---KLPPVVASGGMTLD--EIYELFPNLYER---RTSPGTK---LSGGEQQMLAMARILR 149
Cdd:PRK09700 82 IGIIYQELSVIDELTVLENLyigRHLTKKVCGVNIIDwrEMRVRAAMMLLRvglKVDLDEKvanLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1610782141 150 TGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPVSELS 221
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVS 233
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
14-212 |
8.96e-21 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 86.82 E-value: 8.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 14 YGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLhrtakyGIGFVPEergifat 93
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGL------GGGFNPE------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 94 LSVEENLKLppVVASGGMTLDEIYELFPNLYE------RRTSPGTKLSGGEQQMLAMARILRTGVKVLLLDEpteglapV 167
Cdd:cd03220 99 LTGRENIYL--NGRLLGLSRKEIDEKIDEIIEfselgdFIDLPVKTYSSGMKARLAFAIATALEPDILLIDE-------V 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1610782141 168 I-------VQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMV 212
Cdd:cd03220 170 LavgdaafQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
4-233 |
9.99e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 86.94 E-value: 9.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 4 MLEVSNLkSWYGESQALHgVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDlmpvplHRT---AKYG 80
Cdd:PRK10771 1 MLKLTDI-TWLYHHLPMR-FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD------HTTtppSRRP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 81 IGFVPEERGIFATLSVEEN--LKLPP---VVASGGMTLDEIYEL--FPNLYERRtsPGtKLSGGEQQMLAMARILRTGVK 153
Cdd:PRK10771 73 VSMLFQENNLFSHLTVAQNigLGLNPglkLNAAQREKLHAIARQmgIEDLLARL--PG-QLSGGQRQRVALARCLVREQP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 154 VLLLDEPTEGLAPVIVQrigEVLQKLKS----RGMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPVSEL-SGRMGElN 228
Cdd:PRK10771 150 ILLLDEPFSALDPALRQ---EMLTLVSQvcqeRQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELlSGKASA-S 225
|
....*
gi 1610782141 229 KVLGV 233
Cdd:PRK10771 226 ALLGI 230
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
5-232 |
1.14e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 88.99 E-value: 1.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVplH-RTAKygIGF 83
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL--HaRDRK--VGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 84 VPEERGIFATLSVEEN----LKLPP--------VVASGGMTLDEIYELfPNLYERRTSpgtKLSGGEQQMLAMARILRTG 151
Cdd:PRK10851 79 VFQHYALFRHMTVFDNiafgLTVLPrrerpnaaAIKAKVTQLLEMVQL-AHLADRYPA---QLSGGQKQRVALARALAVE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 152 VKVLLLDEPTEGLAPVIVQRIGEVLQKLKSR-GMTVVLVEQNFRFASRIADRFYLMDHG--------QMVSNFPVSELSG 222
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGnieqagtpDQVWREPATRFVL 234
|
250
....*....|.
gi 1610782141 223 R-MGELNKVLG 232
Cdd:PRK10851 235 EfMGEVNRLQG 245
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-212 |
1.20e-20 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 89.12 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 4 MLEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAkygIGF 83
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRP---INM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 84 VPEERGIFATLSVEENL-------KLPPvvASGGMTLDEIYELFpNLYERRTSPGTKLSGGEQQMLAMARILRTGVKVLL 156
Cdd:PRK11607 96 MFQSYALFPHMTVEQNIafglkqdKLPK--AEIASRVNEMLGLV-HMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1610782141 157 LDEPTEGLAPVIVQRIG-EVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMV 212
Cdd:PRK11607 173 LDEPMGALDKKLRDRMQlEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-220 |
1.41e-20 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 88.21 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 4 MLEVSNL-KSWY---GESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVP---LhRT 76
Cdd:COG1135 1 MIELENLsKTFPtkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSereL-RA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 77 AKYGIGFVPEErgiFATLS---VEENLKLPPVVAsgGMTLDEI----YEL--FPNLYERRTSPGTKLSGGEQQMLAMARI 147
Cdd:COG1135 80 ARRKIGMIFQH---FNLLSsrtVAENVALPLEIA--GVPKAEIrkrvAELleLVGLSDKADAYPSQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1610782141 148 LRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSR-GMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPVSEL 220
Cdd:COG1135 155 LANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDV 228
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
23-223 |
2.27e-20 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 87.85 E-value: 2.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 23 VDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDL------MPVPLHRTAkygIGFVPEERGIFATLSV 96
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdsargIFLPPHRRR---IGYVFQEARLFPHLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 97 EENLK-----LPPvvASGGMTLDEIYELF--PNLYERRtsPGTkLSGGEQQMLAMARILRTGVKVLLLDEPtegLAPVIV 169
Cdd:COG4148 95 RGNLLygrkrAPR--AERRISFDEVVELLgiGHLLDRR--PAT-LSGGERQRVAIGRALLSSPRLLLMDEP---LAALDL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1610782141 170 QRIGEV---LQKLKSR-GMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPVSELSGR 223
Cdd:COG4148 167 ARKAEIlpyLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-212 |
2.82e-20 |
|
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: 87.03 E-value: 2.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 4 MLEVSNLKSWY----GESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNR---KGVIKLGGKDLMPVPLHRT 76
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 77 AKYgigfvpeeRG-----IF----ATL--------SVEEnlklpPVVASGGMTLDEIY----ELF-----PNLYERRTS- 129
Cdd:COG0444 81 RKI--------RGreiqmIFqdpmTSLnpvmtvgdQIAE-----PLRIHGGLSKAEAReraiELLervglPDPERRLDRy 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 130 PGTkLSGGEQQ--MLAMARILRtgVKVLLLDEPTEGLaPVIVQR-IGEVLQKL-KSRGMTVVLVEQNFRFASRIADRFYL 205
Cdd:COG0444 148 PHE-LSGGMRQrvMIARALALE--PKLLIADEPTTAL-DVTIQAqILNLLKDLqRELGLAILFITHDLGVVAEIADRVAV 223
|
....*..
gi 1610782141 206 MDHGQMV 212
Cdd:COG0444 224 MYAGRIV 230
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-216 |
3.50e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 88.58 E-value: 3.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 4 MLEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGgkdlmpvplhRTAKygIGF 83
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG----------ETVK--IGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 84 VPEERgifATLSVEENLklppvvasggmtLDEIYELFPNLYERR---------------TSPGTKLSGGEQQMLAMARIL 148
Cdd:COG0488 383 FDQHQ---EELDPDKTV------------LDELRDGAPGGTEQEvrgylgrflfsgddaFKPVGVLSGGEKARLALAKLL 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1610782141 149 RTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKsrGmTVVLVEQNFRFASRIADRFYLMDHGQmVSNFP 216
Cdd:COG0488 448 LSPPNVLLLDEPTNHLDIETLEALEEALDDFP--G-TVLLVSHDRYFLDRVATRILEFEDGG-VREYP 511
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
4-188 |
3.65e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 84.93 E-value: 3.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 4 MLEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDlMPVPLHRTAKYGIGf 83
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD-IDDPDVAEACHYLG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 84 vpEERGIFATLSVEENLK----------LPPVVASGGMTLDEIYELfpnlyerrtsPGTKLSGGEQQMLAMARILRTGVK 153
Cdd:PRK13539 80 --HRNAMKPALTVAENLEfwaaflggeeLDIAAALEAVGLAPLAHL----------PFGYLSAGQKRRVALARLLVSNRP 147
|
170 180 190
....*....|....*....|....*....|....*
gi 1610782141 154 VLLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVL 188
Cdd:PRK13539 148 IWILDEPTAALDAAAVALFAELIRAHLAQGGIVIA 182
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
4-220 |
4.81e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 86.01 E-value: 4.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 4 MLEVSNLKSWY-GESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKY-GI 81
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFvGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 82 GFVPEERGIFATlSVEENLKLPPVvasgGMTLDE------IYELFP--NLYERRTSPGTKLSGGEQQMLAMARILRTGVK 153
Cdd:PRK13652 83 VFQNPDDQIFSP-TVEQDIAFGPI----NLGLDEetvahrVSSALHmlGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1610782141 154 VLLLDEPTEGLAPVIVQRIGEVLQKL-KSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPVSEL 220
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELIDFLNDLpETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
5-222 |
4.91e-20 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 85.79 E-value: 4.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPV------------- 71
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 72 --PLHRTAkygIGFVPEERGIFATLSVEENLKLPPVVASG-----GMTLDEIYELFPNLYER-RTSPGTKLSGGEQQMLA 143
Cdd:PRK10619 86 qlRLLRTR---LTMVFQHFNLWSHMTVLENVMEAPIQVLGlskqeARERAVKYLAKVGIDERaQGKYPVHLSGGQQQRVS 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1610782141 144 MARILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPVSELSG 222
Cdd:PRK10619 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFG 241
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-219 |
5.50e-20 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 86.78 E-value: 5.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 4 MLEVSNL-KSWYGES---QALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLM--PVPLHRTA 77
Cdd:PRK11153 1 MIELKNIsKVFPQGGrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTalSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 78 KYGIGFVPEErgiFATLS---VEENLKLPPVVAsgGMTLDEIY----ELFP--NLYERRTSPGTKLSGGEQQMLAMARIL 148
Cdd:PRK11153 81 RRQIGMIFQH---FNLLSsrtVFDNVALPLELA--GTPKAEIKarvtELLElvGLSDKADRYPAQLSGGQKQRVAIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1610782141 149 RTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSR-GMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPVSE 219
Cdd:PRK11153 156 ASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSE 227
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
3-220 |
6.73e-20 |
|
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: 85.24 E-value: 6.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 3 AMLEVSNLKSWY---------GESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPV-P 72
Cdd:TIGR02769 1 SLLEVRDVTHTYrtgglfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 73 LHRTA---------KYGIGFVPEERGIFATLSVE----ENLKLPPVVASGGMTLDEIyELFPNLYERRTSpgtKLSGGEQ 139
Cdd:TIGR02769 81 KQRRAfrrdvqlvfQDSPSAVNPRMTVRQIIGEPlrhlTSLDESEQKARIAELLDMV-GLRSEDADKLPR---QLSGGQL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 140 QMLAMARILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSR-GMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPVS 218
Cdd:TIGR02769 157 QRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAfGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVA 236
|
..
gi 1610782141 219 EL 220
Cdd:TIGR02769 237 QL 238
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
5-212 |
8.04e-20 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 83.73 E-value: 8.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNR--KGVIKLGGKDLMPVPLHRTAKYGIg 82
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKGEDITDLPPEERARLGI- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 83 fvpeergifaTLSVEENLKLPpvvasgGMTLDEiyelfpnlYERRTSPGtkLSGGEQQMLAMARILRTGVKVLLLDEPTE 162
Cdd:cd03217 80 ----------FLAFQYPPEIP------GVKNAD--------FLRYVNEG--FSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1610782141 163 GLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRI-ADRFYLMDHGQMV 212
Cdd:cd03217 134 GLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIV 184
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
5-188 |
8.44e-20 |
|
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: 83.70 E-value: 8.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVP--LHRTAKYgIG 82
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRdsIARGLLY-LG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 83 FVPeerGIFATLSVEENLKLPPVVASGGMTLDEIYELFPNLYERRtsPGTKLSGGEQQMLAMARILRTGVKVLLLDEPTE 162
Cdd:cd03231 80 HAP---GIKTTLSVLENLRFWHADHSDEQVEEALARVGLNGFEDR--PVAQLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170 180
....*....|....*....|....*.
gi 1610782141 163 GLAPVIVQRIGEVLQKLKSRGMTVVL 188
Cdd:cd03231 155 ALDKAGVARFAEAMAGHCARGGMVVL 180
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-211 |
9.44e-20 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 84.06 E-value: 9.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 1 MAA--MLEVSNLKSWYGESQA----LHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLH 74
Cdd:PRK10584 1 MPAenIVEVHHLKKSVGQGEHelsiLTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 75 RTAKY---GIGFVPEERGIFATLSVEENLKLPPVV--ASGGMTLDEIYELFPN--LYERRTSPGTKLSGGEQQMLAMARI 147
Cdd:PRK10584 81 ARAKLrakHVGFVFQSFMLIPTLNALENVELPALLrgESSRQSRNGAKALLEQlgLGKRLDHLPAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1610782141 148 LRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKL-KSRGMTVVLVEQNFRFASRIADRFYLMDhGQM 211
Cdd:PRK10584 161 FNGRPDVLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDLQLAARCDRRLRLVN-GQL 224
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
23-223 |
1.30e-19 |
|
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: 85.93 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 23 VDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDL------MPVPLHRTAkygIGFVPEERGIFATLSV 96
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsrkgIFLPPEKRR---IGYVFQEARLFPHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 97 EENLKL---PPVVASGGMTLDEIYELF--PNLYERRTSpgtKLSGGEQQMLAMARILRTGVKVLLLDEPtegLAPVIVQR 171
Cdd:TIGR02142 93 RGNLRYgmkRARPSERRISFERVIELLgiGHLLGRLPG---RLSGGEKQRVAIGRALLSSPRLLLMDEP---LAALDDPR 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1610782141 172 IGEVLQKLKSR----GMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPVSELSGR 223
Cdd:TIGR02142 167 KYEILPYLERLhaefGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWAS 222
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-216 |
1.46e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 86.70 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 1 MAAMLEVSNLKSWY--GESQ--ALHGVDLTVGEGETITILGRNGVGKTTtLRTIMGII-RNRKGVIKLGGKD---LMPVP 72
Cdd:PRK10535 1 MTALLELKDIRRSYpsGEEQveVLKGISLDIYAGEMVAIVGASGSGKST-LMNILGCLdKPTSGTYRVAGQDvatLDADA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 73 LHRTAKYGIGFVPEERGIFATLSVEENLKLPPVVASGGMT--LDEIYELFP--NLYERRTSPGTKLSGGEQQMLAMARIL 148
Cdd:PRK10535 80 LAQLRREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKqrLLRAQELLQrlGLEDRVEYQPSQLSGGQQQRVSIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1610782141 149 RTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRiADRFYLMDHGQMVSNFP 216
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPP 226
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-212 |
1.55e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 84.33 E-value: 1.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 4 MLEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGK------DLMPVPLHRTA 77
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 78 KYgIGFVPEERGIFATLSVEENLKLPpvVASGGMT----LDEIYE-------LFPNLYERRTSPGTKLSGGEQQMLAMAR 146
Cdd:PRK14246 90 KE-VGMVFQQPNPFPHLSIYDNIAYP--LKSHGIKekreIKKIVEeclrkvgLWKEVYDRLNSPASQLSGGQQQRLTIAR 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1610782141 147 ILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSRgMTVVLVEQNFRFASRIADRFYLMDHGQMV 212
Cdd:PRK14246 167 ALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELV 231
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-212 |
2.46e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 83.52 E-value: 2.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 4 MLEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKYgIGF 83
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARR-LAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 84 VPEErgifatLSVEENLKLPPVVASG---------------------GMTLDEIYElfpnLYERRTspgTKLSGGEQQML 142
Cdd:PRK11231 81 LPQH------HLTPEGITVRELVAYGrspwlslwgrlsaednarvnqAMEQTRINH----LADRRL---TDLSGGQRQRA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 143 AMARILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMV 212
Cdd:PRK11231 148 FLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVM 217
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
5-211 |
2.69e-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: 81.49 E-value: 2.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGESQA--LHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLhrtAKYG-- 80
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDP---NELGdh 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 81 IGFVPEERGIFATlSVEENLklppvvasggmtldeiyelfpnlyerrtspgtkLSGGEQQMLAMARILRTGVKVLLLDEP 160
Cdd:cd03246 78 VGYLPQDDELFSG-SIAENI---------------------------------LSGGQRQRLGLARALYGNPRILVLDEP 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1610782141 161 TEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRfASRIADRFYLMDHGQM 211
Cdd:cd03246 124 NSHLDVEGERALNQAIAALKAAGATRIVIAHRPE-TLASADRILVLEDGRV 173
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
5-219 |
3.30e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 85.44 E-value: 3.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSwygesQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKYGIGFV 84
Cdd:PRK10762 258 LKVDNLSG-----PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIVYI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 85 PEER---GIFATLSVEENLKLPPVVA---SGG--------MTLDEIYELFPNLYERRTSPGTKLSGGEQQMLAMARILRT 150
Cdd:PRK10762 333 SEDRkrdGLVLGMSVKENMSLTALRYfsrAGGslkhadeqQAVSDFIRLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMT 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1610782141 151 GVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPVSE 219
Cdd:PRK10762 413 RPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTREQ 481
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-212 |
6.77e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 82.97 E-value: 6.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 4 MLEVSNLKSWYGE-SQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKdlmpvPLHRTAK---- 78
Cdd:PRK13636 5 ILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGK-----PIDYSRKglmk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 79 ----YGIGFVPEERGIFATlSVEENLKLPPVvaSGGMTLDEIYELFPNLYER------RTSPGTKLSGGEQQMLAMARIL 148
Cdd:PRK13636 80 lresVGMVFQDPDNQLFSA-SVYQDVSFGAV--NLKLPEDEVRKRVDNALKRtgiehlKDKPTHCLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1610782141 149 RTGVKVLLLDEPTEGLAPVIVQRIGE-VLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMV 212
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKlLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVI 221
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-220 |
8.69e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 82.45 E-value: 8.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 19 ALHGVDLTVG-EGETI--------------TILGRNGVGKTTTLRTImgiirNR----------KGVIKLGGKDLMPVPL 73
Cdd:PRK14271 21 AMAAVNLTLGfAGKTVldqvsmgfparavtSLMGPTGSGKTTFLRTL-----NRmndkvsgyrySGDVLLGGRSIFNYRD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 74 HRTAKYGIGFVPEERGIFAtLSVEENL-------KLPPVVASGGMTLDEIYE--LFPNLYERRTSPGTKLSGGEQQMLAM 144
Cdd:PRK14271 96 VLEFRRRVGMLFQRPNPFP-MSIMDNVlagvrahKLVPRKEFRGVAQARLTEvgLWDAVKDRLSDSPFRLSGGQQQLLCL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1610782141 145 ARILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSRgMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPVSEL 220
Cdd:PRK14271 175 ARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-212 |
9.29e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 81.67 E-value: 9.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 1 MAAMLEVSN--------------LKSW--------YGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRK 58
Cdd:COG1134 1 MSSMIEVENvsksyrlyhepsrsLKELllrrrrtrREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 59 GVIKLGGKdlMPVPLhrtaKYGIGFVPEergifatLSVEENLKLppvvaSG---GMTLDEIYELFPNLYE---------- 125
Cdd:COG1134 81 GRVEVNGR--VSALL----ELGAGFHPE-------LTGRENIYL-----NGrllGLSRKEIDEKFDEIVEfaelgdfidq 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 126 --RRTSPGtklsggeqqM---LAMAriLRTGVK--VLLLDeptEGLA---PVIVQRIGEVLQKLKSRGMTVVLVEQNFRF 195
Cdd:COG1134 143 pvKTYSSG---------MrarLAFA--VATAVDpdILLVD---EVLAvgdAAFQKKCLARIRELRESGRTVIFVSHSMGA 208
|
250
....*....|....*..
gi 1610782141 196 ASRIADRFYLMDHGQMV 212
Cdd:COG1134 209 VRRLCDRAIWLEKGRLV 225
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-221 |
1.08e-18 |
|
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: 84.11 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 4 MLEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIR--NRKGVIKLGGKDLMPVPLHRTAKYGI 81
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 82 GFVPEERGIFATLSVEENLKLPPVVASGG--MTLDEIYELFPNLYER-------RTSPGTKLSGGEQQMLAMARILRTGV 152
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNEITLPGgrMAYNAMYLRAKNLLRElqldadnVTRPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1610782141 153 KVLLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPVSELS 221
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMS 229
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-210 |
1.36e-18 |
|
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: 79.03 E-value: 1.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGgkdlmpvplhrtAKYGIGFV 84
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG------------STVKIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 85 PeergifatlsveenlklppvvasggmtldeiyelfpnlyerrtspgtKLSGGEQQMLAMARILRTGVKVLLLDEPTEGL 164
Cdd:cd03221 69 E-----------------------------------------------QLSGGEKMRLALAKLLLENPNLLLLDEPTNHL 101
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1610782141 165 APVIVQRIGEVLQKLKSrgmTVVLVEQNFRFASRIADRFYLMDHGQ 210
Cdd:cd03221 102 DLESIEALEEALKEYPG---TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
16-212 |
1.66e-18 |
|
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: 81.05 E-value: 1.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 16 ESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKYgIGFVPEERGIFATlS 95
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQ-IGLVSQEPVLFDG-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 96 VEENLKL--PPVV------ASGGMTLDEIYELFPNLYERRTSP-GTKLSGGEQQMLAMARILRTGVKVLLLDEPTEGLAP 166
Cdd:cd03249 93 IAENIRYgkPDATdeeveeAAKKANIHDFIMSLPDGYDTLVGErGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1610782141 167 VIVQRIGEVLQKLKsRGMTVVLVeqnfrfASRI-----ADRFYLMDHGQMV 212
Cdd:cd03249 173 ESEKLVQEALDRAM-KGRTTIVI------AHRLstirnADLIAVLQNGQVV 216
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
14-214 |
3.39e-18 |
|
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: 80.07 E-value: 3.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 14 YGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKdlmpVPLHRTAKY--GIGFVPEERGIF 91
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL----VPWKRRKKFlrRIGVVFGQKTQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 92 A-TLSVEENLKLppvvasggmtLDEIYELFPNLYERRT--------------SPGTKLSGGEQQMLAMARILRTGVKVLL 156
Cdd:cd03267 107 WwDLPVIDSFYL----------LAAIYDLPPARFKKRLdelselldleelldTPVRQLSLGQRMRAEIAAALLHEPEILF 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1610782141 157 LDEPTEGLAPVIVQRIGEVLQKL-KSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVSN 214
Cdd:cd03267 177 LDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYD 235
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-211 |
3.46e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 80.83 E-value: 3.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 1 MAAMLEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGV---IKLGG----------KD 67
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAgshIELLGrtvqregrlaRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 68 LmpvplhRTAKYGIGFVPEERGIFATLSVEENLklppVVASGGMT--LDEIYELFPNLYERR-----TSPG--------- 131
Cdd:PRK09984 81 I------RKSRANTGYIFQQFNLVNRLSVLENV----LIGALGSTpfWRTCFSWFTREQKQRalqalTRVGmvhfahqrv 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 132 TKLSGGEQQMLAMARILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKL-KSRGMTVVLVEQNFRFASRIADRFYLMDHGQ 210
Cdd:PRK09984 151 STLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQGH 230
|
.
gi 1610782141 211 M 211
Cdd:PRK09984 231 V 231
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
11-214 |
4.40e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 79.53 E-value: 4.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 11 KSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLM-----PVPLHRTAkygIGFVP 85
Cdd:PRK10908 9 KAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrlknrEVPFLRRQ---IGMIF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 86 EERGIFATLSVEENLKLPPVVAsgGMTLDEIYELFP------NLYERRTSPGTKLSGGEQQMLAMARILRTGVKVLLLDE 159
Cdd:PRK10908 86 QDHHLLMDRTVYDNVAIPLIIA--GASGDDIRRRVSaaldkvGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1610782141 160 PTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVSN 214
Cdd:PRK10908 164 PTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGG 218
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
11-212 |
5.80e-18 |
|
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: 79.24 E-value: 5.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 11 KSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRK---GVIKLGGKdlmpvPLHR-TAKYGIGFVPE 86
Cdd:cd03234 14 KNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQ-----PRKPdQFQKCVAYVRQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 87 ERGIFATLSVEE------NLKLP---------PVVASGGMTLDEIYELFPNLYErrtspgtKLSGGEQQMLAMARILRTG 151
Cdd:cd03234 89 DDILLPGLTVREtltytaILRLPrkssdairkKRVEDVLLRDLALTRIGGNLVK-------GISGGERRRVSIAVQLLWD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1610782141 152 VKVLLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVL-VEQN----FRFASRIAdrfyLMDHGQMV 212
Cdd:cd03234 162 PKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILtIHQPrsdlFRLFDRIL----LLSSGEIV 223
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-212 |
7.45e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 80.03 E-value: 7.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 4 MLEVSNLKSWYGE-SQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLM-PVPLHRTAKY-G 80
Cdd:PRK13644 1 MIRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGdFSKLQGIRKLvG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 81 IGFV-PEERGIFATLSVE-----ENLKLPPVVASG--GMTLDEI-YELFpnlyeRRTSPGTkLSGGEQQMLAMARILRTG 151
Cdd:PRK13644 81 IVFQnPETQFVGRTVEEDlafgpENLCLPPIEIRKrvDRALAEIgLEKY-----RHRSPKT-LSGGQGQCVALAGILTME 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1610782141 152 VKVLLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRfASRIADRFYLMDHGQMV 212
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLE-ELHDADRIIVMDRGKIV 214
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
5-210 |
7.93e-18 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 81.15 E-value: 7.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPlhrtakygigfv 84
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 85 PEERGI---------FATLSVEEN----LKLPPVVAsggmtlDEIYEL---------FPNLYERRTspgTKLSGGEQQML 142
Cdd:PRK09452 83 AENRHVntvfqsyalFPHMTVFENvafgLRMQKTPA------AEITPRvmealrmvqLEEFAQRKP---HQLSGGQQQRV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1610782141 143 AMARILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSR-GMTVVLVEQNFRFASRIADRFYLMDHGQ 210
Cdd:PRK09452 154 AIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGR 222
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
5-216 |
8.19e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 81.50 E-value: 8.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSwygesQALHG-VDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKdlmPVPLHRTA---KYG 80
Cdd:PRK11288 258 LRLDGLKG-----PGLREpISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGK---PIDIRSPRdaiRAG 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 81 IGFVPEER---GIFATLSVEENLKLP--PVVASGGMTLDEIYE-----LFPNLYERRT-SPGTK---LSGGEQQMLAMAR 146
Cdd:PRK11288 330 IMLCPEDRkaeGIIPVHSVADNINISarRHHLRAGCLINNRWEaenadRFIRSLNIKTpSREQLimnLSGGNQQKAILGR 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 147 ILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFP 216
Cdd:PRK11288 410 WLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGELA 479
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-210 |
1.02e-17 |
|
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: 78.63 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 1 MAAMLEVSNL-KSWYGESQ------ALHGVDLTVGEGETITILGRNGVGKTTTLRTIMG---------IIRNRKGVIKLG 64
Cdd:COG4778 1 MTTLLEVENLsKTFTLHLQggkrlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGnylpdsgsiLVRHDGGWVDLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 65 gkDLMPVPLHRTAKYGIGFVPEergiF-------ATLS-VEEnlklpPVVASGGMT---LDEIYELFP--NLYER--RTS 129
Cdd:COG4778 81 --QASPREILALRRRTIGYVSQ----FlrviprvSALDvVAE-----PLLERGVDReeaRARARELLArlNLPERlwDLP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 130 PGTkLSGGEQQMLAMARILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHG 209
Cdd:COG4778 150 PAT-FSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
.
gi 1610782141 210 Q 210
Cdd:COG4778 229 S 229
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-213 |
1.37e-17 |
|
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: 78.63 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 2 AAMLEVSNLKSWYGESQA----LHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPV---PLH 74
Cdd:COG4181 6 APIIELRGLTKTVGTGAGeltiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALdedARA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 75 RTAKYGIGFVPEERGIFATLSVEENLKLPpvvasggmtldeiYELF--PNLYER------------RTS--PGTkLSGGE 138
Cdd:COG4181 86 RLRARHVGFVFQSFQLLPTLTALENVMLP-------------LELAgrRDARARarallervglghRLDhyPAQ-LSGGE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1610782141 139 QQMLAMARILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKL-KSRGMTVVLVEQNFRFASRiADRFYLMDHGQMVS 213
Cdd:COG4181 152 QQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELnRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVE 226
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-220 |
1.46e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 79.37 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 1 MAAMLEVSNLKSWY---GESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTA 77
Cdd:PRK13642 1 MNKILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 78 KyGIGFV---PEERGIFATlsVEENLKLPpvVASGGMTLDEIYE------LFPNLYERRTSPGTKLSGGEQQMLAMARIL 148
Cdd:PRK13642 81 R-KIGMVfqnPDNQFVGAT--VEDDVAFG--MENQGIPREEMIKrvdealLAVNMLDFKTREPARLSGGQKQRVAVAGII 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1610782141 149 RTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSR-GMTVVLVEQNFRFASRiADRFYLMDHGQMVSNFPVSEL 220
Cdd:PRK13642 156 ALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSEL 227
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
12-227 |
1.56e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 80.78 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 12 SWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLhRTAKYGIGFVPEERGIF 91
Cdd:PRK13657 343 SYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTR-ASLRRNIAVVFQDAGLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 92 ATlSVEENLKlppvVASGGMTLDEIYELFP-----NLYERRTSP--------GTKLSGGEQQMLAMARILRTGVKVLLLD 158
Cdd:PRK13657 422 NR-SIEDNIR----VGRPDATDEEMRAAAEraqahDFIERKPDGydtvvgerGRQLSGGERQRLAIARALLKDPPILILD 496
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1610782141 159 EPTEGLAPVIVQRIGEVLQKLkSRGMTVVLVEQnfRFAS-RIADRFYLMDHGQMVSNFPVSELS---GRMGEL 227
Cdd:PRK13657 497 EATSALDVETEAKVKAALDEL-MKGRTTFIIAH--RLSTvRNADRILVFDNGRVVESGSFDELVargGRFAAL 566
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
5-212 |
1.88e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 79.36 E-value: 1.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYG-----ESQALHGVDLTVGEGETITILGRNGVGKTT-----------TLRTIMGIIRNRKGVIKLGGKD- 67
Cdd:PRK13651 3 IKVKNIVKIFNkklptELKALDNVSVEINQGEFIAIIGQTGSGKTTfiehlnalllpDTGTIEWIFKDEKNKKKTKEKEk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 68 -LMPVPLHRTAKYGIGFVPEER---GI---FATL-----SVEENLKLPPVvaSGGMTLDEIYEL---------FPNLYER 126
Cdd:PRK13651 83 vLEKLVIQKTRFKKIKKIKEIRrrvGVvfqFAEYqlfeqTIEKDIIFGPV--SMGVSKEEAKKRaakyielvgLDESYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 127 RtSPgTKLSGGEQQMLAMARILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLM 206
Cdd:PRK13651 161 R-SP-FELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFF 238
|
....*.
gi 1610782141 207 DHGQMV 212
Cdd:PRK13651 239 KDGKII 244
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-225 |
2.00e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 79.36 E-value: 2.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 18 QALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDlmPVPLHRTAKYGIGFVPEERG-IFATLSV 96
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV--PFKRRKEFARRIGVVFGQRSqLWWDLPA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 97 EENLKLppvvasggmtLDEIYELFPNLYERR--------------TSPGTKLSGGeQQM---LAMARILRTgvKVLLLDE 159
Cdd:COG4586 114 IDSFRL----------LKAIYRIPDAEYKKRldelvelldlgellDTPVRQLSLG-QRMrceLAAALLHRP--KILFLDE 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1610782141 160 PTEGLAPVIVQRIGEVLQKL-KSRGMTVVL-------VEQnfrfasrIADRFYLMDHGQMVSNFPVSELSGRMG 225
Cdd:COG4586 181 PTIGLDVVSKEAIREFLKEYnRERGTTILLtshdmddIEA-------LCDRVIVIDHGRIIYDGSLEELKERFG 247
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
24-201 |
2.23e-17 |
|
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: 76.42 E-value: 2.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 24 DLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKG-VIKLGGKDLMpvplhrtakygigFVPEErgifatlsveenlkl 102
Cdd:cd03223 21 SFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGrIGMPEGEDLL-------------FLPQR--------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 103 pPVVASGgmTLDE--IYelfpnlyerrtsP-GTKLSGGEQQMLAMARILRTGVKVLLLDEPTEGLAPVIVQRIgevLQKL 179
Cdd:cd03223 73 -PYLPLG--TLREqlIY------------PwDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRL---YQLL 134
|
170 180
....*....|....*....|....*
gi 1610782141 180 KSRGMTVVLV---EQNFRFASRIAD 201
Cdd:cd03223 135 KELGITVISVghrPSLWKFHDRVLD 159
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-164 |
2.26e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 78.23 E-value: 2.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 1 MAAMLEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKlggkdlmpvplhRTAKYG 80
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK------------RNGKLR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 81 IGFVPEERGIFAT--LSVEENLKLPPVVASGgmtldeiyELFPNLYERRTS-----PGTKLSGGEQQMLAMARILRTGVK 153
Cdd:PRK09544 69 IGYVPQKLYLDTTlpLTVNRFLRLRPGTKKE--------DILPALKRVQAGhlidaPMQKLSGGETQRVLLARALLNRPQ 140
|
170
....*....|.
gi 1610782141 154 VLLLDEPTEGL 164
Cdd:PRK09544 141 LLVLDEPTQGV 151
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-212 |
3.89e-17 |
|
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: 79.85 E-value: 3.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 4 MLEVSNLKSWY-----GESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKG-VIKLGGKDLM----PVPL 73
Cdd:TIGR03269 279 IIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGeVNVRVGDEWVdmtkPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 74 HR-TAKYGIGFVPEERGIFATLSVEENL------KLPP---------VVASGGMTLDEIYELFPNLYErrtspgtKLSGG 137
Cdd:TIGR03269 359 GRgRAKRYIGILHQEYDLYPHRTVLDNLteaiglELPDelarmkaviTLKMVGFDEEKAEEILDKYPD-------ELSEG 431
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1610782141 138 EQQMLAMARILRTGVKVLLLDEPTEGLAPVIVQRIGEVLqkLKSR---GMTVVLVEQNFRFASRIADRFYLMDHGQMV 212
Cdd:TIGR03269 432 ERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSI--LKAReemEQTFIIVSHDMDFVLDVCDRAALMRDGKIV 507
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
5-212 |
4.43e-17 |
|
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: 76.44 E-value: 4.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNL------KSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNR--KGVIKLGGKDLMPvplhRT 76
Cdd:cd03213 4 LSFRNLtvtvksSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRPLDK----RS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 77 AKYGIGFVPEERGIFATLSVEENLKlppVVAsggmtldeiyELfpnlyerrtspgTKLSGGEQQMLAMARILRTGVKVLL 156
Cdd:cd03213 80 FRKIIGYVPQDDILHPTLTVRETLM---FAA----------KL------------RGLSGGERKRVSIALELVSNPSLLF 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1610782141 157 LDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLV-----EQNFRFasriADRFYLMDHGQMV 212
Cdd:cd03213 135 LDEPTSGLDSSSALQVMSLLRRLADTGRTIICSihqpsSEIFEL----FDKLLLLSQGRVI 191
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-223 |
4.52e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 77.85 E-value: 4.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 1 MAAMLEVSNLKSWYGE-SQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPvplhRTAKY 79
Cdd:PRK13647 1 MDNIIEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNA----ENEKW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 80 -----GIGFVPEERGIFATlSVEENLKLPPVvaSGGMTLDEIYELFP------NLYERRTSPGTKLSGGEQQMLAMARIL 148
Cdd:PRK13647 77 vrskvGLVFQDPDDQVFSS-TVWDDVAFGPV--NMGLDKDEVERRVEealkavRMWDFRDKPPYHLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1610782141 149 RTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPVSELSGR 223
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
16-229 |
5.80e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 77.90 E-value: 5.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 16 ESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMpvplHRT---------AKYGIGFVPE 86
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIT----HKTkdkyirpvrKRIGMVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 87 ERGIFATlSVEENLKLPPvvASGGMTLDEI----YELFPNL-YER---RTSPgTKLSGGEQQMLAMARILRTGVKVLLLD 158
Cdd:PRK13646 95 ESQLFED-TVEREIIFGP--KNFKMNLDEVknyaHRLLMDLgFSRdvmSQSP-FQMSGGQMRKIAIVSILAMNPDIIVLD 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1610782141 159 EPTEGLAPVIVQRIGEVLQKLK-SRGMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPVSELSGRMGELNK 229
Cdd:PRK13646 171 EPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKKLAD 242
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
5-213 |
6.14e-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: 76.30 E-value: 6.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGE--SQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTaKYGIG 82
Cdd:cd03369 7 IEVENLSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL-RSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 83 FVPEERGIFATlSVEENLKlppvvASGGMTLDEIYELFpnlyeRRTSPGTKLSGGEQQMLAMARILRTGVKVLLLDEPTE 162
Cdd:cd03369 86 IIPQDPTLFSG-TIRSNLD-----PFDEYSDEEIYGAL-----RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1610782141 163 GLAPVIVQRIGEVLQKLKSrGMTVVLVEQNFRfasRIA--DRFYLMDHGQMVS 213
Cdd:cd03369 155 SIDYATDALIQKTIREEFT-NSTILTIAHRLR---TIIdyDKILVMDAGEVKE 203
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
16-233 |
7.25e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 77.40 E-value: 7.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 16 ESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRT---AKYGIGFVPEERGIFA 92
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSdirKKVGLVFQYPEYQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 93 TlSVEENLKLPPVvaSGGMTLDEIYE----------LFPNLYERRtSPgTKLSGGEQQMLAMARILRTGVKVLLLDEPTE 162
Cdd:PRK13637 99 E-TIEKDIAFGPI--NLGLSEEEIENrvkramnivgLDYEDYKDK-SP-FELSGGQKRRVAIAGVVAMEPKILILDEPTA 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1610782141 163 GLAPVIVQRIGEVLQKL-KSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPVSELSGRMGELNKV-LGV 233
Cdd:PRK13637 174 GLDPKGRDEILNKIKELhKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVETLESIgLAV 246
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-212 |
7.53e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 78.71 E-value: 7.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWY--GESQALHGVDLTVGEGETITILGRNGVGKTTTLRTImgiIRN---RKGVIKLGGKDLMPVPlHRTAKY 79
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL---TRAwdpQQGEILLNGQPIADYS-EAALRQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 80 GIGFVPEERGIFATlSVEENLKLppvvASGGMTLDEIYEL-----FPNLYERRTS-------PGTKLSGGEQQMLAMARI 147
Cdd:PRK11160 415 AISVVSQRVHLFSA-TLRDNLLL----AAPNASDEALIEVlqqvgLEKLLEDDKGlnawlgeGGRQLSGGEQRRLGIARA 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1610782141 148 LRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLkSRGMTVVLVEQNFRFASRIaDRFYLMDHGQMV 212
Cdd:PRK11160 490 LLHDAPLLLLDEPTEGLDAETERQILELLAEH-AQNKTVLMITHRLTGLEQF-DRICVMDNGQII 552
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
19-211 |
9.40e-17 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 78.90 E-value: 9.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 19 ALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLmPVPLHrTAKYGIGFVPEERGIFATLSVEE 98
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLD-AVRQSLGMCPQHNILFHHLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 99 NLKLPPVVA-----SGGMTLDEIYElFPNLYERRTSPGTKLSGGEQQMLAMARILRTGVKVLLLDEPTEGLAPVIVQRIG 173
Cdd:TIGR01257 1023 HILFYAQLKgrsweEAQLEMEAMLE-DTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIW 1101
|
170 180 190
....*....|....*....|....*....|....*...
gi 1610782141 174 EVLQKLKSrGMTVVLVEQNFRFASRIADRFYLMDHGQM 211
Cdd:TIGR01257 1102 DLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
4-188 |
1.20e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 75.37 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 4 MLEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGG----KDLMpvplhrTAKY 79
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERqsikKDLC------TYQK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 80 GIGFVPEERGIFATLSVEENLKLPPVVASGGMTLDEIYELFpNLYERRTSPGTKLSGGEQQMLAMARILRTGVKVLLLDE 159
Cdd:PRK13540 75 QLCFVGHRSGINPYLTLRENCLYDIHFSPGAVGITELCRLF-SLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDE 153
|
170 180
....*....|....*....|....*....
gi 1610782141 160 PTEGLAPVIVQRIGEVLQKLKSRGMTVVL 188
Cdd:PRK13540 154 PLVALDELSLLTIITKIQEHRAKGGAVLL 182
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-221 |
1.53e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 78.05 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 1 MAAMLEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIR--NRKGVIKLGGKDLMPVPLHRTAK 78
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgTYEGEIIFEGEELQASNIRDTER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 79 YGIGFVPEERGIFATLSVEENLKLPPVVASGG-MTLDEIYELFPNLYER---RTSPGTK---LSGGEQQMLAMARILRTG 151
Cdd:PRK13549 82 AGIAIIHQELALVKELSVLENIFLGNEITPGGiMDYDAMYLRAQKLLAQlklDINPATPvgnLGLGQQQLVEIAKALNKQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 152 VKVLLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPVSELS 221
Cdd:PRK13549 162 ARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMT 231
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
16-212 |
1.67e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 76.60 E-value: 1.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 16 ESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLG---------GKDLMPVplhrTAKYGIGFVPE 86
Cdd:PRK13634 19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGervitagkkNKKLKPL----RKKVGIVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 87 ERGIFATlSVEENLKLPPVvaSGGMTLDEIYE----------LFPNLYERrtSPgTKLSGGEQQMLAMARILRTGVKVLL 156
Cdd:PRK13634 95 EHQLFEE-TVEKDICFGPM--NFGVSEEDAKQkaremielvgLPEELLAR--SP-FELSGGQMRRVAIAGVLAMEPEVLV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1610782141 157 LDEPTEGLAPVIVQRIGEVLQKL-KSRGMTVVLVEQNFRFASRIADRFYLMDHGQMV 212
Cdd:PRK13634 169 LDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVF 225
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
18-220 |
1.71e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 76.26 E-value: 1.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 18 QALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLmpVPLHRTAKYG------------IGFVP 85
Cdd:PRK10419 26 TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPL--AKLNRAQRKAfrrdiqmvfqdsISAVN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 86 EERGIFA----------TLSVEENLklppvvASGGMTLDEIyELFPNLYERRtsPGtKLSGGEQQMLAMARILRTGVKVL 155
Cdd:PRK10419 104 PRKTVREiireplrhllSLDKAERL------ARASEMLRAV-DLDDSVLDKR--PP-QLSGGQLQRVCLARALAVEPKLL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1610782141 156 LLDEPTEGLAPVIVQRIGEVLQKLKSR-GMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPVSEL 220
Cdd:PRK10419 174 ILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDK 239
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-221 |
2.09e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 77.35 E-value: 2.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 1 MAAMLEVSNL-KSWYGeSQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKY 79
Cdd:PRK10762 1 MQALLQLKGIdKAFPG-VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 80 GIGFVPEERGIFATLSVEENLKL--PPVVASGGMTLDEIYELFPNLYER---RTSPGT---KLSGGEQQMLAMARILRTG 151
Cdd:PRK10762 80 GIGIIHQELNLIPQLTIAENIFLgrEFVNRFGRIDWKKMYAEADKLLARlnlRFSSDKlvgELSIGEQQMVEIAKVLSFE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 152 VKVLLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPVSELS 221
Cdd:PRK10762 160 SKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLT 229
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-221 |
2.21e-16 |
|
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: 77.56 E-value: 2.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 4 MLEVSNLKSWYGESQALHGVD---LTVGEGETITILGRNGVGKTTTLRTIMGIIRNR-KGVIKLGGKDLMPVPLHRTAKY 79
Cdd:TIGR02633 257 ILEARNLTCWDVINPHRKRVDdvsFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQAIRA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 80 GIGFVPEER---GIFATLSVEENLKLPPVVA-SGGMTLDEIYEL------FPNLYERRTSPG---TKLSGGEQQMLAMAR 146
Cdd:TIGR02633 337 GIAMVPEDRkrhGIVPILGVGKNITLSVLKSfCFKMRIDAAAELqiigsaIQRLKVKTASPFlpiGRLSGGNQQKAVLAK 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1610782141 147 ILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPVSELS 221
Cdd:TIGR02633 417 MLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGDFVNHALT 491
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-220 |
3.36e-16 |
|
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: 77.03 E-value: 3.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 1 MAAMLEVSNLKSWYG----ESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGI----IRNRKGVIKLGGKDLMPVP 72
Cdd:COG4172 3 SMPLLSVEDLSVAFGqgggTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLlpdpAAHPSGSILFDGQDLLGLS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 73 LHRTAKY---GIGFVPEE------------RGIFATLSVEENLklppvvaSGGMTLDEIYELF-----PNLYERRTSPGT 132
Cdd:COG4172 83 ERELRRIrgnRIAMIFQEpmtslnplhtigKQIAEVLRLHRGL-------SGAAARARALELLervgiPDPERRLDAYPH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 133 KLSGGEQQ--MLAMAriLRTGVKVLLLDEPTEGLaPVIVQR-IGEVLQKLKSR-GMTVVLVEQNFRFASRIADRFYLMDH 208
Cdd:COG4172 156 QLSGGQRQrvMIAMA--LANEPDLLIADEPTTAL-DVTVQAqILDLLKDLQRElGMALLLITHDLGVVRRFADRVAVMRQ 232
|
250
....*....|..
gi 1610782141 209 GQMVSNFPVSEL 220
Cdd:COG4172 233 GEIVEQGPTAEL 244
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4-221 |
3.46e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 76.89 E-value: 3.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 4 MLEVSNLKSWYGESQALHGVD---LTVGEGETITILGRNGVGKTTTLRTIMGIIRNRK-GVIKLGGKdlmPVPLHRTA-- 77
Cdd:PRK13549 259 ILEVRNLTAWDPVNPHIKRVDdvsFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGK---PVKIRNPQqa 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 78 -KYGIGFVPEER---GIFATLSVEENLKLPPVVA-SGGMTLDEIYEL------FPNLYERRTSPG---TKLSGGEQQMLA 143
Cdd:PRK13549 336 iAQGIAMVPEDRkrdGIVPVMGVGKNITLAALDRfTGGSRIDDAAELktilesIQRLKVKTASPElaiARLSGGNQQKAV 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1610782141 144 MARILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPVSELS 221
Cdd:PRK13549 416 LAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLKGDLINHNLT 493
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
5-212 |
3.85e-16 |
|
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: 74.57 E-value: 3.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYG-ESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLH--RTAkygI 81
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDslRRA---I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 82 GFVPEERGIFATlSVEENLKLPPVVASGgmtlDEIYEL------------FPNLY-----ERrtspGTKLSGGEQQMLAM 144
Cdd:cd03253 78 GVVPQDTVLFND-TIGYNIRYGRPDATD----EEVIEAakaaqihdkimrFPDGYdtivgER----GLKLSGGEKQRVAI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1610782141 145 ARILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLkSRGMTVVLVEQNFRFASRiADRFYLMDHGQMV 212
Cdd:cd03253 149 ARAILKNPPILLLDEATSALDTHTEREIQAALRDV-SKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIV 214
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
15-212 |
5.89e-16 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 73.68 E-value: 5.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 15 GESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLH--RTAkygIGFVPEERGIFA 92
Cdd:cd03244 15 NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHdlRSR---ISIIPQDPVLFS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 93 TlSVEENL---------KLPPVVASGGMTlDEIYELFPNLYERRTSPGTKLSGGEQQMLAMARILRTGVKVLLLDEPTEG 163
Cdd:cd03244 92 G-TIRSNLdpfgeysdeELWQALERVGLK-EFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATAS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1610782141 164 LAPVIVQRIGEVLQ-KLKSRgmTVVLVeqnfrfASRI-----ADRFYLMDHGQMV 212
Cdd:cd03244 170 VDPETDALIQKTIReAFKDC--TVLTI------AHRLdtiidSDRILVLDKGRVV 216
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-189 |
6.06e-16 |
|
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: 74.35 E-value: 6.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 3 AMLEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKG-VIKLGGKDLMPVPLHRTAKYgI 81
Cdd:COG1119 2 PLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKR-I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 82 GFV-PE-ERGIFATLSVEEnlklppVVASGG---------------MTLDEIYELFpNLYERRTSPGTKLSGGEQQMLAM 144
Cdd:COG1119 81 GLVsPAlQLRFPRDETVLD------VVLSGFfdsiglyreptdeqrERARELLELL-GLAHLADRPFGTLSQGEQRRVLI 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1610782141 145 ARILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKL-KSRGMTVVLV 189
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELLLALLDKLaAEGAPTLVLV 199
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
17-213 |
7.65e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 74.77 E-value: 7.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 17 SQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGG---------KDLMPVplhrTAKYGIGFVPEE 87
Cdd:PRK13643 19 SRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvsstskqKEIKPV----RKKVGVVFQFPE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 88 RGIFATlSVEENLKLPPvvASGGMTLDEIYELFPNLYER--------RTSPgTKLSGGEQQMLAMARILRTGVKVLLLDE 159
Cdd:PRK13643 95 SQLFEE-TVLKDVAFGP--QNFGIPKEKAEKIAAEKLEMvgladefwEKSP-FELSGGQMRRVAIAGILAMEPEVLVLDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1610782141 160 PTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVS 213
Cdd:PRK13643 171 PTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIIS 224
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-201 |
8.89e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 74.30 E-value: 8.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTImgiirNR----KGVIKLGGK-------------- 66
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-----NRmnelESEVRVEGRveffnqniyerrvn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 67 ---------------DLMPVPLHRTAKYG---IGFVP--EERGIfatlsVEENLKLPpvvasggmtldeiyELFPNLYER 126
Cdd:PRK14258 83 lnrlrrqvsmvhpkpNLFPMSVYDNVAYGvkiVGWRPklEIDDI-----VESALKDA--------------DLWDEIKHK 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1610782141 127 RTSPGTKLSGGEQQMLAMARILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSRG-MTVVLVEQNFRFASRIAD 201
Cdd:PRK14258 144 IHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSeLTMVIVSHNLHQVSRLSD 219
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-213 |
1.14e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 75.21 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 4 MLEVSNLKSWygESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKYGIGF 83
Cdd:PRK09700 265 VFEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAY 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 84 VPEER---GIFATLSVEENLKLPPVVASGGmtLDEIYELFPNLYERRTSPG----------------TKLSGGEQQMLAM 144
Cdd:PRK09700 343 ITESRrdnGFFPNFSIAQNMAISRSLKDGG--YKGAMGLFHEVDEQRTAENqrellalkchsvnqniTELSGGNQQKVLI 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1610782141 145 ARILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVS 213
Cdd:PRK09700 421 SKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
16-212 |
2.28e-15 |
|
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: 72.65 E-value: 2.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 16 ESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKYgIGFVPEERGIFATlS 95
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQ-IGLVSQDVFLFND-T 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 96 VEENlklppvVASG--GMTLDEIYEL------------FPNLYERRT-SPGTKLSGGEQQMLAMARILRTGVKVLLLDEP 160
Cdd:cd03251 92 VAEN------IAYGrpGATREEVEEAaraanahefimeLPEGYDTVIgERGVKLSGGQRQRIAIARALLKDPPILILDEA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1610782141 161 TEGLAPVIVQRIGEVLQKLkSRGMTVVLVeqnfrfASRI-----ADRFYLMDHGQMV 212
Cdd:cd03251 166 TSALDTESERLVQAALERL-MKNRTTFVI------AHRLstienADRIVVLEDGKIV 215
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-212 |
3.08e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 72.72 E-value: 3.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 3 AMLEVSNLKSWYGESQ--ALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMP--VPLHRTaK 78
Cdd:PRK13632 6 VMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKenLKEIRK-K 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 79 YGIGFV-PEERGIFATlsVE-------ENLKLPPVVASggmtlDEIYEL-----FPNLYERRTSpgtKLSGGEQQMLAMA 145
Cdd:PRK13632 85 IGIIFQnPDNQFIGAT--VEddiafglENKKVPPKKMK-----DIIDDLakkvgMEDYLDKEPQ---NLSGGQKQRVAIA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1610782141 146 RILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKL-KSRGMTVVLVEQNFRFASrIADRFYLMDHGQMV 212
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLrKTRKKTLISITHDMDEAI-LADKVIVFSEGKLI 221
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-213 |
3.19e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 72.74 E-value: 3.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 1 MAAMLEVSNLKSWY--GESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAK 78
Cdd:PRK13635 2 KEEIIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 79 YgIGFV---PEERGIFATlsVEENlklppvVASG----GMTLDEIYELFP------NLYERRTSPGTKLSGGEQQMLAMA 145
Cdd:PRK13635 82 Q-VGMVfqnPDNQFVGAT--VQDD------VAFGleniGVPREEMVERVDqalrqvGMEDFLNREPHRLSGGQKQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1610782141 146 RILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLK-SRGMTVVLVEQNFRFASRiADRFYLMDHGQMVS 213
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDPRGRREVLETVRQLKeQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILE 220
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
15-212 |
3.39e-15 |
|
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: 72.68 E-value: 3.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 15 GESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVP---LHRTAKYGIGFVPEERGIF 91
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkeLRELRRKKISMVFQSFALL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 92 ATLSVEENLKLPPVVAsgGMTLDEIYEL------FPNLYERRTSPGTKLSGGEQQMLAMARILRTGVKVLLLDEPTEGLA 165
Cdd:cd03294 115 PHRTVLENVAFGLEVQ--GVPRAEREERaaealeLVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1610782141 166 PVIVQRIGEVLQKL-KSRGMTVVLVEQNFRFASRIADRFYLMDHGQMV 212
Cdd:cd03294 193 PLIRREMQDELLRLqAELQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
16-212 |
4.71e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 72.47 E-value: 4.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 16 ESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGG---------KDLMPVPLH------------ 74
Cdd:PRK13649 19 EGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtlitstsknKDIKQIRKKvglvfqfpesql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 75 --RTAKYGIGFVPEERGIfatlSVEENLKLppvvASGGMTLDEIYElfpNLYERrtSPgTKLSGGEQQMLAMARILRTGV 152
Cdd:PRK13649 99 feETVLKDVAFGPQNFGV----SQEEAEAL----AREKLALVGISE---SLFEK--NP-FELSGGQMRRVAIAGILAMEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 153 KVLLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMV 212
Cdd:PRK13649 165 KILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-227 |
9.15e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 71.69 E-value: 9.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 1 MAAMLEVSNLKSWYGESQ---ALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTa 77
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDI- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 78 KYGIGFV---PEERGIFATlsVEENlklppvVASG----GMTLDEIYEL------FPNLYERRTSPGTKLSGGEQQMLAM 144
Cdd:PRK13650 80 RHKIGMVfqnPDNQFVGAT--VEDD------VAFGlenkGIPHEEMKERvnealeLVGMQDFKEREPARLSGGQKQRVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 145 ARILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSR-GMTVVLVEQNFRFASrIADRFYLMDHGQMVSNFPVSELSGR 223
Cdd:PRK13650 152 AGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELFSR 230
|
....
gi 1610782141 224 MGEL 227
Cdd:PRK13650 231 GNDL 234
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-212 |
9.82e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 71.27 E-value: 9.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 1 MAAMLEVSNLKSWYGESQ------ALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKG---VIKLGGKDLMPV 71
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNEesteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGkvyVDGLDTSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 72 PLHRTaKYGIGFVPEERGIFATLSVE------ENLKLPPvvasggmtlDEIYELFP------NLYERRTSPGTKLSGGEQ 139
Cdd:PRK13633 81 WDIRN-KAGMVFQNPDNQIVATIVEEdvafgpENLGIPP---------EEIRERVDeslkkvGMYEYRRHAPHLLSGGQK 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1610782141 140 QMLAMARILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKL-KSRGMTVVLVEQNFRFASRiADRFYLMDHGQMV 212
Cdd:PRK13633 151 QRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDSGKVV 223
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
14-189 |
1.31e-14 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 69.57 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 14 YGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGViklggkdlmpvpLHRTAKYGIGFVPEERGIFAT 93
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGT------------VRRAGGARVAYVPQRSEVPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 94 L--SVEENLKL---------PPVVASGGMTLDEIYELFpNLYERRTSPGTKLSGGEQQMLAMARILRTGVKVLLLDEPTE 162
Cdd:NF040873 70 LplTVRDLVAMgrwarrglwRRLTRDDRAAVDDALERV-GLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180
....*....|....*....|....*..
gi 1610782141 163 GLAPVIVQRIGEVLQKLKSRGMTVVLV 189
Cdd:NF040873 149 GLDAESRERIIALLAEEHARGATVVVV 175
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
5-211 |
1.58e-14 |
|
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: 70.65 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGE--SQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIrNRKGVIKLGGKDLMPVPLHRTAKyGIG 82
Cdd:cd03289 3 MTVKDLTAKYTEggNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGDIQIDGVSWNSVPLQKWRK-AFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 83 FVPEERGIFA-----------TLSVEENLKLPPVVAsggmtLDEIYELFPN-LYERRTSPGTKLSGGEQQMLAMARILRT 150
Cdd:cd03289 81 VIPQKVFIFSgtfrknldpygKWSDEEIWKVAEEVG-----LKSVIEQFPGqLDFVLVDGGCVLSHGHKQLMCLARSVLS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1610782141 151 GVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSrGMTVVLVEQNFRfASRIADRFYLMDHGQM 211
Cdd:cd03289 156 KAKILLLDEPSAHLDPITYQVIRKTLKQAFA-DCTVILSEHRIE-AMLECQRFLVIEENKV 214
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
16-213 |
1.96e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 70.81 E-value: 1.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 16 ESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKG-------VIKLGGKDLMPVPLHRTaKYGIGFVPEER 88
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqtivgdyAIPANLKKIKEVKRLRK-EIGLVFQFPEY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 89 GIFATlSVEENLKLPPVvaSGGMTLDEIYELFPNL---------YERRtSPgTKLSGGEQQMLAMARILRTGVKVLLLDE 159
Cdd:PRK13645 102 QLFQE-TIEKDIAFGPV--NLGENKQEAYKKVPELlklvqlpedYVKR-SP-FELSGGQKRRVALAGIIAMDGNTLVLDE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1610782141 160 PTEGLAPVIVQRIGEVLQKL-KSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVS 213
Cdd:PRK13645 177 PTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVIS 231
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-225 |
3.53e-14 |
|
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: 69.44 E-value: 3.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 16 ESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLM---PVPLHRTakygIGFVPEERGIFA 92
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLAladPAWLRRQ----VGVVLQENVLFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 93 TlSVEENLKLppvvASGGMTLDEIYEL------------FPNLYERRTSP-GTKLSGGEQQMLAMARILRTGVKVLLLDE 159
Cdd:cd03252 90 R-SIRDNIAL----ADPGMSMERVIEAaklagahdfiseLPEGYDTIVGEqGAGLSGGQRQRIAIARALIHNPRILIFDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1610782141 160 PTEGLAPVIVQRIGEVLQKLkSRGMTVVLVEQNFRfASRIADRFYLMDHGQMVSNFPVSELSGRMG 225
Cdd:cd03252 165 ATSALDYESEHAIMRNMHDI-CAGRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDELLAENG 228
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-209 |
4.53e-14 |
|
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: 69.03 E-value: 4.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 20 LHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAkygigfVPEERGIFATLSVEEN 99
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV------VFQNYSLLPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 100 LKLPPVVASGGMT-------LDEIYELFpNLYERRTSPGTKLSGGEQQMLAMARILRTGVKVLLLDEPTEGLAPVIVQRI 172
Cdd:TIGR01184 75 IALAVDRVLPDLSkserraiVEEHIALV-GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 1610782141 173 GEVLQKL-KSRGMTVVLVEQNFRFASRIADRFYLMDHG 209
Cdd:TIGR01184 154 QEELMQIwEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4-212 |
7.08e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 69.49 E-value: 7.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 4 MLEVSNLKSWYGESQ-----ALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVI---------KLGGKDLM 69
Cdd:PRK13631 21 ILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyigdKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 70 PVPLHRTAK--------YGIGFVPEERGIFATlSVEENLKLPPVvASG---------------GMTLDEIYelfpnlYER 126
Cdd:PRK13631 101 TNPYSKKIKnfkelrrrVSMVFQFPEYQLFKD-TIEKDIMFGPV-ALGvkkseakklakfylnKMGLDDSY------LER 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 127 rtSPgTKLSGGEQQMLAMARILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLM 206
Cdd:PRK13631 173 --SP-FGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVM 249
|
....*.
gi 1610782141 207 DHGQMV 212
Cdd:PRK13631 250 DKGKIL 255
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
3-160 |
7.94e-14 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 69.49 E-value: 7.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 3 AMLEVSNL-KSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGK---DLMPvplhrtAK 78
Cdd:PRK11650 2 AGLKLQAVrKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRvvnELEP------AD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 79 YGIGFVPEERGIFATLSVEENLklppvvASG----GMTLDEI----------YELFPNLyERRTSpgtKLSGGEQQMLAM 144
Cdd:PRK11650 76 RDIAMVFQNYALYPHMSVRENM------AYGlkirGMPKAEIeervaeaariLELEPLL-DRKPR---ELSGGQRQRVAM 145
|
170
....*....|....*..
gi 1610782141 145 AR-ILRTGvKVLLLDEP 160
Cdd:PRK11650 146 GRaIVREP-AVFLFDEP 161
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
4-188 |
1.21e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.14 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 4 MLEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDL--MPVPLHRTAKYgI 81
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIrrQRDEYHQDLLY-L 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 82 GFVPeerGIFATLSVEENLK--LPpvvASGGMTLDEIYELFP--NLYERRTSPGTKLSGGEQQMLAMARILRTGVKVLLL 157
Cdd:PRK13538 80 GHQP---GIKTELTALENLRfyQR---LHGPGDDEALWEALAqvGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWIL 153
|
170 180 190
....*....|....*....|....*....|....*.
gi 1610782141 158 DEP-----TEGLApVIVQRIGEVLQklksRGMTVVL 188
Cdd:PRK13538 154 DEPftaidKQGVA-RLEALLAQHAE----QGGMVIL 184
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-160 |
1.57e-13 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 67.96 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 3 AMLEVSNLKSWYGES----QALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKdlmPVpLHRTAK 78
Cdd:COG4525 2 SMLTVRHVSVRYPGGgqpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGV---PV-TGPGAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 79 YGIGFvpEERGIFATLSVEENLKLPPVVAsgGMTLDEIYELFPNL--------YERRtsPGTKLSGGEQQMLAMARILRT 150
Cdd:COG4525 78 RGVVF--QKDALLPWLNVLDNVAFGLRLR--GVPKAERRARAEELlalvgladFARR--RIWQLSGGMRQRVGIARALAA 151
|
170
....*....|
gi 1610782141 151 GVKVLLLDEP 160
Cdd:COG4525 152 DPRFLLMDEP 161
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
14-209 |
2.28e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 68.13 E-value: 2.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 14 YGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPlhrTAKYGIGFVPEERGIFAT 93
Cdd:PRK11000 13 YGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVP---PAERGVGMVFQSYALYPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 94 LSVEENLklppvvaSGGMTL---------------DEIYELfPNLYERRTSpgtKLSGGEQQMLAMARILRTGVKVLLLD 158
Cdd:PRK11000 90 LSVAENM-------SFGLKLagakkeeinqrvnqvAEVLQL-AHLLDRKPK---ALSGGQRQRVAIGRTLVAEPSVFLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1610782141 159 EPTEGL-APVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHG 209
Cdd:PRK11000 159 EPLSNLdAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAG 210
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-225 |
2.77e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 67.34 E-value: 2.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 4 MLEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLmpvplhRTAKYGI-- 81
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL------DYSKRGLla 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 82 -------GFVPEERGIFAT-------LSVEeNLKLPPvvASGGMTLDEIYELFpNLYERRTSPGTKLSGGEQQMLAMARI 147
Cdd:PRK13638 75 lrqqvatVFQDPEQQIFYTdidsdiaFSLR-NLGVPE--AEITRRVDEALTLV-DAQHFRHQPIQCLSHGQKKRVAIAGA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 148 LRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVSN------FPVSELS 221
Cdd:PRK13638 151 LVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHgapgevFACTEAM 230
|
....
gi 1610782141 222 GRMG 225
Cdd:PRK13638 231 EQAG 234
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
15-220 |
4.58e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 67.76 E-value: 4.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 15 GESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGiiRNRKGVIKLGGKDLMPVPLHRTAKYGI-GFVPEERGIFAT 93
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAF--RSPKGVKGSGSVLLNGMPIDAKEMRAIsAYVQQDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 94 LSVEENL------KLPPVVASGGMTL--DEIYE---LFPNLYERRTSPGTK--LSGGEQQMLAMARILRTGVKVLLLDEP 160
Cdd:TIGR00955 114 LTVREHLmfqahlRMPRRVTKKEKRErvDEVLQalgLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEP 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1610782141 161 TEGLAPVIVQRIGEVLQKLKSRGMTVVL-VEQNfrfASRIADRF---YLMDHGQMVSNFPVSEL 220
Cdd:TIGR00955 194 TSGLDSFMAYSVVQVLKGLAQKGKTIICtIHQP---SSELFELFdkiILMAEGRVAYLGSPDQA 254
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-212 |
4.63e-13 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 67.79 E-value: 4.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWY-----------GESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRkGVIKLGGKDLMpvPL 73
Cdd:COG4172 276 LEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE-GEIRFDGQDLD--GL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 74 HRTAkygigFVPEERGI-------FATLS--------VEENLKLPPVVASGGMTLDEIYELF------PNLYERrtSPgT 132
Cdd:COG4172 353 SRRA-----LRPLRRRMqvvfqdpFGSLSprmtvgqiIAEGLRVHGPGLSAAERRARVAEALeevgldPAARHR--YP-H 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 133 KLSGGEQQMLAMAR--ILRTgvKVLLLDEPTEGLaPVIVQ-RIGEVLQKL-KSRGMTVVLVEQNFRFASRIADRFYLMDH 208
Cdd:COG4172 425 EFSGGQRQRIAIARalILEP--KLLVLDEPTSAL-DVSVQaQILDLLRDLqREHGLAYLFISHDLAVVRALAHRVMVMKD 501
|
....
gi 1610782141 209 GQMV 212
Cdd:COG4172 502 GKVV 505
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
4-212 |
6.14e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 66.65 E-value: 6.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 4 MLEVSNLK---------SWYGES----QALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLM- 69
Cdd:PRK15079 8 LLEVADLKvhfdikdgkQWFWQPpktlKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 70 --PVPLHRTAKygigfvpEERGIF----ATL----SVEENLKLPPVVASGGMTLDEIYE----------LFPNLYERRTS 129
Cdd:PRK15079 88 mkDDEWRAVRS-------DIQMIFqdplASLnprmTIGEIIAEPLRTYHPKLSRQEVKDrvkammlkvgLLPNLINRYPH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 130 pgtKLSGGEQQMLAMARILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKL-KSRGMTVVLVEQNFRFASRIADRFYLMDH 208
Cdd:PRK15079 161 ---EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYL 237
|
....
gi 1610782141 209 GQMV 212
Cdd:PRK15079 238 GHAV 241
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-212 |
8.31e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 65.72 E-value: 8.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 1 MAAMLEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKyg 80
Cdd:PRK11701 3 DQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSE-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 81 igfvPEERGIFATL--SVEENLK--LPPVVASGG------MT----------------LDEIyELFPNlyeRRTSPGTKL 134
Cdd:PRK11701 81 ----AERRRLLRTEwgFVHQHPRdgLRMQVSAGGnigerlMAvgarhygdiratagdwLERV-EIDAA---RIDDLPTTF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 135 SGGEQQMLAMARILRTGVKVLLLDEPTEGLaPVIVQ-RIGEVLQKLKSR-GMTVVLVEQNFRFASRIADRFYLMDHGQMV 212
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGL-DVSVQaRLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGRVV 231
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
5-228 |
1.03e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 66.28 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMpvplHRTAKY-GIGF 83
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT----HRSIQQrDICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 84 VPEERGIFATLSVEEN----LKLPPVVASGGMT-LDEIYEL-----FPNLYErrtspgTKLSGGEQQMLAMARILRTGVK 153
Cdd:PRK11432 83 VFQSYALFPHMSLGENvgygLKMLGVPKEERKQrVKEALELvdlagFEDRYV------DQISGGQQQRVALARALILKPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 154 VLLLDEPTEGLAPVIVQRIGEVLQKLKSR-GMTVVLV--EQNFRFAsrIADRFYLMDHGQMVSNFPVSELSGR------- 223
Cdd:PRK11432 157 VLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVthDQSEAFA--VSDTVIVMNKGKIMQIGSPQELYRQpasrfma 234
|
....*..
gi 1610782141 224 --MGELN 228
Cdd:PRK11432 235 sfMGDAN 241
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
19-210 |
1.39e-12 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 64.41 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 19 ALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGkdlmpvplhrtakyGIGFVPEERGIFATlSVEE 98
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--------------SIAYVSQEPWIQNG-TIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 99 NLklppvvaSGGMTLDEIY--------------ELFPN-----LYERrtspGTKLSGGEQQMLAMARILRTGVKVLLLDE 159
Cdd:cd03250 85 NI-------LFGKPFDEERyekvikacalepdlEILPDgdlteIGEK----GINLSGGQKQRISLARAVYSDADIYLLDD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1610782141 160 PTEGLAPVIVQRIGE-VLQKLKSRGMTVVLVEQNFRFASRiADRFYLMDHGQ 210
Cdd:cd03250 154 PLSAVDAHVGRHIFEnCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4-211 |
1.80e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.91 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 4 MLEVSNLKSWYGESqaLHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKYGIGF 83
Cdd:PRK10982 250 ILEVRNLTSLRQPS--IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHGFAL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 84 VPEER---GIFATLSVEENlklpPVVASggmtLDEIYELFPNLYERRTSPGTK-------------------LSGGEQQM 141
Cdd:PRK10982 328 VTEERrstGIYAYLDIGFN----SLISN----IRNYKNKVGLLDNSRMKSDTQwvidsmrvktpghrtqigsLSGGNQQK 399
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 142 LAMARILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQM 211
Cdd:PRK10982 400 VIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
5-215 |
1.97e-12 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 66.09 E-value: 1.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGES--QALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIrNRKGVIKLGGKDLMPVPLHRTAKyGIG 82
Cdd:TIGR01271 1218 MDVQGLTAKYTEAgrAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWNSVTLQTWRK-AFG 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 83 FVPEERGIF-----------ATLSVEENLKLPPVVAsggmtLDEIYELFPN-LYERRTSPGTKLSGGEQQMLAMARILRT 150
Cdd:TIGR01271 1296 VIPQKVFIFsgtfrknldpyEQWSDEEIWKVAEEVG-----LKSVIEQFPDkLDFVLVDGGYVLSNGHKQLMCLARSILS 1370
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1610782141 151 GVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSrGMTVVLVEQnfRFASRIADRFYLMDHGQMVSNF 215
Cdd:TIGR01271 1371 KAKILLLDEPSAHLDPVTLQIIRKTLKQSFS-NCTVILSEH--RVEALLECQQFLVIEGSSVKQY 1432
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
111-209 |
2.11e-12 |
|
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: 64.56 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 111 MTLDEIYELFPNL----------------YERRTSPGTKLSGGEQQMLAMARILR---TGVKVLLLDEPTEGLAPVIVQR 171
Cdd:cd03271 131 MTVEEALEFFENIpkiarklqtlcdvglgYIKLGQPATTLSGGEAQRIKLAKELSkrsTGKTLYILDEPTTGLHFHDVKK 210
|
90 100 110
....*....|....*....|....*....|....*...
gi 1610782141 172 IGEVLQKLKSRGMTVVLVEQNFRFAsRIADrfYLMDHG 209
Cdd:cd03271 211 LLEVLQRLVDKGNTVVVIEHNLDVI-KCAD--WIIDLG 245
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
4-212 |
3.07e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 63.89 E-value: 3.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 4 MLEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMG-----IIrnrKGVIKLGGKDLMPVPlhrtak 78
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpaykIL---EGDILFKGESILDLE------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 79 ygigfvPEER---GIFatLSVEENLKLPPV--------------VASGGMTLD--EIYELF----------PNLYERRTS 129
Cdd:CHL00131 78 ------PEERahlGIF--LAFQYPIEIPGVsnadflrlaynskrKFQGLPELDplEFLEIIneklklvgmdPSFLSRNVN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 130 PGtkLSGGEQ---QMLAMArILRTgvKVLLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIA-DRFYL 205
Cdd:CHL00131 150 EG--FSGGEKkrnEILQMA-LLDS--ELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLDYIKpDYVHV 224
|
....*..
gi 1610782141 206 MDHGQMV 212
Cdd:CHL00131 225 MQNGKII 231
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
5-225 |
4.76e-12 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 64.37 E-value: 4.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTttlrtimgiirnrKGVI--KLGGKDLMPVPLH-------- 74
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**-------------RGALpaHV*GPDAGRRPWRf*twcanr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 75 RTAKYGIGF-VPEERGIFATLSVEENL-----KLPPVVASGGMTLDEIYELFpNLYERRTSPGTKLSGGEQQMLAMARIL 148
Cdd:NF000106 81 RALRRTIG*hRPVR*GRRESFSGRENLymigr*LDLSRKDARARADELLERF-SLTEAAGRAAAKYSGGMRRRLDLAASM 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1610782141 149 RTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPVSELSGRMG 225
Cdd:NF000106 160 IGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG 236
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-164 |
5.64e-12 |
|
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: 64.57 E-value: 5.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGgkdlmpvplhRTAKygIGFV 84
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG----------ETVK--LAYV 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 85 PEER-GIFATLSVEEnlklppvVASGGmtLDEI----YELFPNLY-----------ERRTSpgtKLSGGEQQMLAMARIL 148
Cdd:TIGR03719 391 DQSRdALDPNKTVWE-------EISGG--LDIIklgkREIPSRAYvgrfnfkgsdqQKKVG---QLSGGERNRVHLAKTL 458
|
170
....*....|....*.
gi 1610782141 149 RTGVKVLLLDEPTEGL 164
Cdd:TIGR03719 459 KSGGNVLLLDEPTNDL 474
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
15-212 |
8.57e-12 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 63.90 E-value: 8.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 15 GESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVP---LHRTAKYGIGFVPEERGIF 91
Cdd:PRK10070 39 GLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaeLREVRRKKIAMVFQSFALM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 92 ATLSVEEN----LKLPPVVASGGM--TLDEIYELFPNLYERRTSpgTKLSGGEQQMLAMARILRTGVKVLLLDEPTEGLA 165
Cdd:PRK10070 119 PHMTVLDNtafgMELAGINAEERRekALDALRQVGLENYAHSYP--DELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1610782141 166 PVIVQRIGEVLQKLKSRGM-TVVLVEQNFRFASRIADRFYLMDHGQMV 212
Cdd:PRK10070 197 PLIRTEMQDELVKLQAKHQrTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
4-219 |
8.96e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 63.35 E-value: 8.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 4 MLEVsNLKswygesQALHGVDLTVGE---GETIT-ILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDL------MPVPL 73
Cdd:PRK11144 1 MLEL-NFK------QQLGDLCLTVNLtlpAQGITaIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfdaekgICLPP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 74 HrtaKYGIGFVPEERGIFATLSVEENLKLppvvasgGMT------LDEIYELF--PNLYERrtSPGTkLSGGEQQMLAMA 145
Cdd:PRK11144 74 E---KRRIGYVFQDARLFPHYKVRGNLRY-------GMAksmvaqFDKIVALLgiEPLLDR--YPGS-LSGGEKQRVAIG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1610782141 146 RILRTGVKVLLLDEPtegLAPVIVQRIGEV---LQKL-KSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPVSE 219
Cdd:PRK11144 141 RALLTAPELLLMDEP---LASLDLPRKRELlpyLERLaREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEE 215
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-160 |
1.54e-11 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 62.02 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 4 MLEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRtakygiGF 83
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER------GV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 84 VPEERGIFATLSVEENLKLPPVVAsgGMTLDEIYELFPNLYERRTSPGT------KLSGGEQQMLAMARILRTGVKVLLL 157
Cdd:PRK11248 75 VFQNEGLLPWRNVQDNVAFGLQLA--GVEKMQRLEIAHQMLKKVGLEGAekryiwQLSGGQRQRVGIARALAANPQLLLL 152
|
...
gi 1610782141 158 DEP 160
Cdd:PRK11248 153 DEP 155
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-161 |
1.70e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 63.16 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 7 VSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIklggkdlmpvplHRTAKYGIGFVPE 86
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV------------SIPKGLRIGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 87 ERGIFATLSVEEnlklppVVASG------------------------GMTLDEIYELFPNL----YERR----------- 127
Cdd:COG0488 69 EPPLDDDLTVLD------TVLDGdaelraleaeleeleaklaepdedLERLAELQEEFEALggweAEARaeeilsglgfp 142
|
170 180 190
....*....|....*....|....*....|....*...
gi 1610782141 128 TSPGTK----LSGGEQQMLAMARILRTGVKVLLLDEPT 161
Cdd:COG0488 143 EEDLDRpvseLSGGWRRRVALARALLSEPDLLLLDEPT 180
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
15-212 |
1.80e-11 |
|
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: 62.92 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 15 GESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLH--RTAkygIGFVPEERGIFA 92
Cdd:COG5265 369 PERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQAslRAA---IGIVPQDTVLFN 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 93 TlSVEENlklppvVASG--GMTLDEIY------------ELFPNLY-----ERrtspGTKLSGGEQQMLAMARILRTGVK 153
Cdd:COG5265 446 D-TIAYN------IAYGrpDASEEEVEaaaraaqihdfiESLPDGYdtrvgER----GLKLSGGEKQRVAIARTLLKNPP 514
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1610782141 154 VLLLDEPTEGLAPVIVQRIGEVLQKLkSRGMTVVLVeqnfrfASRI-----ADRFYLMDHGQMV 212
Cdd:COG5265 515 ILIFDEATSALDSRTERAIQAALREV-ARGRTTLVI------AHRLstivdADEILVLEAGRIV 571
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
16-212 |
1.92e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 62.15 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 16 ESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAK-----YGIGFVPEERGI 90
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKklrkkVSLVFQFPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 91 FATlSVEENLKLPPVvaSGGMTLDEIYE----------LFPNLYERrtSPgTKLSGGEQQMLAMARILRTGVKVLLLDEP 160
Cdd:PRK13641 99 FEN-TVLKDVEFGPK--NFGFSEDEAKEkalkwlkkvgLSEDLISK--SP-FELSGGQMRRVAIAGVMAYEPEILCLDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1610782141 161 TEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMV 212
Cdd:PRK13641 173 AAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLI 224
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
16-211 |
3.88e-11 |
|
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: 60.56 E-value: 3.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 16 ESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKdlmPVPL--HRTAKYGIGFVPEERGIFAT 93
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGK---PISQyeHKYLHSKVSLVGQEPVLFAR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 94 lSVEENLK--LPPV-------VASGGMTLDEIYELFPNLYERRTSPGTKLSGGEQQMLAMARILRTGVKVLLLDEPTEGL 164
Cdd:cd03248 103 -SLQDNIAygLQSCsfecvkeAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSAL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1610782141 165 APVIVQRIGEVLQKLKSRgMTVVLVEQNFRFASRiADRFYLMDHGQM 211
Cdd:cd03248 182 DAESEQQVQQALYDWPER-RTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-233 |
4.06e-11 |
|
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: 60.88 E-value: 4.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 26 TVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKYGI---GFVPEERGIFATLSVEENLKL 102
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADYEGtvrDLLSSITKDFYTHPYFKTEIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 103 PPvvasggMTLDEIyelfpnlYERRTspgTKLSGGEQQMLAMARILRTGVKVLLLDEPTEGL-------APVIVQRIGEV 175
Cdd:cd03237 101 KP------LQIEQI-------LDREV---PELSGGELQRVAIAACLSKDADIYLLDEPSAYLdveqrlmASKVIRRFAEN 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1610782141 176 LQKlksrgmTVVLVEQNFRFASRIADRFYLMDhGQ----MVSNFPVSELSGrMGELNKVLGV 233
Cdd:cd03237 165 NEK------TAFVVEHDIIMIDYLADRLIVFE-GEpsvnGVANPPQSLRSG-MNRFLKNLDI 218
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
20-189 |
4.47e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 61.75 E-value: 4.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 20 LHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKL-GGKDLMPVP---------LHRTAKYgigfvPEERG 89
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLFLPqrpylplgtLREALLY-----PATAE 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 90 IFATLSVEENLK---LPPVVASggmtLDEiyelfpnlyERRTSpgTKLSGGEQQMLAMARILRTGVKVLLLDEPTEGLAP 166
Cdd:COG4178 454 AFSDAELREALEavgLGHLAER----LDE---------EADWD--QVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDE 518
|
170 180
....*....|....*....|....*
gi 1610782141 167 VIVQRIgevLQKLKSR--GMTVVLV 189
Cdd:COG4178 519 ENEAAL---YQLLREElpGTTVISV 540
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
5-225 |
5.65e-11 |
|
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: 61.66 E-value: 5.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYG--ESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLhRTAKYGIG 82
Cdd:TIGR02203 331 VEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTL-ASLRRQVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 83 FVPEERGIFATlSVEENlklppvVASGGMT---------------LDEIYELFPN-LYERRTSPGTKLSGGEQQMLAMAR 146
Cdd:TIGR02203 410 LVSQDVVLFND-TIANN------IAYGRTEqadraeieralaaayAQDFVDKLPLgLDTPIGENGVLLSGGQRQRLAIAR 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 147 ILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLveqnfrfASRI-----ADRFYLMDHGQMVSNFPVSELS 221
Cdd:TIGR02203 483 ALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVI-------AHRLstiekADRIVVMDDGRIVERGTHNELL 555
|
....
gi 1610782141 222 GRMG 225
Cdd:TIGR02203 556 ARNG 559
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
4-211 |
9.09e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 59.83 E-value: 9.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 4 MLEVSNLKSWYGESQ----ALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPvpLHRTAK- 78
Cdd:PRK11629 5 LLQCDNLCKRYQEGSvqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSK--LSSAAKa 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 79 ----YGIGFVPEERGIFATLSVEENLKLPPVVasGGMTLDEIYE------LFPNLYERRTSPGTKLSGGEQQMLAMARIL 148
Cdd:PRK11629 83 elrnQKLGFIYQFHHLLPDFTALENVAMPLLI--GKKKPAEINSralemlAAVGLEHRANHRPSELSGGERQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1610782141 149 RTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSR-GMTVVLVEQNFRFASRIaDRFYLMDHGQM 211
Cdd:PRK11629 161 VNNPRLVLADEPTGNLDARNADSIFQLLGELNRLqGTAFLVVTHDLQLAKRM-SRQLEMRDGRL 223
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
18-221 |
9.17e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.90 E-value: 9.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 18 QALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKYGIGFVPEERGIFATLSVE 97
Cdd:PRK10982 12 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQELNLVLQRSVM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 98 ENLKL---PpvvaSGGMTLDE--IYELFPNLYER---RTSPGTK---LSGGEQQMLAMARILRTGVKVLLLDEPTEGLAP 166
Cdd:PRK10982 92 DNMWLgryP----TKGMFVDQdkMYRDTKAIFDEldiDIDPRAKvatLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1610782141 167 VIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPVSELS 221
Cdd:PRK10982 168 KEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLT 222
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
20-212 |
1.09e-10 |
|
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: 58.81 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 20 LHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGV---IKLGGKDlmPVPLHRTAKYGIGFVPEERGIFATLSV 96
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVegdIHYNGIP--YKEFAEKYPGEIIYVSEEDVHFPTLTV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 97 EEnlklppvvasggmTLDEIYELFPNLYERrtspgtKLSGGEQQMLAMARILRTGVKVLLLDEPTEGLAPVIVQRIGEVL 176
Cdd:cd03233 101 RE-------------TLDFALRCKGNEFVR------GISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCI 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1610782141 177 QKL--KSRGMTVVLVEQnfrfASRIA----DRFYLMDHGQMV 212
Cdd:cd03233 162 RTMadVLKTTTFVSLYQ----ASDEIydlfDKVLVLYEGRQI 199
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-223 |
1.25e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 60.31 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 1 MAAMLEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKdlmPVPLHRTA--- 77
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ---EMRFASTTaal 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 78 KYGIGFVPEERGIFATLSVEENLKLPPVVASGGMtLDE---IYELFPNLYE--RRTSPGTK---LSGGEQQMLAMARILR 149
Cdd:PRK11288 78 AAGVAIIYQELHLVPEMTVAENLYLGQLPHKGGI-VNRrllNYEAREQLEHlgVDIDPDTPlkyLSIGQRQMVEIAKALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 150 TGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFP----------VSE 219
Cdd:PRK11288 157 RNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATFDdmaqvdrdqlVQA 236
|
....
gi 1610782141 220 LSGR 223
Cdd:PRK11288 237 MVGR 240
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
111-192 |
2.09e-10 |
|
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: 60.03 E-value: 2.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 111 MTLDEIYELFPNL----------------YERRTSPGTKLSGGEQQMLAMARILR---TGVKVLLLDEPTEGLAPVIVQR 171
Cdd:TIGR00630 791 MTVEEAYEFFEAVpsisrklqtlcdvglgYIRLGQPATTLSGGEAQRIKLAKELSkrsTGRTLYILDEPTTGLHFDDIKK 870
|
90 100
....*....|....*....|.
gi 1610782141 172 IGEVLQKLKSRGMTVVLVEQN 192
Cdd:TIGR00630 871 LLEVLQRLVDKGNTVVVIEHN 891
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-214 |
2.28e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 58.79 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 26 TVGEGETITILGRNGVGKTTTLRTIMGIIRNrKGVIKLGGKDLMPVPLHRTAKYGIGFVPEERGIFAtLSVEENLKL--- 102
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFA-MPVFQYLTLhqp 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 103 -PPVVASGGMTLDEIYELFpNLYERRTSPGTKLSGGEQQMLAMA----RILRTG---VKVLLLDEPTEGLApvIVQR--I 172
Cdd:PRK03695 96 dKTRTEAVASALNEVAEAL-GLDDKLGRSVNQLSGGEWQRVRLAavvlQVWPDInpaGQLLLLDEPMNSLD--VAQQaaL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1610782141 173 GEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVSN 214
Cdd:PRK03695 173 DRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLAS 214
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
21-220 |
2.40e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 58.56 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 21 HGVDLTVGEGETITILGRNGVGKTTTLRTIMGI----IRNRKGVIKLGGKDLMPV-------------------PLHRTA 77
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGIlpagVRQTAGRVLLDGKPVAPCalrgrkiatimqnprsafnPLHTMH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 78 KYGIGFVpEERGIFATLSVeenlkLPPVVASGGMTLDE-IYELFPnlYErrtspgtkLSGGEQQ--MLAMAriLRTGVKV 154
Cdd:PRK10418 100 THARETC-LALGKPADDAT-----LTAALEAVGLENAArVLKLYP--FE--------MSGGMLQrmMIALA--LLCEAPF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1610782141 155 LLLDEPTEGLAPVIVQRIGEVLQKL-KSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPVSEL 220
Cdd:PRK10418 162 IIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-210 |
3.25e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 58.54 E-value: 3.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIkLGGKdlmpVPLHrTAKYGIGFV 84
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGT----APLA-EAREDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 85 PEERGIFATLSVEENLKLppvvasgGMT----------LDEIyelfpNLYERRTSPGTKLSGGEQQMLAMARILRTGVKV 154
Cdd:PRK11247 87 FQDARLLPWKKVIDNVGL-------GLKgqwrdaalqaLAAV-----GLADRANEWPAALSGGQKQRVALARALIHRPGL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1610782141 155 LLLDEPTEGLAPVIVQRIGEVLQKL-KSRGMTVVLVEQNFRFASRIADRFYLMDHGQ 210
Cdd:PRK11247 155 LLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-227 |
3.66e-10 |
|
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: 59.05 E-value: 3.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMG----------IIRN-----RKGVIKLGGKDLM 69
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdqyeptsgrIIYHvalceKCGYVERPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 70 PVPL--HRTAKYGIGFVPEERGIFATL------------------SVEENL--KLPPVVASGGMTLDEIYELFP--NLYE 125
Cdd:TIGR03269 81 PCPVcgGTLEPEEVDFWNLSDKLRRRIrkriaimlqrtfalygddTVLDNVleALEEIGYEGKEAVGRAVDLIEmvQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 126 RRTSPGTKLSGGEQQMLAMARILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKL-KSRGMTVVLVEQNFRFASRIADRFY 204
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSHWPEVIEDLSDKAI 240
|
250 260
....*....|....*....|...
gi 1610782141 205 LMDHGQMVSNFPVSELSGRMGEL 227
Cdd:TIGR03269 241 WLENGEIKEEGTPDEVVAVFMEG 263
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
4-220 |
4.72e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 57.91 E-value: 4.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 4 MLEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNR--------KGVIKLGGKDLMPVPLHR 75
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 76 TAKYGIGFVPEERGIFAtLSVEENLKLP--PVVASGGMTLDEIYELFPNLYERRTSPG------TKLSGGEQQMLAMARI 147
Cdd:PRK13547 81 LARLRAVLPQAAQPAFA-FSAREIVLLGryPHARRAGALTHRDGEIAWQALALAGATAlvgrdvTTLSGGELARVQFARV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 148 L---------RTGVKVLLLDEPTEGLAPVIVQRIGEVLQKL-KSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPV 217
Cdd:PRK13547 160 LaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLaRDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAP 239
|
...
gi 1610782141 218 SEL 220
Cdd:PRK13547 240 ADV 242
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-62 |
7.01e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 58.36 E-value: 7.01e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1610782141 5 LEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIK 62
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK 377
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-220 |
7.16e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 57.47 E-value: 7.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 1 MAAMLEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHR--TAK 78
Cdd:PRK11831 4 VANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRlyTVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 79 YGIGFVPEERGIFATLSVEENLKLP---------PVVASGGMT------LDEIYELFPNlyerrtspgtKLSGGEQQMLA 143
Cdd:PRK11831 84 KRMSMLFQSGALFTDMNVFDNVAYPlrehtqlpaPLLHSTVMMkleavgLRGAAKLMPS----------ELSGGMARRAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 144 MARILRTGVKVLLLDEPTEGLAP----VIVQRIGEVLQKLksrGMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPVSE 219
Cdd:PRK11831 154 LARAIALEPDLIMFDEPFVGQDPitmgVLVKLISELNSAL---GVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQA 230
|
.
gi 1610782141 220 L 220
Cdd:PRK11831 231 L 231
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
18-225 |
7.68e-10 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 58.20 E-value: 7.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 18 QALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMP---VPLHRTakygIGFVPEERGIFATl 94
Cdd:TIGR00958 495 PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQydhHYLHRQ----VALVGQEPVLFSG- 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 95 SVEEN----LKLPP-----VVASGGMTLDEIYElFPNLYERRTSP-GTKLSGGEQQMLAMARILRTGVKVLLLDEPTEGL 164
Cdd:TIGR00958 570 SVRENiaygLTDTPdeeimAAAKAANAHDFIME-FPNGYDTEVGEkGSQLSGGQKQRIAIARALVRKPRVLILDEATSAL 648
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1610782141 165 ApvivQRIGEVLQKLKSR-GMTVVLVEQNFRFASRiADRFYLMDHGQMVSNFPVSELSGRMG 225
Cdd:TIGR00958 649 D----AECEQLLQESRSRaSRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQG 705
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
4-221 |
1.11e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 57.49 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 4 MLEVSNLKSW---YGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGII--RNRKGVIKLGGK--DLMPVPlhRT 76
Cdd:NF040905 257 VFEVKNWTVYhplHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISGTVFKDGKevDVSTVS--DA 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 77 AKYGIGFVPEER---GIFATLSVEENLKLP--PVVASGGMtLDEIYEL-FPNLYERRT---SPGT-----KLSGGEQQML 142
Cdd:NF040905 335 IDAGLAYVTEDRkgyGLNLIDDIKRNITLAnlGKVSRRGV-IDENEEIkVAEEYRKKMnikTPSVfqkvgNLSGGNQQKV 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 143 AMARILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVeqnfrfASR------IADRFYLMDHGQMVSNFP 216
Cdd:NF040905 414 VLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVI------SSElpellgMCDRIYVMNEGRITGELP 487
|
....*
gi 1610782141 217 VSELS 221
Cdd:NF040905 488 REEAS 492
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
5-225 |
2.27e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 56.35 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGESQ--ALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGII---RNRKGVI-----KLGGKDLMPVplh 74
Cdd:PRK13640 6 VEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKItvdgiTLTAKTVWDI--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 75 rTAKYGIGFV-PEERGIFATLSVE-----ENLKLP---------PVVASGGMTldeiyelfpnlyERRTSPGTKLSGGEQ 139
Cdd:PRK13640 83 -REKVGIVFQnPDNQFVGATVGDDvafglENRAVPrpemikivrDVLADVGML------------DYIDSEPANLSGGQK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 140 QMLAMARILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKL-KSRGMTVVLVEQNFRFASrIADRFYLMDHGQMVSN---- 214
Cdd:PRK13640 150 QRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLkKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQgspv 228
|
250
....*....|...
gi 1610782141 215 --FPVSELSGRMG 225
Cdd:PRK13640 229 eiFSKVEMLKEIG 241
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-225 |
2.91e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 56.67 E-value: 2.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 6 EVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDlMPVPLHRTAKYG-IGFV 84
Cdd:NF033858 3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGD-MADARHRRAVCPrIAYM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 85 PEERG--IFATLSVEENLklppvvasggmtldeiyELFPNLY-----ERR----------------TSPGTKLSGGEQQM 141
Cdd:NF033858 82 PQGLGknLYPTLSVFENL-----------------DFFGRLFgqdaaERRrridellratglapfaDRPAGKLSGGMKQK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 142 LAM--ARI----LrtgvkvLLLDEPTEGLAPVIVQRIGEVLQKLKSR--GMTvVLV------EqnfrfasriADRF-YL- 205
Cdd:NF033858 145 LGLccALIhdpdL------LILDEPTTGVDPLSRRQFWELIDRIRAErpGMS-VLVataymeE---------AERFdWLv 208
|
250 260
....*....|....*....|.
gi 1610782141 206 -MDHGQMVSNFPVSELSGRMG 225
Cdd:NF033858 209 aMDAGRVLATGTPAELLARTG 229
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-161 |
9.64e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.74 E-value: 9.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGgkdlmpvplhRTAKygIGFV 84
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIG----------ETVK--LAYV 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 85 PEER-GIFATLSVEEnlklppvVASGGmtLDEIYelfpnlYERRTSP-----------GT-------KLSGGEQQMLAMA 145
Cdd:PRK11819 393 DQSRdALDPNKTVWE-------EISGG--LDIIK------VGNREIPsrayvgrfnfkGGdqqkkvgVLSGGERNRLHLA 457
|
170
....*....|....*.
gi 1610782141 146 RILRTGVKVLLLDEPT 161
Cdd:PRK11819 458 KTLKQGGNVLLLDEPT 473
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
5-212 |
1.14e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 54.72 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGESQ-ALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPlHRTAKYGIGF 83
Cdd:PRK10790 341 IDIDNVSFAYRDDNlVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLS-HSVLRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 84 VPEERGIFATlSVEENLKLPPVVASGGM-------TLDEIYELFPN-LYERRTSPGTKLSGGEQQMLAMARILRTGVKVL 155
Cdd:PRK10790 420 VQQDPVVLAD-TFLANVTLGRDISEEQVwqaletvQLAELARSLPDgLYTPLGEQGNNLSVGQKQLLALARVLVQTPQIL 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1610782141 156 LLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEqnfRFASRI-ADRFYLMDHGQMV 212
Cdd:PRK10790 499 ILDEATANIDSGTEQAIQQALAAVREHTTLVVIAH---RLSTIVeADTILVLHRGQAV 553
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
16-181 |
1.36e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 53.99 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 16 ESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKYgIGFV---PEERGIFA 92
Cdd:PRK13648 21 ASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKH-IGIVfqnPDNQFVGS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 93 TLSVE-----ENLKLPpvvasggmtLDEIYELFP------NLYERRTSPGTKLSGGEQQMLAMARILRTGVKVLLLDEPT 161
Cdd:PRK13648 100 IVKYDvafglENHAVP---------YDEMHRRVSealkqvDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEAT 170
|
170 180
....*....|....*....|
gi 1610782141 162 EGLAPVIVQRIGEVLQKLKS 181
Cdd:PRK13648 171 SMLDPDARQNLLDLVRKVKS 190
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
15-164 |
1.74e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 53.18 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 15 GESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKYgIGFVPEERGIFATl 94
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQ-VSYCAQTPTLFGD- 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1610782141 95 SVEENLKLP-------PVVASGGMTLDEiYELFPNLYERRTspgTKLSGGEQQMLAMARILRTGVKVLLLDEPTEGL 164
Cdd:PRK10247 96 TVYDNLIFPwqirnqqPDPAIFLDDLER-FALPDTILTKNI---AELSGGEKQRISLIRNLQFMPKVLLLDEITSAL 168
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
17-226 |
1.79e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 54.63 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 17 SQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMP--VPLHRTakygIGFVPEERGIFATL 94
Cdd:TIGR01257 1952 SPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTniSDVHQN----MGYCPQFDAIDDLL 2027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 95 SVEENLKL------PPVVASGGMTLDEIYELFPNLYERRTSpGTkLSGGEQQMLAMARILRTGVKVLLLDEPTEGLAPVI 168
Cdd:TIGR01257 2028 TGREHLYLyarlrgVPAEEIEKVANWSIQSLGLSLYADRLA-GT-YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQA 2105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1610782141 169 VQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFPVSELSGRMGE 226
Cdd:TIGR01257 2106 RRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGD 2163
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
134-201 |
1.98e-08 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 54.45 E-value: 1.98e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1610782141 134 LSGGEQQMLAMARIL---RTGVkVLLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVE---QNFRFASRIAD 201
Cdd:PRK00635 477 LSGGEQERTALAKHLgaeLIGI-TYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEhdeQMISLADRIID 549
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
16-187 |
2.22e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 54.12 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 16 ESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIR--NRKGVIKLGGKDLMPVPLHRTakygiGFVPEERGIFAT 93
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQgnNFTGTILANNRKPTKQILKRT-----GFVTQDDILYPH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 94 LSVEENL------KLP-------------PVVASGGMTLDEiYELFPNLYERrtspgtKLSGGEQQMLAMARILRTGVKV 154
Cdd:PLN03211 155 LTVRETLvfcsllRLPksltkqekilvaeSVISELGLTKCE-NTIIGNSFIR------GISGGERKRVSIAHEMLINPSL 227
|
170 180 190
....*....|....*....|....*....|...
gi 1610782141 155 LLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVV 187
Cdd:PLN03211 228 LILDEPTSGLDATAAYRLVLTLGSLAQKGKTIV 260
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
15-231 |
2.70e-08 |
|
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: 53.80 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 15 GESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGviklggkdlmpvplHRTAKYGIGFVPEERGIfATL 94
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEG--------------HVHMKGSVAYVPQQAWI-QND 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 95 SVEENLKLppvvasgGMTLDEIY--------ELFPNLY----ERRTSPGTK---LSGGEQQMLAMARILRTGVKVLLLDE 159
Cdd:TIGR00957 714 SLRENILF-------GKALNEKYyqqvleacALLPDLEilpsGDRTEIGEKgvnLSGGQKQRVSLARAVYSNADIYLFDD 786
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1610782141 160 PTEGLAPVIVQRIGEVLQKLKS--RGMTVVLVEQNFRFASRIaDRFYLMDHGQMVSNFPVSELSGRMGELNKVL 231
Cdd:TIGR00957 787 PLSAVDAHVGKHIFEHVIGPEGvlKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQRDGAFAEFL 859
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
19-202 |
2.87e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 53.25 E-value: 2.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 19 ALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGI---------IRNRKGVIKLGGkdlmpvpLHRTAKYGIGFVPEERG 89
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVyphgsyegeILFDGEVCRFKD-------IRDSEALGIVIIHQELA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 90 IFATLSVEENLKLPPVVASGGM-----TLDEIYELFP--NLYERRTSPGTKLSGGEQQMLAMARILRTGVKVLLLDEPTE 162
Cdd:NF040905 89 LIPYLSIAENIFLGNERAKRGVidwneTNRRARELLAkvGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1610782141 163 GLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADR 202
Cdd:NF040905 169 ALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADS 208
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
111-192 |
4.23e-08 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 53.15 E-value: 4.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 111 MTLDEIYELF---PNLYER-RT------------SPGTKLSGGEQQMLAMARILR---TGVKVLLLDEPTEGLAPVIVQR 171
Cdd:PRK00349 792 MTVEEALEFFeaiPKIARKlQTlvdvglgyiklgQPATTLSGGEAQRVKLAKELSkrsTGKTLYILDEPTTGLHFEDIRK 871
|
90 100
....*....|....*....|.
gi 1610782141 172 IGEVLQKLKSRGMTVVLVEQN 192
Cdd:PRK00349 872 LLEVLHRLVDKGNTVVVIEHN 892
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
23-211 |
5.16e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 52.75 E-value: 5.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 23 VDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPV-PLHRTAKyGIGFVPEER---GIFATLSVEE 98
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALsTAQRLAR-GLVYLPEDRqssGLYLDAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 99 NLkLPPVVASGGMTLDEIYElfPNLYER-RTSPGTK----------LSGGEQQMLAMARILRTGVKVLLLDEPTEGLAPV 167
Cdd:PRK15439 361 NV-CALTHNRRGFWIKPARE--NAVLERyRRALNIKfnhaeqaartLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVS 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1610782141 168 IVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQM 211
Cdd:PRK15439 438 ARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
134-210 |
5.38e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 51.17 E-value: 5.38e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1610782141 134 LSGGEQQMLAMARIL--RTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRiADRFYLMDHGQ 210
Cdd:cd03238 88 LSGGELQRVKLASELfsEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSS-ADWIIDFGPGS 165
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
16-212 |
5.43e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.79 E-value: 5.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 16 ESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNR-----KGVIKLGGKDLM--------------------- 69
Cdd:PRK15134 21 VRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLhaseqtlrgvrgnkiamifqe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 70 PV----PLHRTakygigfvpeERGIFATLSVEENLKLPPVVASGGMTLDEIYelFPNLYERRTSPGTKLSGGEQQ--MLA 143
Cdd:PRK15134 101 PMvslnPLHTL----------EKQLYEVLSLHRGMRREAARGEILNCLDRVG--IRQAAKRLTDYPHQLSGGERQrvMIA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1610782141 144 MAriLRTGVKVLLLDEPTEGLaPVIVQ-RIGEVLQKLKSR-GMTVVLVEQNFRFASRIADRFYLMDHGQMV 212
Cdd:PRK15134 169 MA--LLTRPELLIADEPTTAL-DVSVQaQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCV 236
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-202 |
6.35e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 52.48 E-value: 6.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 26 TVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKdlmpvplhrtakygIGFVPEERGIFATLSVEENLK--LP 103
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK--------------ISYKPQYISPDYDGTVEEFLRsaNT 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 104 PVVASG--------GMTLDEIYElfpnlyerrtSPGTKLSGGEQQMLAMARILRTGVKVLLLDEPTEGLApvIVQRI--G 173
Cdd:COG1245 428 DDFGSSyykteiikPLGLEKLLD----------KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD--VEQRLavA 495
|
170 180 190
....*....|....*....|....*....|
gi 1610782141 174 EVLQKL-KSRGMTVVLVEQNFRFASRIADR 202
Cdd:COG1245 496 KAIRRFaENRGKTAMVVDHDIYLIDYISDR 525
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-213 |
6.63e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 51.91 E-value: 6.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 2 AAMLEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKYgI 81
Cdd:PRK10253 5 VARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARR-I 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 82 GFVPEERGIFATLSVEEnlklppVVASGGMTLDEIYELFPNLYERRTSPGTK--------------LSGGEQQMLAMARI 147
Cdd:PRK10253 84 GLLAQNATTPGDITVQE------LVARGRYPHQPLFTRWRKEDEEAVTKAMQatgithladqsvdtLSGGQRQRAWIAMV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1610782141 148 LRTGVKVLLLDEPTEGLApvIVQRIG--EVLQKL-KSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVS 213
Cdd:PRK10253 158 LAQETAIMLLDEPTTWLD--ISHQIDllELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVA 224
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
111-192 |
9.57e-08 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 51.95 E-value: 9.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 111 MTLDEIYELF---PNLYER-RT------------SPGTKLSGGEQQMLAMARIL---RTGVKVLLLDEPTEGLAPVIVQR 171
Cdd:COG0178 788 MTVEEALEFFeniPKIARKlQTlqdvglgyiklgQPATTLSGGEAQRVKLASELskrSTGKTLYILDEPTTGLHFHDIRK 867
|
90 100
....*....|....*....|.
gi 1610782141 172 IGEVLQKLKSRGMTVVLVEQN 192
Cdd:COG0178 868 LLEVLHRLVDKGNTVVVIEHN 888
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-225 |
9.80e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 52.29 E-value: 9.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 20 LHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKG--------VIKLGGKDLM---------PVPLHRTAKYGIG 82
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGrimiddcdVAKFGLTDLRrvlsiipqsPVLFSGTVRFNID 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 83 FVPE--ERGIFATLsveENLKLPPVVASGGMTLD-EIYElfpnlyerrtsPGTKLSGGEQQMLAMARILRTGVKVLLLDE 159
Cdd:PLN03232 1332 PFSEhnDADLWEAL---ERAHIKDVIDRNPFGLDaEVSE-----------GGENFSVGQRQLLSLARALLRRSKILVLDE 1397
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1610782141 160 PTeglAPVIVqRIGEVLQK-----LKSRGMTVVLveqnFRFASRI-ADRFYLMDHGQMVSNFPVSELSGRMG 225
Cdd:PLN03232 1398 AT---ASVDV-RTDSLIQRtireeFKSCTMLVIA----HRLNTIIdCDKILVLSSGQVLEYDSPQELLSRDT 1461
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
112-201 |
1.68e-07 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 50.33 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 112 TLDEIYELFPNLYER---------------------RTSPgtKLSGGEQQMLAMARILRTGVKVLL--LDEPTEGLAPVI 168
Cdd:cd03270 97 TVTEIYDYLRLLFARvgirerlgflvdvglgyltlsRSAP--TLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRD 174
|
90 100 110
....*....|....*....|....*....|....*.
gi 1610782141 169 VQRIGEVLQKLKSRGMTVVLVE---QNFRFASRIAD 201
Cdd:cd03270 175 NDRLIETLKRLRDLGNTVLVVEhdeDTIRAADHVID 210
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
23-187 |
2.12e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 49.85 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 23 VDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKYgIGFVPeerGIFATLSVEENLKL 102
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAY-LGHLP---GLKADLSTLENLHF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 103 --------PPVVASGGMTLdeiyelfPNLYERRTSPGTKLSGGEQQMLAMARILRTGVKVLLLDEPTEGLAP---VIVQR 171
Cdd:PRK13543 106 lcglhgrrAKQMPGSALAI-------VGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLegiTLVNR 178
|
170
....*....|....*.
gi 1610782141 172 IgeVLQKLKSRGMTVV 187
Cdd:PRK13543 179 M--ISAHLRGGGAALV 192
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-189 |
2.60e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 49.57 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 16 ESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGViklGGKDLMPVPLhrtakygigfvPEERGIfatls 95
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVA---GCVDVPDNQF-----------GREASL----- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 96 VEENLKLPPVVAS----GGMTLDEIYelfpnLYERRTSpgtKLSGGEQQMLAMARILRTGVKVLLLDEPTEGLAPVIVQR 171
Cdd:COG2401 103 IDAIGRKGDFKDAvellNAVGLSDAV-----LWLRRFK---ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKR 174
|
170
....*....|....*....
gi 1610782141 172 IGEVLQKL-KSRGMTVVLV 189
Cdd:COG2401 175 VARNLQKLaRRAGITLVVA 193
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
16-231 |
2.90e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 50.74 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 16 ESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRK--GVIKLGGKDLMP-VP------LHRTAKYGIGFVPE 86
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAEtsSVVIRGSVAYVPqVSwifnatVRENILFGSDFESE 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 87 E--RGIFATlSVEENLKLPPvvasgGMTLDEIYElfpnlyerrtsPGTKLSGGEQQMLAMARILRTGVKVLLLDEPTEGL 164
Cdd:PLN03232 709 RywRAIDVT-ALQHDLDLLP-----GRDLTEIGE-----------RGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSAL 771
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1610782141 165 APVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIaDRFYLMDHGQMVSNFPVSELSgRMGELNKVL 231
Cdd:PLN03232 772 DAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELS-KSGSLFKKL 836
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
56-164 |
3.42e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.41 E-value: 3.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 56 NRKGVIKLGGKDLMPVPLhRTAKYGIGFVPEERGIFaTLSVEENLKLPPVVA--------SGGMTLDEIYELFPNLYERR 127
Cdd:PTZ00265 1274 KNSGKILLDGVDICDYNL-KDLRNLFSIVSQEPMLF-NMSIYENIKFGKEDAtredvkraCKFAAIDEFIESLPNKYDTN 1351
|
90 100 110
....*....|....*....|....*....|....*...
gi 1610782141 128 TSP-GTKLSGGEQQMLAMARILRTGVKVLLLDEPTEGL 164
Cdd:PTZ00265 1352 VGPyGKSLSGGQKQRIAIARALLREPKILLLDEATSSL 1389
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
130-201 |
3.49e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 50.60 E-value: 3.49e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1610782141 130 PGTKLSGGEQQMLAMARILRTGVK---VLLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFAsRIAD 201
Cdd:PRK00635 806 PLSSLSGGEIQRLKLAYELLAPSKkptLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVV-KVAD 879
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-216 |
4.20e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.95 E-value: 4.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 3 AMLEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGgKDLM-------PvPLHR 75
Cdd:PRK11147 2 SLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE-QDLIvarlqqdP-PRNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 76 TAKY------GIGFVPEERGIFATLSV-------EENL-KLPPVVA----SGGMTLD-EIYELFPNLYERRTSPGTKLSG 136
Cdd:PRK11147 80 EGTVydfvaeGIEEQAEYLKRYHDISHlvetdpsEKNLnELAKLQEqldhHNLWQLEnRINEVLAQLGLDPDAALSSLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 137 GEQQMLAMARILRTGVKVLLLDEPTEGLApviVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVSnFP 216
Cdd:PRK11147 160 GWLRKAALGRALVSNPDVLLLDEPTNHLD---IETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVS-YP 235
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-203 |
4.46e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.81 E-value: 4.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 29 EGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKdlmpvplhrtakygIGFVPEERGIFATLSVEENLKLPPVVAS 108
Cdd:PRK13409 364 EGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK--------------ISYKPQYIKPDYDGTVEDLLRSITDDLG 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 109 GGMTLDEIYELF--PNLYERRTspgTKLSGGEQQMLAMARILRTGVKVLLLDEPTEGL--------APVIvQRIGEvlqk 178
Cdd:PRK13409 430 SSYYKSEIIKPLqlERLLDKNV---KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLdveqrlavAKAI-RRIAE---- 501
|
170 180
....*....|....*....|....*
gi 1610782141 179 lkSRGMTVVLVEQNFRFASRIADRF 203
Cdd:PRK13409 502 --EREATALVVDHDIYMIDYISDRL 524
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
30-164 |
5.22e-07 |
|
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: 49.55 E-value: 5.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 30 GETITILGRNGVGKTTTLRTIMGIIRNRKGviklggkDLMPVPlhrtaKYGIGFVPEERGIFATLSVEENLK--LPPVVA 107
Cdd:TIGR03719 31 GAKIGVLGLNGAGKSTLLRIMAGVDKDFNG-------EARPQP-----GIKVGYLPQEPQLDPTKTVRENVEegVAEIKD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 108 SggMT-LDEIYELF--PN-----LYER---------------------------RTSPG----TKLSGGEQQMLAMARIL 148
Cdd:TIGR03719 99 A--LDrFNEISAKYaePDadfdkLAAEqaelqeiidaadawdldsqleiamdalRCPPWdadvTKLSGGERRRVALCRLL 176
|
170
....*....|....*.
gi 1610782141 149 RTGVKVLLLDEPTEGL 164
Cdd:TIGR03719 177 LSKPDMLLLDEPTNHL 192
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
3-220 |
5.99e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 49.35 E-value: 5.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 3 AMLEVSNLKSWYGES----QALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGII----RNRKGVIKLGGKDLMPVPLH 74
Cdd:PRK11022 2 ALLNVDKLSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDLQRISEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 75 RTAK--------------------YGIGFvpeerGIFATLSVEE--NLKLPPVVASGGMTLDEIyelfPNLYERRTSPGT 132
Cdd:PRK11022 82 ERRNlvgaevamifqdpmtslnpcYTVGF-----QIMEAIKVHQggNKKTRRQRAIDLLNQVGI----PDPASRLDVYPH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 133 KLSGGEQQ--MLAMARILRTgvKVLLLDEPTEGLAPVIVQRIGEVLQKLKSR-GMTVVLVEQNFRFASRIADRFYLMDHG 209
Cdd:PRK11022 153 QLSGGMSQrvMIAMAIACRP--KLLIADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAG 230
|
250
....*....|.
gi 1610782141 210 QMVSNFPVSEL 220
Cdd:PRK11022 231 QVVETGKAHDI 241
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
12-216 |
8.97e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 48.34 E-value: 8.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 12 SWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKdlmpvPLHRTAKYG-IGFVPEERGI 90
Cdd:PRK15056 15 TWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQ-----PTRQALQKNlVAYVPQSEEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 91 ---FATLsVEENLKLPPVVASGGM---------TLDEIYELFPNLYERRTSPGtKLSGGEQQMLAMARILRTGVKVLLLD 158
Cdd:PRK15056 90 dwsFPVL-VEDVVMMGRYGHMGWLrrakkrdrqIVTAALARVDMVEFRHRQIG-ELSGGQKKRVFLARAIAQQGQVILLD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1610782141 159 EPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADrFYLMDHGQMVSNFP 216
Cdd:PRK15056 168 EPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGP 224
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
4-220 |
1.01e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.08 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 4 MLEVSNLKSWYGESQ----ALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGII----------------RNRKgVIKL 63
Cdd:PRK10261 12 VLAVENLNIAFMQEQqkiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLeqagglvqcdkmllrrRSRQ-VIEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 64 GGKDLMPVPLHRTAKYGIGF----------VPEERGIFATLSVEENLKLPPVVASGGMTLDEIYelFPNLYERRTSPGTK 133
Cdd:PRK10261 91 SEQSAAQMRHVRGADMAMIFqepmtslnpvFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVR--IPEAQTILSRYPHQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 134 LSGGEQQ--MLAMARILRTGVkvLLLDEPTEGLAPVIVQRIGEVLQKL-KSRGMTVVLVEQNFRFASRIADRFYLMDHGQ 210
Cdd:PRK10261 169 LSGGMRQrvMIAMALSCRPAV--LIADEPTTALDVTIQAQILQLIKVLqKEMSMGVIFITHDMGVVAEIADRVLVMYQGE 246
|
250
....*....|
gi 1610782141 211 MVSNFPVSEL 220
Cdd:PRK10261 247 AVETGSVEQI 256
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
20-212 |
1.24e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.97 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 20 LHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRTAKYgIGFVPEERGIFATlSVEEN 99
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKV-LGIIPQAPVLFSG-TVRFN 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 100 L------------------KLPPVVASGGMTLD-EIYElfpnlyerrtsPGTKLSGGEQQMLAMARILRTGVKVLLLDEP 160
Cdd:PLN03130 1333 LdpfnehndadlwesleraHLKDVIRRNSLGLDaEVSE-----------AGENFSVGQRQLLSLARALLRRSKILVLDEA 1401
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1610782141 161 TeglAPVIVqRIGEVLQK-----LKSRGMTVVlveqnfrfASRI-----ADRFYLMDHGQMV 212
Cdd:PLN03130 1402 T---AAVDV-RTDALIQKtireeFKSCTMLII--------AHRLntiidCDRILVLDAGRVV 1451
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-161 |
1.33e-06 |
|
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: 48.79 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 20 LHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHrTAKYGIGFVPEERGIFatlSVEEN 99
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLH-DLRFKITIIPQDPVLF---SGSLR 1377
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1610782141 100 LKLPPVvasGGMTLDEIY---EL---------FPNLYERRTSPGTK-LSGGEQQMLAMARILRTGVKVLLLDEPT 161
Cdd:TIGR00957 1378 MNLDPF---SQYSDEEVWwalELahlktfvsaLPDKLDHECAEGGEnLSVGQRQLVCLARALLRKTKILVLDEAT 1449
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-216 |
1.37e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 48.70 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 16 ESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGK--DLMPVPLHRTAKYGIGFVPEERgiFAT 93
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQriDTLSPGKLQALRRDIQFIFQDP--YAS 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 94 LSVEENLK---LPPVVASGGMTLDEIYELFPNLYERrtsPGTK----------LSGGEQQMLAMARILRTGVKVLLLDEP 160
Cdd:PRK10261 414 LDPRQTVGdsiMEPLRVHGLLPGKAAAARVAWLLER---VGLLpehawrypheFSGGQRQRICIARALALNPKVIIADEA 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1610782141 161 TEGLAPVIVQRIGEVLQKL-KSRGMTVVLVEQNFRFASRIADRFYLMDHGQMVSNFP 216
Cdd:PRK10261 491 VSALDVSIRGQIINLLLDLqRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGP 547
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-221 |
1.77e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 48.30 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGESQALHG-VDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRkGVIKLGGKDLMPVPLHRTAKYgIGF 83
Cdd:PRK11174 350 IEAEDLEILSPDGKTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRELDPESWRKH-LSW 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 84 VPEERGIFATlSVEENLKLPPVVASGGMT--------LDEIYELFPNLYERRTSPGT-KLSGGEQQMLAMARILRTGVKV 154
Cdd:PRK11174 428 VGQNPQLPHG-TLRDNVLLGNPDASDEQLqqalenawVSEFLPLLPQGLDTPIGDQAaGLSVGQAQRLALARALLQPCQL 506
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1610782141 155 LLLDEPTEGLAPVIVQRIGEVLQKLkSRGMTVVLVEQNFRFASRIaDRFYLMDHGQMVSNFPVSELS 221
Cdd:PRK11174 507 LLLDEPTASLDAHSEQLVMQALNAA-SRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELS 571
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
14-190 |
1.96e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.88 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 14 YGESQ-ALHGVDlTVGEGETITILGRNGVGKTTTLRTIMGIIR----------NRKGVI-------------KLGGKDLM 69
Cdd:PRK13409 83 YGVNGfKLYGLP-IPKEGKVTGILGPNGIGKTTAVKILSGELIpnlgdyeeepSWDEVLkrfrgtelqnyfkKLYNGEIK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 70 PV--P--LHRTAKYGIGFVPE------ERGIFatlsveenlklppvvasggmtlDEIYELF--PNLYERRTSpgtKLSGG 137
Cdd:PRK13409 162 VVhkPqyVDLIPKVFKGKVREllkkvdERGKL----------------------DEVVERLglENILDRDIS---ELSGG 216
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1610782141 138 EQQMLAMARILRTGVKVLLLDEPTEGLApvIVQRI--GEVLQKLkSRGMTVVLVE 190
Cdd:PRK13409 217 ELQRVAIAAALLRDADFYFFDEPTSYLD--IRQRLnvARLIREL-AEGKYVLVVE 268
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
20-209 |
2.15e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.24 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 20 LHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLhRTAKYGIGFVPEERGIFATlSVEEN 99
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGL-RELRRQFSMIPQDPVLFDG-TVRQN 1403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 100 LKlPPVVASGGmtldEIY---ELFpNLYERRTSP-----------GTKLSGGEQQMLAMAR-ILRTGVKVLLLDEPTEGL 164
Cdd:PTZ00243 1404 VD-PFLEASSA----EVWaalELV-GLRERVASEsegidsrvlegGSNYSVGQRQLMCMARaLLKKGSGFILMDEATANI 1477
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1610782141 165 APVIVQRIGEVLQKLKSrGMTVVLVEQNFRFASRIaDRFYLMDHG 209
Cdd:PTZ00243 1478 DPALDRQIQATVMSAFS-AYTVITIAHRLHTVAQY-DKIIVMDHG 1520
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
4-159 |
2.33e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 46.79 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 4 MLEVSNLkSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDlmpvpLHRTAKYGIGF 83
Cdd:PRK13541 1 MLSLHQL-QFNIEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCN-----INNIAKPYCTY 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1610782141 84 VPEERGIFATLSVEENLKLPPVVASGGMTLDEIYELFpNLYERRTSPGTKLSGGEQQMLAMARILRTGVKVLLLDE 159
Cdd:PRK13541 75 IGHNLGLKLEMTVFENLKFWSEIYNSAETLYAAIHYF-KLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDE 149
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-211 |
2.75e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.47 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 4 MLEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKdlmpVPLHRTAKYGIGF 83
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKG----IKLGYFAQHQLEF 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 84 VPEERGIFATLS----VEENLKLPPVVASGGMTLDEIyelfpnlyerrTSPGTKLSGGEQQMLAMARILRTGVKVLLLDE 159
Cdd:PRK10636 388 LRADESPLQHLArlapQELEQKLRDYLGGFGFQGDKV-----------TEETRRFSGGEKARLVLALIVWQRPNLLLLDE 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1610782141 160 PTEGLAPVIVQRIGEVLQKLKSrgmTVVLVEQNFRFASRIADRFYLMDHGQM 211
Cdd:PRK10636 457 PTNHLDLDMRQALTEALIDFEG---ALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
12-209 |
3.73e-06 |
|
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: 46.17 E-value: 3.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 12 SWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPLHRT---AKYGIGFVPEER 88
Cdd:cd03290 9 SWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrNRYSVAYAAQKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 89 GIFaTLSVEENL-------KLPPVVASGGMTLDEIYELFP-----NLYERrtspGTKLSGGEQQMLAMARILRTGVKVLL 156
Cdd:cd03290 89 WLL-NATVEENItfgspfnKQRYKAVTDACSLQPDIDLLPfgdqtEIGER----GINLSGGQRQRICVARALYQNTNIVF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1610782141 157 LDEPTEGLAPVIVQRIGE--VLQKLKSRGMTVVLVEQNFRFASRiADRFYLMDHG 209
Cdd:cd03290 164 LDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
134-220 |
3.99e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 46.70 E-value: 3.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 134 LSGGEQQMLAMARILRTGVKVLLLDEPTEGLApvIVQRIgEVL---QKL-KSRGMTVVLVEQNFRFASRIADRFYLMDHG 209
Cdd:PRK10575 148 LSGGERQRAWIAMLVAQDSRCLLLDEPTSALD--IAHQV-DVLalvHRLsQERGLTVIAVLHDINMAARYCDYLVALRGG 224
|
90
....*....|.
gi 1610782141 210 QMVSNFPVSEL 220
Cdd:PRK10575 225 EMIAQGTPAEL 235
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
133-220 |
1.49e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 45.18 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 133 KLSGGEQQMLAMARILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKL-KSRGMTVVLVEQNFRFASRIADRFYLMDHGQM 211
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVLYCGQT 237
|
....*....
gi 1610782141 212 VSNFPVSEL 220
Cdd:PRK15093 238 VETAPSKEL 246
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
14-190 |
1.51e-05 |
|
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: 45.16 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 14 YGESQ-ALHGVDlTVGEGETITILGRNGVGKTTTLRTIMGIIR-N-----------------------------RKGVIK 62
Cdd:COG1245 83 YGENGfRLYGLP-VPKKGKVTGILGPNGIGKSTALKILSGELKpNlgdydeepswdevlkrfrgtelqdyfkklANGEIK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 63 LGGK----DLMPvplhrtaKYGIGFVPE------ERGIFATLSVEENLKlppvvasggmtldeiyelfpNLYERRTSpgt 132
Cdd:COG1245 162 VAHKpqyvDLIP-------KVFKGTVREllekvdERGKLDELAEKLGLE--------------------NILDRDIS--- 211
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 133 KLSGGEQQMLAMARILRTGVKVLLLDEPTEGLApvIVQRI--GEVLQKLKSRGMTVVLVE 190
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLD--IYQRLnvARLIRELAEEGKYVLVVE 269
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-208 |
3.17e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 42.75 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 30 GETITILGRNGVGKTTTLRTIMGIIRNRKGVIklggkdlmpvplhrtakygigfvpeergifatlsveenlklppVVASG 109
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGV-------------------------------------------IYIDG 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 110 GMTLDEIYELFPNLYERRTspGTKLSGGEQQMLAMARILRTGVKVLLLDEPTEGLAPV------IVQRIGEVLQKLKSRG 183
Cdd:smart00382 39 EDILEEVLDQLLLIIVGGK--KASGSGELRLRLALALARKLKPDVLILDEITSLLDAEqealllLLEELRLLLLLKSEKN 116
|
170 180
....*....|....*....|....*
gi 1610782141 184 MTVVLVEQNFRFASRIADRFYLMDH 208
Cdd:smart00382 117 LTVILTTNDEKDLGPALLRRRFDRR 141
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
12-221 |
4.00e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 44.34 E-value: 4.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 12 SW--YGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVP-----LHRTAK----YG 80
Cdd:PLN03130 623 SWdsKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVIRGTVAYVPqvswiFNATVRdnilFG 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 81 IGFVPE--ERGIFATlSVEENLKLPPvvasgGMTLDEIYElfpnlyerrtsPGTKLSGGEQQMLAMARILRTGVKVLLLD 158
Cdd:PLN03130 703 SPFDPEryERAIDVT-ALQHDLDLLP-----GGDLTEIGE-----------RGVNISGGQKQRVSMARAVYSNSDVYIFD 765
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1610782141 159 EPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIaDRFYLMDHGQMVSNFPVSELS 221
Cdd:PLN03130 766 DPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEELS 827
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
134-201 |
4.39e-05 |
|
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: 44.23 E-value: 4.39e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1610782141 134 LSGGEQQMLAMARILRTG-VKVL-LLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVE---QNFRFASRIAD 201
Cdd:TIGR00630 489 LSGGEAQRIRLATQIGSGlTGVLyVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEhdeDTIRAADYVID 561
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-212 |
5.30e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 43.24 E-value: 5.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 1 MAAMLEVSNLKS-------WYGESQ--ALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKdlmpv 71
Cdd:PRK15112 1 VETLLEVRNLSKtfryrtgWFRRQTveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDH----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 72 PLHrtakYG-IGFVPEE-RGIFATLSVEEN--------LKLPPVVASggmtldeiyELFPNLYERRTSPGTK-------- 133
Cdd:PRK15112 76 PLH----FGdYSYRSQRiRMIFQDPSTSLNprqrisqiLDFPLRLNT---------DLEPEQREKQIIETLRqvgllpdh 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 134 -------LSGGEQQMLAMARILRTGVKVLLLDEPTEGL-APVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRIADRFYL 205
Cdd:PRK15112 143 asyyphmLAPGQKQRLGLARALILRPKVIIADEALASLdMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLV 222
|
....*..
gi 1610782141 206 MDHGQMV 212
Cdd:PRK15112 223 MHQGEVV 229
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-231 |
5.45e-05 |
|
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: 43.75 E-value: 5.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 20 LHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKD--------LMPVPLHRTAKYGIGFvpEE---R 88
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRIsfspqtswIMPGTIKDNIIFGLSY--DEyryT 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 89 GIFATLSVEENLKLPP-----VVASGGMTldeiyelfpnlyerrtspgtkLSGGEQQMLAMARILRTGVKVLLLDEPTEG 163
Cdd:TIGR01271 520 SVIKACQLEEDIALFPekdktVLGEGGIT---------------------LSGGQRARISLARAVYKDADLYLLDSPFTH 578
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1610782141 164 LAPVIVQRIGE-VLQKLKSrGMTVVLVEQNFRFASRiADRFYLMDHGQMVSNFPVSELSGRMGELNKVL 231
Cdd:TIGR01271 579 LDVVTEKEIFEsCLCKLMS-NKTRILVTSKLEHLKK-ADKILLLHEGVCYFYGTFSELQAKRPDFSSLL 645
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
123-193 |
7.42e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.08 E-value: 7.42e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1610782141 123 LYERRTspgTKLSGGEQQMLAMARILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNF 193
Cdd:PRK10938 128 LLDRRF---KYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRF 195
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
4-91 |
9.87e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 42.47 E-value: 9.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 4 MLEVSNLKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGiiRNR----KGVIKLGGKDLMpvplhrtaky 79
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAG--REDyevtGGTVEFKGKDLL---------- 68
|
90
....*....|....*
gi 1610782141 80 giGFVPEER---GIF 91
Cdd:PRK09580 69 --ELSPEDRageGIF 81
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
16-212 |
1.18e-04 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 42.70 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 16 ESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKDLMPVPL-----------------HRTAK 78
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLaslrnqvalvsqnvhlfNDTIA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 79 YGIGFVPEERgiFATLSVEENLKLppvvasgGMTLDEIYELFPNLYERRTSPGTKLSGGEQQMLAMARILRTGVKVLLLD 158
Cdd:PRK11176 435 NNIAYARTEQ--YSREQIEEAARM-------AYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILD 505
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1610782141 159 EPTEGL---APVIVQRIGEVLQKLKSrgmtvVLVeqnfrFASRI-----ADRFYLMDHGQMV 212
Cdd:PRK11176 506 EATSALdteSERAIQAALDELQKNRT-----SLV-----IAHRLstiekADEILVVEDGEIV 557
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
30-161 |
1.27e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.41 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 30 GETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLggkdlMPvplhrtaKYGIGFVPEERGIFATLSVEENLK--LPPVVA 107
Cdd:PRK11819 33 GAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP-----AP-------GIKVGYLPQEPQLDPEKTVRENVEegVAEVKA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 108 SggMT-LDEIYELFPN-------LYER---------------------------RTSPG----TKLSGGEQQMLAMARIL 148
Cdd:PRK11819 101 A--LDrFNEIYAAYAEpdadfdaLAAEqgelqeiidaadawdldsqleiamdalRCPPWdakvTKLSGGERRRVALCRLL 178
|
170
....*....|...
gi 1610782141 149 RTGVKVLLLDEPT 161
Cdd:PRK11819 179 LEKPDMLLLDEPT 191
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
20-160 |
1.94e-04 |
|
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: 41.38 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 20 LHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKD--------LMPVPLHRTAKYGIGFvpEE---R 88
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRIsfssqfswIMPGTIKENIIFGVSY--DEyryK 130
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1610782141 89 GIFATLSVEENL-KLPP----VVASGGMTldeiyelfpnlyerrtspgtkLSGGEQQMLAMARILRTGVKVLLLDEP 160
Cdd:cd03291 131 SVVKACQLEEDItKFPEkdntVLGEGGIT---------------------LSGGQRARISLARAVYKDADLYLLDSP 186
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
133-204 |
1.97e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 40.42 E-value: 1.97e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1610782141 133 KLSGGEQQMLAMARILR----TGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVEQNFRFASRiADRFY 204
Cdd:cd03227 77 QLSGGEKELSALALILAlaslKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAEL-ADKLI 151
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
127-190 |
3.17e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.55 E-value: 3.17e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1610782141 127 RTSpGTkLSGGEQQmlamaRI-----LRTG-VKVL-LLDEPTEGLAPVIVQRIGEVLQKLKSRGMTVVLVE 190
Cdd:COG0178 481 RSA-GT-LSGGEAQ-----RIrlatqIGSGlVGVLyVLDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVE 544
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-200 |
3.26e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 40.95 E-value: 3.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 19 ALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKdlmpvplhrtakygIGFVPEERGIFATLSVEE 98
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE--------------VSVIAISAGLSGQLTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 99 NLKLPPVVAsgGMTLDEIYELFPNLYERRT------SPGTKLSGGEQQMLAMARILRTGVKVLLLDEPTEGLAPVIVQRI 172
Cdd:PRK13546 105 NIEFKMLCM--GFKRKEIKAMTPKIIEFSElgefiyQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKC 182
|
170 180 190
....*....|....*....|....*....|..
gi 1610782141 173 GEVLQKLKSRGMTVVLVEQNFR----FASRIA 200
Cdd:PRK13546 183 LDKIYEFKEQNKTIFFVSHNLGqvrqFCTKIA 214
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
5-227 |
3.48e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 41.11 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 5 LEVSNLKSWYGESQ-ALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKdlmPVPLHRTAKY---- 79
Cdd:PRK10522 323 LELRNVTFAYQDNGfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK---PVTAEQPEDYrklf 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 80 ---------------GIGFVPEERGIF---ATLSVEENLKLppvvaSGGMTLDeiyelfpnlyerrtspgTKLSGGEQQM 141
Cdd:PRK10522 400 savftdfhlfdqllgPEGKPANPALVEkwlERLKMAHKLEL-----EDGRISN-----------------LKLSKGQKKR 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 142 LAMARILRTGVKVLLLDEPTEGLAPVIvQRI--GEVLQKLKSRGMTVVLVEQNFRFASRiADRFYLMDHGQMvsnfpvSE 219
Cdd:PRK10522 458 LALLLALAEERDILLLDEWAADQDPHF-RREfyQVLLPLLQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQL------SE 529
|
....*...
gi 1610782141 220 LSGRMGEL 227
Cdd:PRK10522 530 LTGEERDA 537
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
10-182 |
3.78e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 41.23 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 10 LKSWYGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRkGVIKLGGKdlmpvPLHRTAKYGIgfVPEERG 89
Cdd:PRK15134 292 LKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQ-----PLHNLNRRQL--LPVRHR 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 90 I-------FATLS--------VEENLKLPPVVASGGMTLDEIYE------LFPnlyERRTSPGTKLSGGEQQMLAMARIL 148
Cdd:PRK15134 364 IqvvfqdpNSSLNprlnvlqiIEEGLRVHQPTLSAAQREQQVIAvmeevgLDP---ETRHRYPAEFSGGQRQRIAIARAL 440
|
170 180 190
....*....|....*....|....*....|....
gi 1610782141 149 RTGVKVLLLDEPTEGLAPVIVQRIGEVLQKLKSR 182
Cdd:PRK15134 441 ILKPSLIILDEPTSSLDKTVQAQILALLKSLQQK 474
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
19-125 |
8.23e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 39.87 E-value: 8.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 19 ALHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIKLGGKdlmpvplhrTAKYGIGfvpeeRGIFATLSVEE 98
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS---------AALIAIS-----SGLNGQLTGIE 104
|
90 100
....*....|....*....|....*..
gi 1610782141 99 NLKLPPVVAsgGMTLDEIYELFPNLYE 125
Cdd:PRK13545 105 NIELKGLMM--GLTKEKIKEIIPEIIE 129
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
120-199 |
9.64e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.01 E-value: 9.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 120 FPNLYERRT-SPGTKLSGGEQQMLAMARILRTGVKVLLLDEPTEGL---APVIVQRIGEVLQKLKSRgMTVVLVEQ--NF 193
Cdd:PTZ00265 565 LPDKYETLVgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLdnkSEYLVQKTINNLKGNENR-ITIIIAHRlsTI 643
|
....*.
gi 1610782141 194 RFASRI 199
Cdd:PTZ00265 644 RYANTI 649
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
22-164 |
1.21e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.46 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 22 GVDLTvgegETITILGRNGVGKTTTLRTIMGIIRNRKGVI--------------KLGGKDLMPVPLHRTAKYGIGfVPEE 87
Cdd:PLN03073 531 GIDLD----SRIAMVGPNGIGKSTILKLISGELQPSSGTVfrsakvrmavfsqhHVDGLDLSSNPLLYMMRCFPG-VPEQ 605
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1610782141 88 --RGIFATLSVEENLKLPPVVAsggmtldeiyelfpnlyerrtspgtkLSGGEQQMLAMARILRTGVKVLLLDEPTEGL 164
Cdd:PLN03073 606 klRAHLGSFGVTGNLALQPMYT--------------------------LSGGQKSRVAFAKITFKKPHILLLDEPSNHL 658
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
20-212 |
1.22e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 39.76 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 20 LHGVDLTVGEGETITILGRNGVGKTTTLRTIMGIIRNRKGVIkLGGKDLMPVP-----LHRTAKYGIGFVPEERGifATL 94
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-WAERSIAYVPqqawiMNATVRGNILFFDEEDA--ARL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 95 S-------VEENLKLppvvASGGMTlDEIYElfpnlyerrtsPGTKLSGGEQQMLAMARILRTGVKVLLLDEPTEGLAPV 167
Cdd:PTZ00243 753 AdavrvsqLEADLAQ----LGGGLE-TEIGE-----------KGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAH 816
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1610782141 168 IVQRIGEVLQKLKSRGMTVVLVEQNFRFASRiADRFYLMDHGQMV 212
Cdd:PTZ00243 817 VGERVVEECFLGALAGKTRVLATHQVHVVPR-ADYVVALGDGRVE 860
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
134-178 |
1.50e-03 |
|
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: 39.35 E-value: 1.50e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1610782141 134 LSGGEQQMLAMARILRTGVKVLLLDEPTEGLAPVIVQRIGEVLQK 178
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE 627
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
14-176 |
2.30e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 38.46 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 14 YGESQALHGVDLTVGEGETITILGRNGVGKTTTLRTIMG-----------IIRNRKGviklGGKDLMPVPLHrtakygIG 82
Cdd:PRK10938 270 YNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndltLFGRRRG----SGETIWDIKKH------IG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610782141 83 FVPEErgifATLSVEENLKLPPVVASGGMTLDEIYELFPNLYERRT---------------SPGTKLSGGEQQMLAMARI 147
Cdd:PRK10938 340 YVSSS----LHLDYRVSTSVRNVILSGFFDSIGIYQAVSDRQQKLAqqwldilgidkrtadAPFHSLSWGQQRLALIVRA 415
|
170 180 190
....*....|....*....|....*....|....*
gi 1610782141 148 LrtgVK---VLLLDEPTEGLAPV---IVQRIGEVL 176
Cdd:PRK10938 416 L---VKhptLLILDEPLQGLDPLnrqLVRRFVDVL 447
|
|
| |
