|
Name |
Accession |
Description |
Interval |
E-value |
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
20-258 |
1.16e-177 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 488.00 E-value: 1.16e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 20 GTLIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRLGVG 99
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 100 YLPQEASIFRGLTVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLD 179
Cdd:COG1137 82 YLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521065470 180 EPFAGVDPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNPEVRRLYLGDNFSL 258
Cdd:COG1137 162 EPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPLVRKVYLGEDFRL 240
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
22-253 |
5.47e-154 |
|
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: 427.73 E-value: 5.47e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRLGVGYL 101
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 102 PQEASIFRGLTVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEP 181
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521065470 182 FAGVDPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNPEVRRLYLG 253
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKVYLG 232
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
21-258 |
4.23e-147 |
|
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: 410.51 E-value: 4.23e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 21 TLIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRLGVGY 100
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLGIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 101 LPQEASIFRGLTVEENIRAVLEVHVK-DKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLD 179
Cdd:TIGR04406 81 LPQEASIFRKLTVEENIMAVLEIRKDlDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521065470 180 EPFAGVDPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNPEVRRLYLGDNFSL 258
Cdd:TIGR04406 161 EPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVRRVYLGEQFRL 239
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
21-258 |
5.85e-104 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 301.43 E-value: 5.85e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 21 TLIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRLGVGY 100
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 101 LPQEASIFRGLTVEENIRAVLEVHVKDKAE-REQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLD 179
Cdd:PRK10895 83 LPQEASIFRRLSVYDNLMAVLQIRDDLSAEqREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521065470 180 EPFAGVDPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNPEVRRLYLGDNFSL 258
Cdd:PRK10895 163 EPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYLGEDFRL 241
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
22-254 |
3.30e-75 |
|
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: 229.15 E-value: 3.30e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRLGVGYL 101
Cdd:COG0411 5 LEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLGIART 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 102 PQEASIFRGLTVEENIRAVLEVH---------------VKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIA 166
Cdd:COG0411 85 FQNPRLFPELTVLENVLVAAHARlgrgllaallrlpraRREEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 167 RALATDPTFMLLDEPFAGVDPISVADIQNLVHHLTA-RGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNP 245
Cdd:COG0411 165 RALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDeRGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVRADP 244
|
....*....
gi 521065470 246 EVRRLYLGD 254
Cdd:COG0411 245 RVIEAYLGE 253
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
22-256 |
7.82e-74 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 224.94 E-value: 7.82e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRlgVGYL 101
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRR--IGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 102 PQEASIFRGLTVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEP 181
Cdd:COG1131 79 PQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521065470 182 FAGVDPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANdivnnpEVRRLYLGDNF 256
Cdd:COG1131 159 TSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPD------ELKARLLEDVF 227
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
22-247 |
2.17e-73 |
|
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: 223.85 E-value: 2.17e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRLGVGYL 101
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 102 PQEASIFRGLTVEENIRAVLEVH----------VKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALAT 171
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAQARtgsglllaraRREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521065470 172 DPTFMLLDEPFAGVDPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNPEV 247
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPRV 236
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
22-253 |
2.74e-71 |
|
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: 218.31 E-value: 2.74e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRLGVGYL 101
Cdd:COG0410 4 LEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 102 PQEASIFRGLTVEENIRAVLEVHvKDKAEREQKLNELLEEFHI-QKLRKSAAVALSGGERRRLEIARALATDPTFMLLDE 180
Cdd:COG0410 84 PEGRRIFPSLTVEENLLLGAYAR-RDRAEVRADLERVYELFPRlKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521065470 181 PFAGVDPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNPEVRRLYLG 253
Cdd:COG0410 163 PSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEVREAYLG 235
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
22-244 |
2.71e-65 |
|
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: 202.66 E-value: 2.71e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRLGVGYL 101
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 102 PQEASIFRGLTVEENIRAVLevHVKDKAEREQKLNELLEEFHI-QKLRKSAAVALSGGERRRLEIARALATDPTFMLLDE 180
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGA--YARRRAKRKARLERVYELFPRlKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521065470 181 PFAGVDPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNN 244
Cdd:cd03224 159 PSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
22-241 |
7.87e-65 |
|
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: 202.01 E-value: 7.87e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRLGvgYL 101
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIG--VL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 102 PQEASIFRGLTVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEP 181
Cdd:COG4555 80 PDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 182 FAGVDPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDI 241
Cdd:COG4555 160 TNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
22-232 |
1.60e-60 |
|
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: 188.76 E-value: 1.60e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRlgVGYL 101
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRR--IGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 102 PQEASIFRGLTVEENIRavlevhvkdkaereqklnelleefhiqklrksaavaLSGGERRRLEIARALATDPTFMLLDEP 181
Cdd:cd03230 79 PEEPSLYENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPELLILDEP 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 521065470 182 FAGVDPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEV 232
Cdd:cd03230 123 TSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
25-249 |
1.30e-56 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 180.95 E-value: 1.30e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 25 RGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRL--GVGYLP 102
Cdd:COG1127 9 RNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELrrRIGMLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 103 QEASIFRGLTVEENIRAVLEVHVK-DKAEREQKLNELLEEF---HIQKLRKSaavALSGGERRRLEIARALATDPTFMLL 178
Cdd:COG1127 89 QGGALFDSLTVFENVAFPLREHTDlSEAEIRELVLEKLELVglpGAADKMPS---ELSGGMRKRVALARALALDPEILLY 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521065470 179 DEPFAGVDPISVADIQNLVHHLT-ARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVN--NPEVRR 249
Cdd:COG1127 166 DEPTAGLDPITSAVIDELIRELRdELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLAsdDPWVRQ 239
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
22-246 |
1.56e-55 |
|
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: 177.91 E-value: 1.56e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYA-TRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRLgVGY 100
Cdd:COG1122 1 IELENLSFSYPgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRK-VGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 101 LPQ--EASIFrGLTVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLL 178
Cdd:COG1122 80 VFQnpDDQLF-APTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521065470 179 DEPFAGVDPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNPE 246
Cdd:COG1122 159 DEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
22-236 |
1.86e-55 |
|
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: 177.33 E-value: 1.86e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRsrlGVGYL 101
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERR---NIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 102 PQEASIFRGLTVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEP 181
Cdd:cd03259 78 FQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 521065470 182 FAGVDPISVADIQNLVHHL-TARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHG 236
Cdd:cd03259 158 LSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
22-251 |
2.84e-53 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 172.58 E-value: 2.84e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVttmpmyRRSRLGVGYL 101
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP------RRARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 102 PQEASIFRG--LTVEENIRAVLEVHVK-----DKAEREqKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPT 174
Cdd:COG1121 81 PQRAEVDWDfpITVRDVVLMGRYGRRGlfrrpSRADRE-AVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521065470 175 FMLLDEPFAGVDPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIhAGEVLTHGRANDIVNNPEVRRLY 251
Cdd:COG1121 160 LLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLTPENLSRAY 235
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
22-236 |
4.41e-53 |
|
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: 171.15 E-value: 4.41e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYATRR--VVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRlgVG 99
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQS--LG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 100 YLPQEASIFRGLTVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLD 179
Cdd:cd03263 79 YCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 521065470 180 EPFAGVDPISVADIQNLVHHLTaRGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHG 236
Cdd:cd03263 159 EPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
25-245 |
1.91e-52 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 173.75 E-value: 1.91e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 25 RGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRsrlGVGYLPQE 104
Cdd:COG3842 9 ENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKR---NVGMVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 105 ASIFRGLTVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAG 184
Cdd:COG3842 86 YALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521065470 185 VDPISVADIQN-LVHHLTARGIG-VLVTdHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNP 245
Cdd:COG3842 166 LDAKLREEMREeLRRLQRELGITfIYVT-HDQEEALALADRIAVMNDGRIEQVGTPEEIYERP 227
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
22-250 |
2.19e-52 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 170.66 E-value: 2.19e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYATRR----VVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTtmpmyrRSRLG 97
Cdd:COG1116 8 LELRGVSKRFPTGGggvtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT------GPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 98 VGYLPQEASIFRGLTVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFML 177
Cdd:COG1116 82 RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 178 LDEPFAGVDPISVADIQNLVHHL-TARGIGVL-VTdHNVRETLGLIDRAYIIHA--GEV-------LTHGRANDIVNNPE 246
Cdd:COG1116 162 MDEPFGALDALTRERLQDELLRLwQETGKTVLfVT-HDVDEAVFLADRVVVLSArpGRIveeidvdLPRPRDRELRTSPE 240
|
....
gi 521065470 247 VRRL 250
Cdd:COG1116 241 FAAL 244
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
25-248 |
5.68e-51 |
|
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: 166.52 E-value: 5.68e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 25 RGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTM--PMYRRSRLGVGYLP 102
Cdd:cd03261 4 RGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLseAELYRLRRRMGMLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 103 QEASIFRGLTVEENIRAVLEVHVK-DKAEREQKLNELLEEF---HIQKLRKSaavALSGGERRRLEIARALATDPTFMLL 178
Cdd:cd03261 84 QSGALFDSLTVFENVAFPLREHTRlSEEEIREIVLEKLEAVglrGAEDLYPA---ELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521065470 179 DEPFAGVDPISVADIQNLVHHLTAR-GIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVN--NPEVR 248
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRAsdDPLVR 233
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-241 |
2.22e-50 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 166.82 E-value: 2.22e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 21 TLIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTtmpmyRRSRLGVGY 100
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD-----PEDRRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 101 LPQEasifRGL----TVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFM 176
Cdd:COG4152 76 LPEE----RGLypkmKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521065470 177 LLDEPFAGVDPISVADIQNLVHHLTARGIGVLVTDHN---VREtlgLIDRAYIIHAGEVLTHGRANDI 241
Cdd:COG4152 152 ILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQmelVEE---LCDRIVIINKGRKVLSGSVDEI 216
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
22-251 |
3.69e-50 |
|
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: 164.83 E-value: 3.69e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRLgVGYL 101
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARR-IAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 102 PQEASIFRGLTVEENI----RAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFML 177
Cdd:COG1120 81 PQEPPAPFGLTVRELValgrYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521065470 178 LDEPFAGVDPISVADIQNLVHHLTA-RGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNPEVRRLY 251
Cdd:COG1120 161 LDEPTSHLDLAHQLEVLELLRRLAReRGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVY 235
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
25-231 |
3.80e-50 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 163.41 E-value: 3.80e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 25 RGLTKTY--ATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRLgVGYLP 102
Cdd:cd03225 3 KNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRK-VGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 103 Q--EASIFrGLTVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDE 180
Cdd:cd03225 82 QnpDDQFF-GPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 521065470 181 PFAGVDPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGE 231
Cdd:cd03225 161 PTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
22-245 |
5.23e-50 |
|
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: 171.24 E-value: 5.23e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYATR-----RVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRL 96
Cdd:COG1123 261 LEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 97 G--VGYLPQ--EASIFRGLTVEENIRAVLEVH-VKDKAEREQKLNELLEEFHiqkLRKSAA----VALSGGERRRLEIAR 167
Cdd:COG1123 341 RrrVQMVFQdpYSSLNPRMTVGDIIAEPLRLHgLLSRAERRERVAELLERVG---LPPDLAdrypHELSGGQRQRVAIAR 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521065470 168 ALATDPTFMLLDEPFAGVDPISVADIQNLVHHLTAR-GIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNP 245
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANP 496
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
22-229 |
1.21e-49 |
|
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: 162.64 E-value: 1.21e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYATRR----VVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTtmpmyrRSRLG 97
Cdd:cd03293 1 LEVRNVSKTYGGGGgavtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT------GPGPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 98 VGYLPQEASIFRGLTVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFML 177
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 521065470 178 LDEPFAGVDPISVADIQNLV------HHLTArgigVLVTdHNVRETLGLIDRAYIIHA 229
Cdd:cd03293 155 LDEPFSALDALTREQLQEELldiwreTGKTV----LLVT-HDIDEAVFLADRVVVLSA 207
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
22-250 |
1.63e-49 |
|
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: 162.69 E-value: 1.63e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRLGVGYL 101
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 102 PQEASIFRGLTVEENIRAVLEVHvkdkAEREQKL-NELLEEFHI-QKLRKSAAVALSGGERRRLEIARALATDPTFMLLD 179
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTGLAAL----PRRSRKIpDEIYELFPVlKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521065470 180 EPFAGVDPISVADIQNLVHHLTAR-GIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDiVNNPEVRRL 250
Cdd:TIGR03410 157 EPTEGIQPSIIKDIGRVIRRLRAEgGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDE-LDEDKVRRY 227
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
21-246 |
2.47e-48 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 163.01 E-value: 2.47e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 21 TLIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTT-MPMYRRsrlGVG 99
Cdd:COG1118 2 SIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTnLPPRER---RVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 100 YLPQEASIFRGLTVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLD 179
Cdd:COG1118 79 FVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 180 EPFAGVDpISVADI--QNLVHHLTARGI-GVLVTdHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNPE 246
Cdd:COG1118 159 EPFGALD-AKVRKElrRWLRRLHDELGGtTVFVT-HDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPA 226
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
24-232 |
1.24e-47 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 156.90 E-value: 1.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 24 ARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPM--YRRSrlgVGYL 101
Cdd:COG4619 3 LEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPpeWRRQ---VAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 102 PQEASIFRGlTVEENIRAVLevHVKDKAEREQKLNELLEEFHIQK--LRKSAAvALSGGERRRLEIARALATDPTFMLLD 179
Cdd:COG4619 80 PQEPALWGG-TVRDNLPFPF--QLRERKFDRERALELLERLGLPPdiLDKPVE-RLSGGERQRLALIRALLLQPDVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 521065470 180 EPFAGVDPISVADIQNLVHHLTAR-GIGVLVTDHNVRETLGLIDRAYIIHAGEV 232
Cdd:COG4619 156 EPTSALDPENTRRVEELLREYLAEeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
25-236 |
2.17e-47 |
|
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: 156.22 E-value: 2.17e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 25 RGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVT-TMPMYRRsrlgVGYLPQ 103
Cdd:cd03268 4 NDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQkNIEALRR----IGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 104 EASIFRGLTVEENiravLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFA 183
Cdd:cd03268 80 APGFYPNLTAREN----LRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 521065470 184 GVDPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHG 236
Cdd:cd03268 156 GLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
22-241 |
1.92e-46 |
|
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of this protein family are the ATP-binding subunit of an ABC transporter system that is associated with PQQ biosynthesis and PQQ-dependent alcohol dehydrogenases. While this family shows homology to several efflux ABC transporter subunits, the presence of a periplasmic substrate-binding protein and association with systems for catabolism of alcohols suggests a role in import rather than detoxification. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 274822 [Multi-domain] Cd Length: 236 Bit Score: 154.76 E-value: 1.92e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRLGVGYl 101
Cdd:TIGR03864 2 LEVAGLSFRYGARRALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQISVAGHDLRRAPRAALARLGVVF- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 102 pQEASIFRGLTVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEP 181
Cdd:TIGR03864 81 -QQPTLDLDLSVRQNLRYHAALHGLSRAEARARIAELLARLGLAERADDKVRELNGGHRRRVEIARALLHRPALLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521065470 182 FAGVDPISVADIQNLVHHLTA-RGIGVLVTDHNVREtLGLIDRAYIIHAGEVLTHGRANDI 241
Cdd:TIGR03864 160 TVGLDPASRAAITAHVRALARdQGLSVLWATHLVDE-IEASDRLVVLHRGRVLADGAAAEL 219
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
26-236 |
2.35e-46 |
|
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: 153.84 E-value: 2.35e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 26 GLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVttmpmyRRSRLGVGYLPQEA 105
Cdd:cd03235 4 DLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL------EKERKRIGYVPQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 106 SIFRG--LTVEENIRAVLEVHV----KDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLD 179
Cdd:cd03235 78 SIDRDfpISVRDVVLMGLYGHKglfrRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 521065470 180 EPFAGVDPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIhAGEVLTHG 236
Cdd:cd03235 158 EPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
37-183 |
2.66e-46 |
|
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: 151.65 E-value: 2.66e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 37 VNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMyRRSRLGVGYLPQEASIFRGLTVEEN 116
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDER-KSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521065470 117 IRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVA----LSGGERRRLEIARALATDPTFMLLDEPFA 183
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
29-241 |
4.75e-46 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 156.01 E-value: 4.75e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 29 KTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRLGVgyLPQEASIF 108
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGI--VPQYASVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 109 RGLTVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAGVDPI 188
Cdd:TIGR01188 79 EDLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 521065470 189 SVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDI 241
Cdd:TIGR01188 159 TRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
22-241 |
1.53e-45 |
|
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: 152.14 E-value: 1.53e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPmyRRSRLGVGYL 101
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP--REVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 102 PQEASIFRGLTVEENiravLEVHVK----DKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFML 177
Cdd:cd03265 79 FQDLSVDDELTGWEN----LYIHARlygvPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521065470 178 LDEPFAGVDPISVADIQNLVHHLTAR-GIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDI 241
Cdd:cd03265 155 LDEPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
25-245 |
2.60e-45 |
|
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: 152.07 E-value: 2.60e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 25 RGLTKTYATRR-VVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPM--YRRSrlgVGYL 101
Cdd:cd03295 4 ENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPveLRRK---IGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 102 PQEASIFRGLTVEENIRAVLEVHVKDKAEREQKLNELLEEFHI--QKLRKSAAVALSGGERRRLEIARALATDPTFMLLD 179
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521065470 180 EPFAGVDPISVADIQNLVHHLTaRGIG---VLVTdHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNP 245
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQ-QELGktiVFVT-HDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSP 227
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
22-212 |
4.81e-45 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 150.32 E-value: 4.81e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRLgvGYL 101
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRL--AYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 102 PQEASIFRGLTVEENIRAVLEVHvKDKAEREQkLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEP 181
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALY-GLRADREA-IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190
....*....|....*....|....*....|.
gi 521065470 182 FAGVDPISVADIQNLVHHLTARGIGVLVTDH 212
Cdd:COG4133 159 FTALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
24-236 |
8.59e-45 |
|
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: 150.35 E-value: 8.59e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 24 ARGLTKTYATR----RVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRLG-- 97
Cdd:cd03257 4 VKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRRke 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 98 VGYLPQEA--SIFRGLTVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQ---KLRKSAAVALSGGERRRLEIARALATD 172
Cdd:cd03257 84 IQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGlpeEVLNRYPHELSGGQRQRVAIARALALN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521065470 173 PTFMLLDEPFAGVDPISVADIQNLVHHL-TARGIGVLVTDHNvretLGLI----DRAYIIHAGEVLTHG 236
Cdd:cd03257 164 PKLLIADEPTSALDVSVQAQILDLLKKLqEELGLTLLFITHD----LGVVakiaDRVAVMYAGKIVEEG 228
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
24-231 |
1.40e-44 |
|
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: 147.39 E-value: 1.40e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 24 ARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPmYRRSRLGVGYLPQ 103
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLP-LEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 104 easifrgltveeniravlevhvkdkaereqklnelleefhiqklrksaavaLSGGERRRLEIARALATDPTFMLLDEPFA 183
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 521065470 184 GVDPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGE 231
Cdd:cd00267 110 GLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
25-253 |
1.43e-44 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 150.27 E-value: 1.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 25 RGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRLGVGYLPQE 104
Cdd:COG4674 14 EDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIARLGIGRKFQK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 105 ASIFRGLTVEENI-------RAVLEV--HVKDKAEREqKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTF 175
Cdd:COG4674 94 PTVFEELTVFENLelalkgdRGVFASlfARLTAEERD-RIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 176 MLLDEPFAGvdpISVADIQNLVHHLT--ARGIGVLVTDHN---VREtlgLIDRAYIIHAGEVLTHGRANDIVNNPEVRRL 250
Cdd:COG4674 173 LLLDEPVAG---MTDAETERTAELLKslAGKHSVVVVEHDmefVRQ---IARKVTVLHQGSVLAEGSLDEVQADPRVIEV 246
|
...
gi 521065470 251 YLG 253
Cdd:COG4674 247 YLG 249
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
22-232 |
1.76e-44 |
|
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: 149.18 E-value: 1.76e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTY----ATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRL- 96
Cdd:cd03255 1 IELKNLSKTYggggEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 97 --GVGYLPQEASIFRGLTVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPT 174
Cdd:cd03255 81 rrHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 521065470 175 FMLLDEPFAGVDPISVADIQNLVHHLTA-RGIGVLVTDHNvRETLGLIDRAYIIHAGEV 232
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKeAGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
22-231 |
6.96e-44 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 146.18 E-value: 6.96e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRR-SRLGVGY 100
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPpLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 101 LPQEASIFRGLTVEENIravlevhvkdkaereqklnelleefhiqklrksaAVALSGGERRRLEIARALATDPTFMLLDE 180
Cdd:cd03229 81 VFQDFALFPHLTVLENI----------------------------------ALGLSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 521065470 181 PFAGVDPISVADIQNLVHHLTAR-GIGVLVTDHNVRETLGLIDRAYIIHAGE 231
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
22-254 |
9.13e-44 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 148.60 E-value: 9.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRLGVGYL 101
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 102 PQEASIFRGLTVEENIRAVLEVHVKD-------------KAERE--QKLNELLEEFHIQKLRKSAAVALSGGERRRLEIA 166
Cdd:PRK11300 86 FQHVRLFREMTVIENLLVAQHQQLKTglfsgllktpafrRAESEalDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 167 RALATDPTFMLLDEPFAGVDPISVADIQNLVHHLTAR-GIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNP 245
Cdd:PRK11300 166 RCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
|
....*....
gi 521065470 246 EVRRLYLGD 254
Cdd:PRK11300 246 DVIKAYLGE 254
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
26-236 |
9.20e-44 |
|
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: 147.04 E-value: 9.20e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 26 GLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRrsrlgVGYLPQEA 105
Cdd:cd03269 5 NVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNR-----IGYLPEER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 106 SIFRGLTVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAGV 185
Cdd:cd03269 80 GLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 521065470 186 DPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHG 236
Cdd:cd03269 160 DPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
22-232 |
1.09e-43 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 147.50 E-value: 1.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTY----ATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMP-----MYR 92
Cdd:COG1136 5 LELRNLTKSYgtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSerelaRLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 93 RSRlgVGYLPQEASIFRGLTVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATD 172
Cdd:COG1136 85 RRH--IGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521065470 173 PTFMLLDEPFAGVDPISVADIQNLVHHLTAR-GIGVLVTDHNvRETLGLIDRAYIIHAGEV 232
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHD-PELAARADRVIRLRDGRI 222
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
25-245 |
1.97e-43 |
|
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: 147.10 E-value: 1.97e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 25 RGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRsrlGVGYLPQE 104
Cdd:cd03296 6 RNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER---NVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 105 ASIFRGLTVEENIRAVLEVHVK----DKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDE 180
Cdd:cd03296 83 YALFRHMTVFDNVAFGLRVKPRserpPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521065470 181 PFAGVDPIS-------VADIQNLVHHLTargigVLVTdHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNP 245
Cdd:cd03296 163 PFGALDAKVrkelrrwLRRLHDELHVTT-----VFVT-HDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHP 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
22-246 |
2.41e-43 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 153.52 E-value: 2.41e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYA--TRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVD---EGTIEIDGNDVTTMPMYRRSRL 96
Cdd:COG1123 5 LEVRDLSVRYPggDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 97 gVGYLPQEA-SIFRGLTVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTF 175
Cdd:COG1123 85 -IGMVFQDPmTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521065470 176 MLLDEPFAGVDPISVADIQNLVHHLTA-RGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNPE 246
Cdd:COG1123 164 LIADEPTTALDVTTQAEILDLLRELQReRGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
22-236 |
3.87e-43 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 145.41 E-value: 3.87e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYATRRVVNGVSLVVRRGeAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRLgvGYL 101
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRI--GYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 102 PQEASIFRGLTVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEP 181
Cdd:cd03264 78 PQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 521065470 182 FAGVDPISVADIQNLVHHLTARGIgVLVTDHNVRETLGLIDRAYIIHAGEVLTHG 236
Cdd:cd03264 158 TAGLDPEERIRFRNLLSELGEDRI-VILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
22-236 |
4.18e-43 |
|
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: 145.59 E-value: 4.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTY----ATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRLG 97
Cdd:cd03266 2 ITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 98 VgyLPQEASIFRGLTVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFML 177
Cdd:cd03266 82 F--VSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 521065470 178 LDEPFAGVDPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHG 236
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
22-246 |
8.38e-43 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 145.72 E-value: 8.38e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYAT----RRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRlG 97
Cdd:COG1124 2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRR-R 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 98 VGYLPQ--EASIFRGLTVEENIRAVLEVHVKDkaEREQKLNELLEEFHIQK-LRKSAAVALSGGERRRLEIARALATDPT 174
Cdd:COG1124 81 VQMVFQdpYASLHPRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLPPsFLDRYPHQLSGGQRQRVAIARALILEPE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521065470 175 FMLLDEPFAGVDPISVADIQNLVHHLTA-RGIGVLVTDHNvretLGLI----DRAYIIHAGEVLTHGRANDIVNNPE 246
Cdd:COG1124 159 LLLLDEPTSALDVSVQAEILNLLKDLREeRGLTYLFVSHD----LAVVahlcDRVAVMQNGRIVEELTVADLLAGPK 231
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
25-237 |
6.45e-42 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 142.88 E-value: 6.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 25 RGLTKTYAT-RRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTM-----PMYRRSrlgV 98
Cdd:COG2884 5 ENVSKRYPGgREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrreiPYLRRR---I 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 99 GYLPQEASIFRGLTVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLL 178
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521065470 179 DEPFAGVDPISVADIQNLVHHLTARGIGVLVTDHNvretLGLIDR--AYIIHagevLTHGR 237
Cdd:COG2884 162 DEPTGNLDPETSWEIMELLEEINRRGTTVLIATHD----LELVDRmpKRVLE----LEDGR 214
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
20-245 |
2.32e-41 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 144.83 E-value: 2.32e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 20 GTLIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRsrlGVG 99
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDR---NIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 100 YLPQEASIFRGLTVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKL--RKSAavALSGGERRRLEIARALATDPTFML 177
Cdd:COG3839 79 MVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLldRKPK--QLSGGQRQRVALGRALVREPKVFL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521065470 178 LDEPFAGVDPIS----VADIQNLVHHL--TArgigVLVTdHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNP 245
Cdd:COG3839 157 LDEPLSNLDAKLrvemRAEIKRLHRRLgtTT----IYVT-HDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRP 225
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
24-241 |
3.60e-41 |
|
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: 140.78 E-value: 3.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 24 ARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPV-----DEGTIEIDGNDVTTMPMYRRS-RLG 97
Cdd:cd03260 3 LRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVLElRRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 98 VGYLPQEASIFRGlTVEENIRAVLEVH-VKDKAEREQKLNELLEEFHIQK--LRKSAAVALSGGERRRLEIARALATDPT 174
Cdd:cd03260 83 VGMVFQKPNPFPG-SIYDNVAYGLRLHgIKLKEELDERVEEALRKAALWDevKDRLHALGLSGGQQQRLCLARALANEPE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521065470 175 FMLLDEPFAGVDPISVADIQNLVHHLtARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDI 241
Cdd:cd03260 162 VLLLDEPTSALDPISTAKIEELIAEL-KKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
22-251 |
1.82e-40 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 139.81 E-value: 1.82e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYAT-RRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMP--MYRRSRLGV 98
Cdd:COG3638 3 LELRNLSKRYPGgTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgrALRRLRRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 99 GYLPQEASIFRGLTVEENI-----------RAVLevHVKDKAEREQKLnELLEEFHIQKLRKSAAVALSGGERRRLEIAR 167
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNVlagrlgrtstwRSLL--GLFPPEDRERAL-EALERVGLADKAYQRADQLSGGQQQRVAIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 168 ALATDPTFMLLDEPFAGVDPISVADIQNLVHHL-TARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDiVNNPE 246
Cdd:COG3638 160 ALVQEPKLILADEPVASLDPKTARQVMDLLRRIaREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAE-LTDAV 238
|
....*
gi 521065470 247 VRRLY 251
Cdd:COG3638 239 LREIY 243
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
36-245 |
3.58e-40 |
|
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: 138.62 E-value: 3.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 36 VVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRsrlGVGYLPQEASIFRGLTVEE 115
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKR---DISYVPQNYALFPHMTVYK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 116 NIRAVLEVHVKDKAEREQKLNELLEEFHIQKL--RKSAAvaLSGGERRRLEIARALATDPTFMLLDEPFAGVDPISVADI 193
Cdd:cd03299 91 NIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLlnRKPET--LSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 521065470 194 QNL---VHHLTarGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNP 245
Cdd:cd03299 169 REElkkIRKEF--GVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKP 221
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
25-248 |
6.38e-40 |
|
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: 137.75 E-value: 6.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 25 RGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRsrlGVGYLPQE 104
Cdd:cd03300 4 ENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKR---PVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 105 ASIFRGLTVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAG 184
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521065470 185 VDPISVADIQ----NLVHHLtarGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNPEVR 248
Cdd:cd03300 161 LDLKLRKDMQlelkRLQKEL---GITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANR 225
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
24-236 |
7.78e-40 |
|
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: 136.03 E-value: 7.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 24 ARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRLgVGYLPQ 103
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARK-IAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 104 easifrgltveeniraVLE-VHVKDKAEREqkLNElleefhiqklrksaavaLSGGERRRLEIARALATDPTFMLLDEPF 182
Cdd:cd03214 81 ----------------ALElLGLAHLADRP--FNE-----------------LSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 521065470 183 AGVDPISVADIQNLVHHLTA-RGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHG 236
Cdd:cd03214 126 SHLDIAHQIELLELLRRLAReRGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
22-231 |
1.96e-39 |
|
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: 134.82 E-value: 1.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTY--ATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPM-YRRSRlgV 98
Cdd:cd03228 1 IEFKNVSFSYpgRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLeSLRKN--I 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 99 GYLPQEASIFRGlTVEENIravlevhvkdkaereqklnelleefhiqklrksaavaLSGGERRRLEIARALATDPTFMLL 178
Cdd:cd03228 79 AYVPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 521065470 179 DEPFAGVDPISVADIQNLVHHLTARGIGVLVTdHNVrETLGLIDRAYIIHAGE 231
Cdd:cd03228 121 DEATSALDPETEALILEALRALAKGKTVIVIA-HRL-STIRDADRIIVLDDGR 171
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
25-246 |
2.06e-39 |
|
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: 136.56 E-value: 2.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 25 RGLTKTYATRR----VVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMP--MYRRSRLGV 98
Cdd:cd03258 5 KNVSKVFGDTGgkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkELRKARRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 99 GYLPQEASIFRGLTVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLL 178
Cdd:cd03258 85 GMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLC 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521065470 179 DEPFAGVDPISVADIQNLVHHLTAR-GIGVLVTDHN---VREtlgLIDRAYIIHAGEVLTHGRANDIVNNPE 246
Cdd:cd03258 165 DEATSALDPETTQSILALLRDINRElGLTIVLITHEmevVKR---ICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
25-251 |
9.74e-38 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 132.31 E-value: 9.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 25 RGLTKTYAT-RRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMY--RRSRLGVGYL 101
Cdd:cd03256 4 ENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKalRQLRRQIGMI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 102 PQEASIFRGLTVEENI-----------RAVLEVHvkDKAEREQKLnELLEEFHIQKLRKSAAVALSGGERRRLEIARALA 170
Cdd:cd03256 84 FQQFNLIERLSVLENVlsgrlgrrstwRSLFGLF--PKEEKQRAL-AALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 171 TDPTFMLLDEPFAGVDPISVADIQNLVHHL-TARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIvNNPEVRR 249
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL-TDEVLDE 239
|
..
gi 521065470 250 LY 251
Cdd:cd03256 240 IY 241
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
26-254 |
1.12e-37 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 134.96 E-value: 1.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 26 GLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPmyRRSRLGVGYLPQEA 105
Cdd:PRK13536 46 GVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARA--RLARARIGVVPQFD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 106 SIFRGLTVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAGV 185
Cdd:PRK13536 124 NLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGL 203
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521065470 186 DPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNP---EVRRLYLGD 254
Cdd:PRK13536 204 DPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHigcQVIEIYGGD 275
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
19-251 |
1.41e-37 |
|
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: 138.75 E-value: 1.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 19 QGTLIARGLTKTY--ATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRL 96
Cdd:COG4987 331 GPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 97 gVGYLPQEASIFRGlTVEENIR------------AVLE-VHVKDKAER-EQKLNELLEEfhiqklrksAAVALSGGERRR 162
Cdd:COG4987 411 -IAVVPQRPHLFDT-TLRENLRlarpdatdeelwAALErVGLGDWLAAlPDGLDTWLGE---------GGRRLSGGERRR 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 163 LEIARALATDPTFMLLDEPFAGVDPISVADI-QNLVHHLTARGIgVLVTDHnvRETLGLIDRAYIIHAGEVLTHGRANDI 241
Cdd:COG4987 480 LALARALLRDAPILLLDEPTEGLDAATEQALlADLLEALAGRTV-LLITHR--LAGLERMDRILVLEDGRIVEQGTHEEL 556
|
250
....*....|.
gi 521065470 242 V-NNPEVRRLY 251
Cdd:COG4987 557 LaQNGRYRQLY 567
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
41-253 |
7.49e-37 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 129.87 E-value: 7.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 41 SLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRsrlGVGYLPQEASIFRGLTVEENIRAV 120
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAER---PVSMLFQENNLFPHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 121 LEVHVKDKAEREQKLNELLEEFHIQKL--RKSAavALSGGERRRLEIARALATDPTFMLLDEPFAGVDPISVADIQNLVH 198
Cdd:COG3840 96 LRPGLKLTAEQRAQVEQALERVGLAGLldRLPG--QLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 521065470 199 HLTA-RGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIV--NNPEVRRLYLG 253
Cdd:COG3840 174 ELCReRGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLdgEPPPALAAYLG 231
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
25-242 |
1.09e-36 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 131.47 E-value: 1.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 25 RGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPmyRRSRLGVGYLPQE 104
Cdd:PRK13537 11 RNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA--RHARQRVGVVPQF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 105 ASIFRGLTVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAG 184
Cdd:PRK13537 89 DNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTG 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 521065470 185 VDPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIV 242
Cdd:PRK13537 169 LDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALI 226
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
22-250 |
1.49e-36 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 129.34 E-value: 1.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPM-YRRSRLGVGY 100
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKdINKLRRKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 101 LPQEASIFRGLTVEENI-RAVLEVHVKDKAEREQKLNELLEEFHI-QKLRKSAAvALSGGERRRLEIARALATDPTFMLL 178
Cdd:COG1126 82 VFQQFNLFPHLTVLENVtLAPIKVKKMSKAEAEERAMELLERVGLaDKADAYPA-QLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521065470 179 DEPFAGVDPISVADIQNLVHHLTARGIG-VLVTdHNV---REtlgLIDRAYIIHAGEVLTHGRANDIVNNPEVRRL 250
Cdd:COG1126 161 DEPTSALDPELVGEVLDVMRDLAKEGMTmVVVT-HEMgfaRE---VADRVVFMDGGRIVEEGPPEEFFENPQHERT 232
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
31-253 |
2.18e-36 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 128.84 E-value: 2.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 31 YATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRLGVGYLPQEASIFRG 110
Cdd:PRK11614 15 YGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIVPEGRRVFSR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 111 LTVEENIraVLEVHVKDKAEREQKLNELLEEF-HIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAGVDPIS 189
Cdd:PRK11614 95 MTVEENL--AMGGFFAERDQFQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPII 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521065470 190 VADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNPEVRRLYLG 253
Cdd:PRK11614 173 IQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAYLG 236
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
21-237 |
3.57e-36 |
|
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: 134.50 E-value: 3.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 21 TLIARGLTKTYATRR-VVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRLgVG 99
Cdd:COG4988 336 SIELEDVSFSYPGGRpALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQ-IA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 100 YLPQEASIFRGlTVEENIR------------AVLE-VHVKDKAER-EQKLNELLEEfhiqklrksAAVALSGGERRRLEI 165
Cdd:COG4988 415 WVPQNPYLFAG-TIRENLRlgrpdasdeeleAALEaAGLDEFVAAlPDGLDTPLGE---------GGRGLSGGQAQRLAL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521065470 166 ARALATDPTFMLLDEPFAGVDPISVADIQNLVHHLtARGIGVLVTDHNVrETLGLIDRAYIIHAGEVLTHGR 237
Cdd:COG4988 485 ARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILITHRL-ALLAQADRILVLDDGRIVEQGT 554
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
47-236 |
5.56e-36 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 127.03 E-value: 5.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 47 GEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDG------NDVTTMPMYRRsrlGVGYLPQEASIFRGLTVEENIRAV 120
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsRKKINLPPQQR---KIGLVFQQYALFPHLNVRENLAFG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 121 LEVHvkDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAGVDPISVADIQNLVHHL 200
Cdd:cd03297 100 LKRK--RNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQI 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 521065470 201 TAR-GIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHG 236
Cdd:cd03297 178 KKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
25-246 |
1.91e-35 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 129.04 E-value: 1.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 25 RGLTKTYATR----RVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMY--RRSRLGV 98
Cdd:COG1135 5 ENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERelRAARRKI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 99 GYLPQEASIFRGLTVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLL 178
Cdd:COG1135 85 GMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLC 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521065470 179 DEPFAGVDPISVADIQNLVHHLTAR-GIGVLVTDHN---VREtlgLIDRAYIIHAGEVLTHGRANDIVNNPE 246
Cdd:COG1135 165 DEATSALDPETTRSILDLLKDINRElGLTIVLITHEmdvVRR---ICDRVAVLENGRIVEQGPVLDVFANPQ 233
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
7-237 |
3.11e-35 |
|
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: 133.04 E-value: 3.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 7 PQAAGAADKSRYQGTLIARGLTKTY--ATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGND 84
Cdd:COG2274 459 EEGRSKLSLPRLKGDIELENVSFRYpgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGID 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 85 VTTMPM--YRRSrlgVGYLPQEASIFRGlTVEENI-------------RAVLEVHVKDKAER-EQKLNELLEEFhiqklr 148
Cdd:COG2274 539 LRQIDPasLRRQ---IGVVLQDVFLFSG-TIRENItlgdpdatdeeiiEAARLAGLHDFIEAlPMGYDTVVGEG------ 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 149 ksaAVALSGGERRRLEIARALATDPTFMLLDEPFAGVDPISVADIQNLVHHLtARGIGVLVTDHNvRETLGLIDRAYIIH 228
Cdd:COG2274 609 ---GSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRL-LKGRTVIIIAHR-LSTIRLADRIIVLD 683
|
....*....
gi 521065470 229 AGEVLTHGR 237
Cdd:COG2274 684 KGRIVEDGT 692
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
22-245 |
6.41e-35 |
|
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: 127.09 E-value: 6.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYATR----RVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVP---VDEGTIEIDGNDVTTMPMYRRS 94
Cdd:COG0444 2 LEVRNLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 95 RL---GVGYLPQE--ASIFRGLTVEENIRAVLEVH-VKDKAEREQKLNELLEEFhiqKLRKSAAVA------LSGGERRR 162
Cdd:COG0444 82 KIrgrEIQMIFQDpmTSLNPVMTVGDQIAEPLRIHgGLSKAEARERAIELLERV---GLPDPERRLdrypheLSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 163 LEIARALATDPTFMLLDEPFAGVDPISVADIQNLVHHLTA-RGIGVL-VTdHNvretLGLI----DRAYIIHAGEVLTHG 236
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQReLGLAILfIT-HD----LGVVaeiaDRVAVMYAGRIVEEG 233
|
....*....
gi 521065470 237 RANDIVNNP 245
Cdd:COG0444 234 PVEELFENP 242
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-248 |
7.44e-35 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 128.41 E-value: 7.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 5 PGPQAagaadKSRYQGT--LIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDG 82
Cdd:PRK11607 6 PRPQA-----KTRKALTplLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 83 NDVTTMPMYRRSrlgVGYLPQEASIFRGLTVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRR 162
Cdd:PRK11607 81 VDLSHVPPYQRP---INMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 163 LEIARALATDPTFMLLDEPFAGVDP-------ISVADIQNLVhhltarGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTH 235
Cdd:PRK11607 158 VALARSLAKRPKLLLLDEPMGALDKklrdrmqLEVVDILERV------GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQI 231
|
250
....*....|...
gi 521065470 236 GRANDIVNNPEVR 248
Cdd:PRK11607 232 GEPEEIYEHPTTR 244
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
41-236 |
9.61e-35 |
|
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: 123.76 E-value: 9.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 41 SLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSrlgVGYLPQEASIFRGLTVEENIRAV 120
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP---VSMLFQENNLFAHLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 121 LEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAGVDPISVADIQNLVHHL 200
Cdd:cd03298 95 LSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDL 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 521065470 201 TA-RGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHG 236
Cdd:cd03298 175 HAeTKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
24-212 |
1.67e-34 |
|
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: 123.41 E-value: 1.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 24 ARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVT-TMPMYRRSRLGVGYLP 102
Cdd:cd03262 3 IKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTdDKKNINELRQKVGMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 103 QEASIFRGLTVEENIR-AVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEP 181
Cdd:cd03262 83 QQFNLFPHLTVLENITlAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEP 162
|
170 180 190
....*....|....*....|....*....|.
gi 521065470 182 FAGVDPISVADIQNLVHHLTARGIGVLVTDH 212
Cdd:cd03262 163 TSALDPELVGEVLDVMKDLAEEGMTMVVVTH 193
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
22-251 |
2.18e-34 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 124.07 E-value: 2.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSR-LGVgy 100
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARrRAV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 101 LPQEASIFRGLTVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALA-------TDP 173
Cdd:COG4559 80 LPQHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521065470 174 TFMLLDEPFAGVDPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNPEVRRLY 251
Cdd:COG4559 160 RWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELLERVY 237
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
37-245 |
2.70e-34 |
|
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: 124.29 E-value: 2.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 37 VNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMP-----MYRRSRLGVGYlpQEASIFRGL 111
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkelrELRRKKISMVF--QSFALLPHR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 112 TVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAGVDPISVA 191
Cdd:cd03294 118 TVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRR 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 521065470 192 DIQNLVHHLTA---RGIgVLVTdHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNP 245
Cdd:cd03294 198 EMQDELLRLQAelqKTI-VFIT-HDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNP 252
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
22-232 |
3.84e-34 |
|
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: 121.38 E-value: 3.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTktyaTRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRLGVGYL 101
Cdd:cd03215 5 LEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 102 P---QEASIFRGLTVEENIravlevhvkdkaereqklnelleefhiqklrkSAAVALSGGERRRLEIARALATDPTFMLL 178
Cdd:cd03215 81 PedrKREGLVLDLSVAENI--------------------------------ALSSLLSGGNQQKVVLARWLARDPRVLIL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 521065470 179 DEPFAGVDPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEV 232
Cdd:cd03215 129 DEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
34-236 |
6.19e-34 |
|
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: 121.48 E-value: 6.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 34 RRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGL--VPVDEGTIEIDGNDVTTMPMYRRSRLGVGYLPQEASIFRGL 111
Cdd:cd03217 13 KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARLGIFLAFQYPPEIPGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 112 TVEENIRAVlevhvkdkaereqklNElleefhiqklrksaavALSGGERRRLEIARALATDPTFMLLDEPFAGVDPISVA 191
Cdd:cd03217 93 KNADFLRYV---------------NE----------------GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALR 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 521065470 192 DIQNLVHHLTARGIGVLVTDHNvRETLGLI--DRAYIIHAGEVLTHG 236
Cdd:cd03217 142 LVAEVINKLREEGKSVLIITHY-QRLLDYIkpDRVHVLYDGRIVKSG 187
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
31-236 |
1.11e-33 |
|
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: 121.67 E-value: 1.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 31 YATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDvttmPMYRR----SRLGVgYLPQEAS 106
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLV----PWKRRkkflRRIGV-VFGQKTQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 107 IFRGLTVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAGVD 186
Cdd:cd03267 106 LWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 521065470 187 PISVADIQNLVHHLTA-RGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHG 236
Cdd:cd03267 186 VVAQENIRNFLKEYNReRGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
25-248 |
1.20e-33 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 122.57 E-value: 1.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 25 RGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMpmyRRSRL-----GVG 99
Cdd:PRK11831 11 RGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAM---SRSRLytvrkRMS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 100 YLPQEASIFRGLTVEENIRAVLEVHVkdkaereQKLNELLEEFHIQKLR----KSAA----VALSGGERRRLEIARALAT 171
Cdd:PRK11831 88 MLFQSGALFTDMNVFDNVAYPLREHT-------QLPAPLLHSTVMMKLEavglRGAAklmpSELSGGMARRAALARAIAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521065470 172 DPTFMLLDEPFAGVDPISVADIQNLVHHLT-ARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNPEVR 248
Cdd:PRK11831 161 EPDLIMFDEPFVGQDPITMGVLVKLISELNsALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPR 238
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
22-232 |
1.35e-33 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 120.82 E-value: 1.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRsrlGVGYL 101
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDR---DIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 102 PQEASIFRGLTVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEP 181
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 521065470 182 FAGVDPI----SVADIQNLVHHLTARGIgvLVTdHNVRETLGLIDRAYIIHAGEV 232
Cdd:cd03301 158 LSNLDAKlrvqMRAELKRLQQRLGTTTI--YVT-HDQVEAMTMADRIAVMNDGQI 209
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
33-236 |
2.56e-33 |
|
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: 120.45 E-value: 2.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 33 TRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDE---GTIEIDGNDVTTMPMYRRsrlgVGYLPQEASIFR 109
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKPDQFQKC----VAYVRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 110 GLTVEENIR--AVLEVHVKDKAEREQKLNE--LLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAGV 185
Cdd:cd03234 95 GLTVRETLTytAILRLPRKSSDAIRKKRVEdvLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 521065470 186 DPISVADIQNLVHHLTARGIGVLVTDHNVR-ETLGLIDRAYIIHAGEVLTHG 236
Cdd:cd03234 175 DSFTALNLVSTLSQLARRNRIVILTIHQPRsDLFRLFDRILLLSSGEIVYSG 226
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
7-194 |
5.85e-33 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 126.05 E-value: 5.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 7 PQAAGAADKSRYQGTLIARGLTKTY-ATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDV 85
Cdd:COG1132 325 PDPPGAVPLPPVRGEIEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDI 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 86 TTMPM--YRRSrlgVGYLPQEASIFRGlTVEENIR-------------AVLEVHVKDKAER-EQKLNELLEEfhiqklrk 149
Cdd:COG1132 405 RDLTLesLRRQ---IGVVPQDTFLFSG-TIRENIRygrpdatdeeveeAAKAAQAHEFIEAlPDGYDTVVGE-------- 472
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 521065470 150 sAAVALSGGERRRLEIARALATDPTFMLLDEPFAGVDPISVADIQ 194
Cdd:COG1132 473 -RGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQ 516
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
22-241 |
1.24e-32 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 123.98 E-value: 1.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTtmpmyRRS-----RL 96
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVR-----FRSprdaqAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 97 GVGYLPQEASIFRGLTVEENIRAVLEVHVK---DKAEREQKLNELLEEFHIqKLRKSAAVA-LSGGERRRLEIARALATD 172
Cdd:COG1129 80 GIAIIHQELNLVPNLSVAENIFLGREPRRGgliDWRAMRRRARELLARLGL-DIDPDTPVGdLSVAQQQLVEIARALSRD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521065470 173 PTFMLLDEPFAgvdPISVADIQNL---VHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDI 241
Cdd:COG1129 159 ARVLILDEPTA---SLTEREVERLfriIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
25-251 |
2.87e-32 |
|
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: 118.65 E-value: 2.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 25 RGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEG-TIEIDGN-----DVTTMpmyrRSRLGV 98
Cdd:COG1119 7 RNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGErrggeDVWEL----RKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 99 GYLPQEASIFRGLTVEENIR----AVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPT 174
Cdd:COG1119 83 VSPALQLRFPRDETVLDVVLsgffDSIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 175 FMLLDEPFAGVDPISVADIQNLVHHLTARG---IgVLVTdHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNPEVRRLY 251
Cdd:COG1119 163 LLILDEPTAGLDLGARELLLALLDKLAAEGaptL-VLVT-HHVEEIPPGITHVLLLKDGRVVAAGPKEEVLTSENLSEAF 240
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
21-251 |
5.77e-32 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 117.95 E-value: 5.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 21 TLIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRS-RLGVg 99
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELArRRAV- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 100 yLPQEASIFRGLTVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALA------TDP 173
Cdd:PRK13548 81 -LPQHSSLSFPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 174 TFMLLDEPFAGVDPISVADIQNLVHHLT-ARGIGVLVTDHNvretLGLI----DRAYIIHAGEVLTHGRANDIVNNPEVR 248
Cdd:PRK13548 160 RWLLLDEPTSALDLAHQHHVLRLARQLAhERGLAVIVVLHD----LNLAaryaDRIVLLHQGRLVADGTPAEVLTPETLR 235
|
...
gi 521065470 249 RLY 251
Cdd:PRK13548 236 RVY 238
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
22-249 |
1.09e-31 |
|
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: 1.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTT---CFYMITGLVP---VdEGTIEIDGNDV--TTMPMYR- 92
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTllrCLNRMNDLIPgarV-EGEILLDGEDIydPDVDVVEl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 93 RSRlgVGYLPQEA-----SIFrgltveENIRAVLEVH-VKDKAEreqkLNELLEEfhiqKLRKSA------------AVA 154
Cdd:COG1117 91 RRR--VGMVFQKPnpfpkSIY------DNVAYGLRLHgIKSKSE----LDEIVEE----SLRKAAlwdevkdrlkksALG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 155 LSGGERRRLEIARALATDPTFMLLDEPFAGVDPISVADIQNLVHHLTAR-GIgVLVTdHNVRETLGLIDRAYIIHAGEVL 233
Cdd:COG1117 155 LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDyTI-VIVT-HNMQQAARVSDYTAFFYLGELV 232
|
250
....*....|....*.
gi 521065470 234 THGRANDIVNNPEVRR 249
Cdd:COG1117 233 EFGPTEQIFTNPKDKR 248
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
19-241 |
1.34e-31 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 121.78 E-value: 1.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 19 QGTLIARGLTKTY--ATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTmpmYRRSRL 96
Cdd:COG4618 328 KGRLSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQ---WDREEL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 97 G--VGYLPQEASIFRGlTVEENI--------RAVLE------VHvkdkaereqklnELleefhIQKLRK-------SAAV 153
Cdd:COG4618 405 GrhIGYLPQDVELFDG-TIAENIarfgdadpEKVVAaaklagVH------------EM-----ILRLPDgydtrigEGGA 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 154 ALSGGERRRLEIARALATDPTFMLLDEPFAGVDPISVADIQNLVHHLTARGIGVLVTDHNVReTLGLIDRAYIIHAGEVL 233
Cdd:COG4618 467 RLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDGRVQ 545
|
....*...
gi 521065470 234 THGRANDI 241
Cdd:COG4618 546 AFGPRDEV 553
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
34-241 |
1.78e-31 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 121.30 E-value: 1.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 34 RRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTmpmYRRSRLG--VGYLPQEASIFRGl 111
Cdd:TIGR01842 331 KPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQ---WDRETFGkhIGYLPQDVELFPG- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 112 TVEENI---------RAVLEvhvkdkAEREQKLNELleefhIQKLRK-------SAAVALSGGERRRLEIARALATDPTF 175
Cdd:TIGR01842 407 TVAENIarfgenadpEKIIE------AAKLAGVHEL-----ILRLPDgydtvigPGGATLSGGQRQRIALARALYGDPKL 475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521065470 176 MLLDEPFAGVDPISVADIQNLVHHLTARGIGVLVTDHNVReTLGLIDRAYIIHAGEVLTHGRANDI 241
Cdd:TIGR01842 476 VVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPS-LLGCVDKILVLQDGRIARFGERDEV 540
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
36-249 |
3.66e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 116.33 E-value: 3.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 36 VVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVT---TMPMYRRSRLGVGYLPQEASIFrGLT 112
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydkKSLLEVRKTVGIVFQNPDDQLF-APT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 113 VEENIrAVLEVHVK-DKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAGVDPISVA 191
Cdd:PRK13639 96 VEEDV-AFGPLNLGlSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGAS 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 521065470 192 DIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNPEVRR 249
Cdd:PRK13639 175 QIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIR 232
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
34-232 |
3.75e-31 |
|
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: 114.28 E-value: 3.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 34 RRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTtmpmYRRSRLGVGYLPQEA-SIFRGLT 112
Cdd:cd03226 13 TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK----AKERRKSIGYVMQDVdYQLFTDS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 113 VEENIRavleVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAGVDPISVAD 192
Cdd:cd03226 89 VREELL----LGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMER 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 521065470 193 IQNLVHHLTARGIGVLVTDHNVrETLGLI-DRAYIIHAGEV 232
Cdd:cd03226 165 VGELIRELAAQGKAVIVITHDY-EFLAKVcDRVLLLANGAI 204
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
24-232 |
5.30e-31 |
|
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: 112.52 E-value: 5.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 24 ARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRLGVGYLPQ 103
Cdd:cd03216 3 LRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMVYQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 104 easifrgltveeniravlevhvkdkaereqklnelleefhiqklrksaavaLSGGERRRLEIARALATDPTFMLLDEPFA 183
Cdd:cd03216 83 ---------------------------------------------------LSVGERQMVEIARALARNARLLILDEPTA 111
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 521065470 184 GVDPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEV 232
Cdd:cd03216 112 ALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
21-236 |
1.38e-30 |
|
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: 112.64 E-value: 1.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 21 TLIARGLTKT------YATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPV--DEGTIEIDGndvttMPMYR 92
Cdd:cd03213 3 TLSFRNLTVTvksspsKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLING-----RPLDK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 93 RS-RLGVGYLPQEASIFRGLTVEENIRavlevhvkdkaereqklnelleefHIQKLRKsaavaLSGGERRRLEIARALAT 171
Cdd:cd03213 78 RSfRKIIGYVPQDDILHPTLTVRETLM------------------------FAAKLRG-----LSGGERKRVSIALELVS 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521065470 172 DPTFMLLDEPFAGVDPISVADIQNLVHHLTARGIGVLVTDHNVR-ETLGLIDRAYIIHAGEVLTHG 236
Cdd:cd03213 129 NPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSsEIFELFDKLLLLSQGRVIYFG 194
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
51-254 |
1.81e-30 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 116.35 E-value: 1.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 51 GLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDV------TTMPMYRRSrlgVGYLPQEASIFRGLTVEENIRAVLevH 124
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdsargIFLPPHRRR---IGYVFQEARLFPHLSVRGNLLYGR--K 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 125 VKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAGVDPISVADI----QNLVHHL 200
Cdd:COG4148 104 RAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEIlpylERLRDEL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 521065470 201 tarGIGVL-VTdHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNPEVRRLYLGD 254
Cdd:COG4148 184 ---DIPILyVS-HSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGE 234
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
25-250 |
3.72e-30 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 117.44 E-value: 3.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 25 RGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTmpmyrRS-----RLGVG 99
Cdd:COG3845 9 RGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRI-----RSprdaiALGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 100 YLPQEASIFRGLTVEENI---RAVLEVHVKDKAEREQKLNELLEEFHIqKLRKSAAVA-LSGGERRRLEIARALATDPTF 175
Cdd:COG3845 84 MVHQHFMLVPNLTVAENIvlgLEPTKGGRLDRKAARARIRELSERYGL-DVDPDAKVEdLSVGEQQRVEILKALYRGARI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521065470 176 MLLDEPFAGVDPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDiVNNPEVRRL 250
Cdd:COG3845 163 LILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAE-TSEEELAEL 236
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
24-232 |
4.73e-30 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 117.04 E-value: 4.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 24 ARGLTktyaTRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTtmpmyRRS-----RLGV 98
Cdd:COG1129 259 VEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVR-----IRSprdaiRAGI 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 99 GYLP---QEASIFRGLTVEENIR-AVLEVHVKDKAEREQKLNELLEEFhIQKLR------KSAAVALSGGERRRLEIARA 168
Cdd:COG1129 330 AYVPedrKGEGLVLDLSIRENITlASLDRLSRGGLLDRRRERALAEEY-IKRLRiktpspEQPVGNLSGGNQQKVVLAKW 408
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521065470 169 LATDPTFMLLDEPFAGVDPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEV 232
Cdd:COG1129 409 LATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
26-248 |
6.29e-30 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 114.80 E-value: 6.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 26 GLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTmpMYRRSRlGVGYLPQEA 105
Cdd:PRK10851 7 NIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSR--LHARDR-KVGFVFQHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 106 SIFRGLTVEENIR---AVLEVHVK-DKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEP 181
Cdd:PRK10851 84 ALFRHMTVFDNIAfglTVLPRRERpNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521065470 182 FAGVDPISVADIQNLVH--HLTARGIGVLVTdHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNPEVR 248
Cdd:PRK10851 164 FGALDAQVRKELRRWLRqlHEELKFTSVFVT-HDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATR 231
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
34-236 |
6.40e-30 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 112.08 E-value: 6.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 34 RRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGL--VPVDEGTIEIDGNDVTTMPMYRRSRLGVGYL---PQEasiF 108
Cdd:COG0396 13 KEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPDERARAGIFLAfqyPVE---I 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 109 RGLTVEENIRAVLEVHVKDK---AEREQKLNELLEEFHIQK--LRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFA 183
Cdd:COG0396 90 PGVSVSNFLRTALNARRGEElsaREFLKLLKEKMKELGLDEdfLDRYVNEGFSGGEKKRNEILQMLLLEPKLAILDETDS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 521065470 184 GVDPISVADIQNLVHHLTARGIGVLVTDHNVReTLGLI--DRAYIIHAGEVLTHG 236
Cdd:COG0396 170 GLDIDALRIVAEGVNKLRSPDRGILIITHYQR-ILDYIkpDFVHVLVDGRIVKSG 223
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
22-196 |
9.64e-30 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 113.67 E-value: 9.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYATR-----------RVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMP- 89
Cdd:COG4608 8 LEVRDLKKHFPVRgglfgrtvgvvKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 90 --MyRRSRLGVGYLPQE--ASIFRGLTVEENIRAVLEVH-VKDKAEREQKLNELLEEFhiqKLRKSAAV----ALSGGER 160
Cdd:COG4608 88 reL-RPLRRRMQMVFQDpyASLNPRMTVGDIIAEPLRIHgLASKAERRERVAELLELV---GLRPEHADryphEFSGGQR 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 521065470 161 RRLEIARALATDPTFMLLDEPFAGVDpISV-ADIQNL 196
Cdd:COG4608 164 QRIGIARALALNPKLIVCDEPVSALD-VSIqAQVLNL 199
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
22-181 |
1.71e-29 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 115.55 E-value: 1.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIdGNDVTtmpmyrrsrlgVGYL 101
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK-----------IGYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 102 PQEASIFR-GLTVEENIRAVLEvhvkdkAEREQKLNELLEE--FHIQKLRKSAAVaLSGGERRRLEIARALATDPTFMLL 178
Cdd:COG0488 384 DQHQEELDpDKTVLDELRDGAP------GGTEQEVRGYLGRflFSGDDAFKPVGV-LSGGEKARLALAKLLLSPPNVLLL 456
|
...
gi 521065470 179 DEP 181
Cdd:COG0488 457 DEP 459
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
24-241 |
2.15e-29 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 115.53 E-value: 2.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 24 ARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRLGVGYLPQ 103
Cdd:PRK15439 14 ARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYLVPQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 104 EASIFRGLTVEENIRAVLEVHvkdkAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFA 183
Cdd:PRK15439 94 EPLLFPNLSVKENILFGLPKR----QASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 521065470 184 GVDPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDI 241
Cdd:PRK15439 170 SLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
21-220 |
2.60e-29 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 111.11 E-value: 2.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 21 TLIARGLTKTY----ATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTmPMYRRsrl 96
Cdd:COG4525 3 MLTVRHVSVRYpgggQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGADR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 97 GVGYlpQEASIFRGLTVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFM 176
Cdd:COG4525 79 GVVF--QKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 521065470 177 LLDEPFAGVDPISVADIQNLVHHLTAR-GIGVLVTDHNVRETLGL 220
Cdd:COG4525 157 LMDEPFGALDALTREQMQELLLDVWQRtGKGVFLITHSVEEALFL 201
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
22-232 |
2.88e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 110.95 E-value: 2.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYAT-----RRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRL 96
Cdd:COG1101 2 LELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 97 gVGYLPQEASI--FRGLTVEENI-------------RAVlevhvkDKAEREQkLNELLEEFHI---QKLrKSAAVALSGG 158
Cdd:COG1101 82 -IGRVFQDPMMgtAPSMTIEENLalayrrgkrrglrRGL------TKKRREL-FRELLATLGLgleNRL-DTKVGLLSGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 159 ERRRLEIARALATDPTFMLLDEPFAGVDPISVADI----QNLV--HHLTArgigVLVTdHNVRETLGLIDRAYIIHAGEV 232
Cdd:COG1101 153 QRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVleltEKIVeeNNLTT----LMVT-HNMEQALDYGNRLIMMHEGRI 227
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
32-232 |
5.80e-29 |
|
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: 107.69 E-value: 5.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 32 ATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTmpmYRRSRLG--VGYLPQEASIFR 109
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQ---WDPNELGdhVGYLPQDDELFS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 110 GlTVEENIravlevhvkdkaereqklnelleefhiqklrksaavaLSGGERRRLEIARALATDPTFMLLDEPFAGVDPIS 189
Cdd:cd03246 90 G-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEG 131
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 521065470 190 VADIQNLVHHLTARGIGVLVTDHNvRETLGLIDRAYIIHAGEV 232
Cdd:cd03246 132 ERALNQAIAALKAAGATRIVIAHR-PETLASADRILVLEDGRV 173
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
22-230 |
5.87e-29 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 108.98 E-value: 5.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYATR----RVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRL- 96
Cdd:TIGR02211 2 LKCENLGKRYQEGkldtRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKLr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 97 --GVGYLPQEASIFRGLTVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPT 174
Cdd:TIGR02211 82 nkKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPS 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 521065470 175 FMLLDEPFAGVDPISVADIQNLVHHL-TARGIGVLVTDHNvRETLGLIDRAYIIHAG 230
Cdd:TIGR02211 162 LVLADEPTGNLDNNNAKIIFDLMLELnRELNTSFLVVTHD-LELAKKLDRVLEMKDG 217
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
41-243 |
2.38e-28 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 107.75 E-value: 2.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 41 SLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSrlgVGYLPQEASIFRGLTVEENIRAV 120
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRP---VSMLFQENNLFSHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 121 LEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAGVDPISVADIQNLVHHL 200
Cdd:PRK10771 96 LNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQV 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 521065470 201 -TARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVN 243
Cdd:PRK10771 176 cQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
15-236 |
3.36e-28 |
|
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: 107.23 E-value: 3.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 15 KSRYQGTLIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMpmyrrs 94
Cdd:cd03220 16 GSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLL------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 95 RLGVGYLPQeasifrgLTVEENIRAVLEVHVKDKAEREQKLNEL-----LEEFHIQKLRKsaavaLSGGERRRLEIARAL 169
Cdd:cd03220 90 GLGGGFNPE-------LTGRENIYLNGRLLGLSRKEIDEKIDEIiefseLGDFIDLPVKT-----YSSGMKARLAFAIAT 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521065470 170 ATDPTFMLLDEPFAGVDPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHG 236
Cdd:cd03220 158 ALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
25-213 |
6.70e-28 |
|
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: 105.95 E-value: 6.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 25 RGLTKTY-ATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTM-----PMYRRSrLGV 98
Cdd:cd03292 4 INVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgraiPYLRRK-IGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 99 GYlpQEASIFRGLTVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLL 178
Cdd:cd03292 83 VF--QDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190
....*....|....*....|....*....|....*
gi 521065470 179 DEPFAGVDPISVADIQNLVHHLTARGIGVLVTDHN 213
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHA 195
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
21-210 |
8.24e-28 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 105.64 E-value: 8.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 21 TLIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVD---EGTIEIDGNDVTTMPMYRRsrlG 97
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQR---R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 98 VGYLPQEASIFRGLTVEENIRAVLEVHVKdKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFML 177
Cdd:COG4136 78 IGILFQDDLLFPHLSVGENLAFALPPTIG-RAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALL 156
|
170 180 190
....*....|....*....|....*....|....*
gi 521065470 178 LDEPFAGVDPISVADIQNLV-HHLTARGI-GVLVT 210
Cdd:COG4136 157 LDEPFSKLDAALRAQFREFVfEQIRQRGIpALLVT 191
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
24-181 |
9.72e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 110.92 E-value: 9.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 24 ARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNdvttmpmyrrsrLGVGYLPQ 103
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG------------LRIGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 104 EASIFRGLTVEENIRAVLEVHVKDKAEREQ-------------KLNELLEEFH--------------IQKLRKSAAV--- 153
Cdd:COG0488 69 EPPLDDDLTVLDTVLDGDAELRALEAELEEleaklaepdedleRLAELQEEFEalggweaearaeeiLSGLGFPEEDldr 148
|
170 180 190
....*....|....*....|....*....|.
gi 521065470 154 ---ALSGGERRRLEIARALATDPTFMLLDEP 181
Cdd:COG0488 149 pvsELSGGWRRRVALARALLSEPDLLLLDEP 179
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
34-236 |
1.83e-27 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 105.81 E-value: 1.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 34 RRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITG--LVPVDEGTIEIDGNDVTTMPMYRRSRLGVGYLPQEASIFRGL 111
Cdd:TIGR01978 13 KEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGhpSYEVTSGTILFKGQDLLELEPDERARAGLFLAFQYPEEIPGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 112 TVEENIRAVLEVHVKDKAEREQKLNELLEEFH--IQKLRKSAA-------VALSGGERRRLEIARALATDPTFMLLDEPF 182
Cdd:TIGR01978 93 SNLEFLRSALNARRSARGEEPLDLLDFEKLLKekLALLDMDEEflnrsvnEGFSGGEKKRNEILQMALLEPKLAILDEID 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 521065470 183 AGVDPISVADIQNLVHHLTARGIGVLVTDHNVReTLGLI--DRAYIIHAGEVLTHG 236
Cdd:TIGR01978 173 SGLDIDALKIVAEGINRLREPDRSFLIITHYQR-LLNYIkpDYVHVLLDGRIVKSG 227
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
24-188 |
4.10e-27 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 109.83 E-value: 4.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 24 ARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTI-----EIDGNDVTTmpmyrRSRlgV 98
Cdd:NF033858 269 ARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwlfgqPVDAGDIAT-----RRR--V 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 99 GYLPQEASIFRGLTVEENiravLEVHVK----DKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPT 174
Cdd:NF033858 342 GYMSQAFSLYGELTVRQN----LELHARlfhlPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPE 417
|
170
....*....|....
gi 521065470 175 FMLLDEPFAGVDPI 188
Cdd:NF033858 418 LLILDEPTSGVDPV 431
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
21-223 |
1.84e-26 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 107.37 E-value: 1.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 21 TLIARGLTKTYATRR-VVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRsRLGVG 99
Cdd:TIGR02857 321 SLEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW-RDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 100 YLPQEASIFRGlTVEENIR----AVLEVHVKDKAEReQKLNELLEEF--HIQKLRKSAAVALSGGERRRLEIARALATDP 173
Cdd:TIGR02857 400 WVPQHPFLFAG-TIAENIRlarpDASDAEIREALER-AGLDEFVAALpqGLDTPIGEGGAGLSGGQAQRLALARAFLRDA 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 521065470 174 TFMLLDEPFAGVDPISVADIQNLVHHLtARGIGVLVTDHNvRETLGLIDR 223
Cdd:TIGR02857 478 PLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHR-LALAALADR 525
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
31-212 |
1.91e-26 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 101.54 E-value: 1.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 31 YATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEidgndvttmpmyRRSRLGVGYLPQEASIFRG 110
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR------------RAGGARVAYVPQRSEVPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 111 L--TVEENI-------RAVLEVHvkdKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEP 181
Cdd:NF040873 70 LplTVRDLVamgrwarRGLWRRL---TRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEP 146
|
170 180 190
....*....|....*....|....*....|.
gi 521065470 182 FAGVDPISVADIQNLVHHLTARGIGVLVTDH 212
Cdd:NF040873 147 TTGLDAESRERIIALLAEEHARGATVVVVTH 177
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
25-245 |
2.13e-26 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 105.41 E-value: 2.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 25 RGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSrlgVGYLPQE 104
Cdd:PRK09452 18 RGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRH---VNTVFQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 105 ASIFRGLTVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAG 184
Cdd:PRK09452 95 YALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521065470 185 VDPISVADIQNLVHHLTaRGIG---VLVTdHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNP 245
Cdd:PRK09452 175 LDYKLRKQMQNELKALQ-RKLGitfVFVT-HDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEP 236
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
20-237 |
2.13e-26 |
|
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: 102.11 E-value: 2.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 20 GTLIARGLTKTYATR--RVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYR-RSRL 96
Cdd:cd03369 5 GEIEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDlRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 97 GVgyLPQEASIFRGltveeNIRAVLEVhvkdkaEREQKLNELLEEFHIqklrKSAAVALSGGERRRLEIARALATDPTFM 176
Cdd:cd03369 85 TI--IPQDPTLFSG-----TIRSNLDP------FDEYSDEEIYGALRV----SEGGLNLSQGQRQLLCLARALLKRPRVL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521065470 177 LLDEPFAGVDPISVADIQNLVHHLTArGIGVLVTDHNVReTLGLIDRAYIIHAGEVLTHGR 237
Cdd:cd03369 148 VLDEATASIDYATDALIQKTIREEFT-NSTILTIAHRLR-TIIDYDKILVMDAGEVKEYDH 206
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
22-212 |
2.86e-26 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 101.28 E-value: 2.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDV-TTMPMYRRSRLGVGY 100
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLaEQRDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 101 LPqeaSIFRGLTVEENIRAVLEVHvkdkAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDE 180
Cdd:TIGR01189 81 LP---GLKPELSALENLHFWAAIH----GGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDE 153
|
170 180 190
....*....|....*....|....*....|..
gi 521065470 181 PFAGVDPISVADIQNLVHHLTARGIGVLVTDH 212
Cdd:TIGR01189 154 PTTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
40-245 |
4.63e-26 |
|
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: 104.42 E-value: 4.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 40 VSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDG-------NDVTTMPMYRRsrlgVGYLPQEASIFRGLT 112
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfdsrKGIFLPPEKRR----IGYVFQEARLFPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 113 VEENIR-AVLEVHVKDKAEREQKLNELLeefHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAGVDPISVA 191
Cdd:TIGR02142 92 VRGNLRyGMKRARPSERRISFERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 521065470 192 DIQNLVHHLTAR-GIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNP 245
Cdd:TIGR02142 169 EILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
22-244 |
5.62e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 103.24 E-value: 5.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYATR-----RVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGND------------ 84
Cdd:PRK13651 3 IKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 85 -----VTTMPMYR--------RSRLGVGYLPQEASIFRGlTVEENI------RAVLEVHVKDKAEREQKLNELLEEFhiq 145
Cdd:PRK13651 83 vleklVIQKTRFKkikkikeiRRRVGVVFQFAEYQLFEQ-TIEKDIifgpvsMGVSKEEAKKRAAKYIELVGLDESY--- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 146 kLRKSAaVALSGGERRRLEIARALATDPTFMLLDEPFAGVDPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAY 225
Cdd:PRK13651 159 -LQRSP-FELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTI 236
|
250
....*....|....*....
gi 521065470 226 IIHAGEVLTHGRANDIVNN 244
Cdd:PRK13651 237 FFKDGKIIKDGDTYDILSD 255
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
34-236 |
5.99e-26 |
|
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: 106.64 E-value: 5.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 34 RRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDV-TTMPMYRRSrlgVGYLPQEASIFRGLT 112
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAVRQS---LGMCPQHNILFHHLT 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 113 VEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAGVDPISVAD 192
Cdd:TIGR01257 1020 VAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRS 1099
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 521065470 193 IQNLVhhLTAR-GIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHG 236
Cdd:TIGR01257 1100 IWDLL--LKYRsGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
25-244 |
6.15e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 103.24 E-value: 6.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 25 RGLTK-TYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITG-LVPvDEGTIEIDGNDvttmPMYRRSRlgvgYLP 102
Cdd:COG4586 25 KGLFRrEYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGiLVP-TSGEVRVLGYV----PFKRRKE----FAR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 103 QEASIFrG--------LTVEEN---IRAVLEVhvkDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALAT 171
Cdd:COG4586 96 RIGVVF-GqrsqlwwdLPAIDSfrlLKAIYRI---PDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLH 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521065470 172 DPTFMLLDEPFAGVDPISVADIQNLVHHLTA-RGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNN 244
Cdd:COG4586 172 RPKILFLDEPTIGLDVVSKEAIREFLKEYNReRGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKER 245
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
3-213 |
6.35e-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: 105.91 E-value: 6.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 3 GKPGPQAAGAADKSRYQGTLIARGLTKTYAT-RRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEID 81
Cdd:TIGR02868 316 PVAEGSAPAAGAVGLGKPTLELRDLSAGYPGaPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLD 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 82 GNDVTTMPMYRRSRLgVGYLPQEASIFrGLTVEENIR-AVLEVHVKD--KAEREQKLNELLEEFH--IQKLRKSAAVALS 156
Cdd:TIGR02868 396 GVPVSSLDQDEVRRR-VSVCAQDAHLF-DTTVRENLRlARPDATDEElwAALERVGLADWLRALPdgLDTVLGEGGARLS 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 521065470 157 GGERRRLEIARALATDPTFMLLDEPFAGVDPISVADiqnLVHHLTA--RGIGVLVTDHN 213
Cdd:TIGR02868 474 GGERQRLALARALLADAPILLLDEPTEHLDAETADE---LLEDLLAalSGRTVVLITHH 529
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
26-214 |
7.09e-26 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 101.63 E-value: 7.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 26 GLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGN--DVTTMPMYRRSRL---GVGY 100
Cdd:COG4161 7 NINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSEKAIRLlrqKVGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 101 LPQEASIFRGLTVEEN-IRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLD 179
Cdd:COG4161 87 VFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFD 166
|
170 180 190
....*....|....*....|....*....|....*
gi 521065470 180 EPFAGVDPISVADIQNLVHHLTARGIGVLVTDHNV 214
Cdd:COG4161 167 EPTAALDPEITAQVVEIIRELSQTGITQVIVTHEV 201
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
22-212 |
8.58e-26 |
|
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: 100.26 E-value: 8.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGN-DVTTMPMYRRSRLGVGY 100
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGpLDFQRDSIARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 101 LPqeaSIFRGLTVEENIRAVLEVHVKDKAEreqklnELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDE 180
Cdd:cd03231 81 AP---GIKTTLSVLENLRFWHADHSDEQVE------EALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDE 151
|
170 180 190
....*....|....*....|....*....|..
gi 521065470 181 PFAGVDPISVADIQNLVHHLTARGIGVLVTDH 212
Cdd:cd03231 152 PTTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
22-218 |
9.42e-26 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 101.31 E-value: 9.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTmPMYRRsrlgvGYL 101
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-PGAER-----GVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 102 PQEASIFRGLTVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEP 181
Cdd:PRK11248 76 FQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEP 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 521065470 182 FAGVDPISVADIQNLVHHLTAR-GIGVLVTDHNVRETL 218
Cdd:PRK11248 156 FGALDAFTREQMQTLLLKLWQEtGKQVLLITHDIEEAV 193
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-246 |
9.93e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 101.53 E-value: 9.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 19 QGTLIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLV-----PVDEGTIEIDGNDVTTMPMYRR 93
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 94 SRLgVGYLPQEASIFRGLTVEENIRAVLEVH--VKDKAEREQKLNELLEEFHIQKLRK----SAAVALSGGERRRLEIAR 167
Cdd:PRK14247 81 RRR-VQMVFQIPNPIPNLSIFENVALGLKLNrlVKSKKELQERVRWALEKAQLWDEVKdrldAPAGKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521065470 168 ALATDPTFMLLDEPFAGVDPISVADIQNLVHHLTARGIGVLVTdHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNPE 246
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVT-HFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPR 237
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
25-250 |
1.81e-25 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 100.55 E-value: 1.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 25 RGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRS-RLGVGYLPQ 103
Cdd:PRK09493 5 KNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLiRQEAGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 104 EASIFRGLTVEENIrAVLEVHVK--DKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEP 181
Cdd:PRK09493 85 QFYLFPHLTALENV-MFGPLRVRgaSKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521065470 182 FAGVDPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNPEVRRL 250
Cdd:PRK09493 164 TSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRL 232
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
21-249 |
3.26e-25 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 99.82 E-value: 3.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 21 TLIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTI-----EIDGNDVTTMP--MYRR 93
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTARSLSQQkgLIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 94 SRLGVGYLPQEASIFRGLTVEEN-IRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATD 172
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHRTVLENiIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521065470 173 PTFMLLDEPFAGVDPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNPEVRR 249
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPR 239
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
25-251 |
4.36e-25 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 99.77 E-value: 4.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 25 RGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSR-LGVgyLPQ 103
Cdd:COG4604 5 KNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKrLAI--LRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 104 EASIFRGLTVEEniravLeV------HVKDK--AEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTF 175
Cdd:COG4604 83 ENHINSRLTVRE-----L-VafgrfpYSKGRltAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 176 MLLDEPFAGVDPISVADIQNLVHHLT-ARGIGVLVTDHNvretlglIDRA-----YII--HAGEVLTHGRANDIVNNPEV 247
Cdd:COG4604 157 VLLDEPLNNLDMKHSVQMMKLLRRLAdELGKTVVIVLHD-------INFAscyadHIVamKDGRVVAQGTPEEIITPEVL 229
|
....
gi 521065470 248 RRLY 251
Cdd:COG4604 230 SDIY 233
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
36-242 |
5.60e-25 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 98.84 E-value: 5.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 36 VVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVT--TMPMYRRSrlgVGYLPQEASIFRGlTV 113
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRdyTLASLRRQ---IGLVSQDVFLFND-TV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 114 EENIRavlevHVKDKAEREQKLNEL----LEEFhIQKLRK-------SAAVALSGGERRRLEIARALATDPTFMLLDEPF 182
Cdd:cd03251 93 AENIA-----YGRPGATREEVEEAAraanAHEF-IMELPEgydtvigERGVKLSGGQRQRIAIARALLKDPPILILDEAT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 183 AGVDPISVADIQNLVHHLTArGIGVLVTDHNVrETLGLIDRAYIIHAGEVLTHGRANDIV 242
Cdd:cd03251 167 SALDTESERLVQAALERLMK-NRTTFVIAHRL-STIENADRIVVLEDGKIVERGTHEELL 224
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
35-247 |
5.66e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 99.81 E-value: 5.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 35 RVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYR-RSRLGVGYLPQEASIFRGlTV 113
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvRSKVGLVFQDPDDQVFSS-TV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 114 EENIrAVLEVHVK-DKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAGVDPISVAD 192
Cdd:PRK13647 98 WDDV-AFGPVNMGlDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQET 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 521065470 193 IQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGrANDIVNNPEV 247
Cdd:PRK13647 177 LMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG-DKSLLTDEDI 230
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
34-232 |
6.62e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 102.80 E-value: 6.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 34 RRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRLGVGYLPQEasifR---- 109
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVAYIPED----Rlgrg 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 110 ---GLTVEENirAVLEVHVK---------DKAEREQKLNELLEEFHIQKLRKSAAV-ALSGGERRRLEIARALATDPTFM 176
Cdd:COG3845 347 lvpDMSVAEN--LILGRYRRppfsrggflDRKAIRAFAEELIEEFDVRTPGPDTPArSLSGGNQQKVILARELSRDPKLL 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 521065470 177 LLDEPFAGVDPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEV 232
Cdd:COG3845 425 IAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-249 |
8.84e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 98.96 E-value: 8.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 25 RGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTT---CFYMITGLvpvdEGTIEIDGN-DVTTMPMYRRsRLGVGY 100
Cdd:PRK14258 11 NNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTflkCLNRMNEL----ESEVRVEGRvEFFNQNIYER-RVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 101 LPQEASIFRG------LTVEENIRAVLE-------VHVKDKAEREQKLNELLEEFHiQKLRKSAaVALSGGERRRLEIAR 167
Cdd:PRK14258 86 LRRQVSMVHPkpnlfpMSVYDNVAYGVKivgwrpkLEIDDIVESALKDADLWDEIK-HKIHKSA-LDLSGGQQQRLCIAR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 168 ALATDPTFMLLDEPFAGVDPISVADIQNLVHHLTARG-IGVLVTDHNVRETLGLIDRAYIIHA-----GEVLTHGRANDI 241
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSeLTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKI 243
|
....*...
gi 521065470 242 VNNPEVRR 249
Cdd:PRK14258 244 FNSPHDSR 251
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
34-246 |
1.06e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 98.97 E-value: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 34 RRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGN------DVTTMPMYRRsRLGVGYLPQEASI 107
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKL-RKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 108 FRGLTVEENIRAVLEVH-VKDKAEREQKLNELLEEFHIQK----LRKSAAVALSGGERRRLEIARALATDPTFMLLDEPF 182
Cdd:PRK14246 102 FPHLSIYDNIAYPLKSHgIKEKREIKKIVEECLRKVGLWKevydRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521065470 183 AGVDPISVADIQNLVHHLTaRGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNPE 246
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELK-NEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPK 244
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
36-195 |
2.09e-24 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 97.30 E-value: 2.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 36 VVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYR-RSRlgVGYLPQEASIFRGlTVE 114
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlRSM--IGVVLQDTFLFSG-TIM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 115 ENIRAVLEVHVKDKAEREQKLNELLEEfhIQKLRK-------SAAVALSGGERRRLEIARALATDPTFMLLDEPFAGVDP 187
Cdd:cd03254 95 ENIRLGRPNATDEEVIEAAKEAGAHDF--IMKLPNgydtvlgENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDT 172
|
....*...
gi 521065470 188 ISVADIQN 195
Cdd:cd03254 173 ETEKLIQE 180
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
25-249 |
2.43e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 98.34 E-value: 2.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 25 RGLTKTYAT-RRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYR-RSRLGVGYLP 102
Cdd:PRK13652 7 RDLCYSYSGsKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREvRKFVGLVFQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 103 QEASIFrGLTVEENIrAVLEVHVK-DKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEP 181
Cdd:PRK13652 87 PDDQIF-SPTVEQDI-AFGPINLGlDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521065470 182 FAGVDPISVADIQNLVHHLTAR-GIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNPEVRR 249
Cdd:PRK13652 165 TAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDLLA 233
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
36-247 |
3.17e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 97.75 E-value: 3.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 36 VVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPM-YRRSRLGVgylpqeasIFR----- 109
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLkEIRKKIGI--------IFQnpdnq 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 110 --GLTVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAGVDP 187
Cdd:PRK13632 96 fiGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDP 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521065470 188 ISVADIQNLVHHLTARGIGVLVT-DHNVRETLgLIDRAYIIHAGEVLTHGRANDIVNNPEV 247
Cdd:PRK13632 176 KGKREIKKIMVDLRKTRKKTLISiTHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNNKEI 235
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
27-255 |
3.25e-24 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 97.78 E-value: 3.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 27 LTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVD---EGTIEIDGNDVTTMPMY----RRSRLGVG 99
Cdd:PRK09984 10 LAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksaGSHIELLGRTVQREGRLardiRKSRANTG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 100 YLPQEASIFRGLTVEENI-----------RAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSaavALSGGERRRLEIARA 168
Cdd:PRK09984 90 YIFQQFNLVNRLSVLENVligalgstpfwRTCFSWFTREQKQRALQALTRVGMVHFAHQRVS---TLSGGQQQRVAIARA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 169 LATDPTFMLLDEPFAGVDPISVADIQNLVHHLTAR-GIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGrANDIVNNPEV 247
Cdd:PRK09984 167 LMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHVFYDG-SSQQFDNERF 245
|
....*...
gi 521065470 248 RRLYLGDN 255
Cdd:PRK09984 246 DHLYRSIN 253
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
22-254 |
3.70e-24 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 99.02 E-value: 3.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSrlgVGYL 101
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRD---ICMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 102 PQEASIFRGLTVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEP 181
Cdd:PRK11432 84 FQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521065470 182 FAGVDPISVADIQNLVHHLTAR-GIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNPEVRRL--YLGD 254
Cdd:PRK11432 164 LSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMasFMGD 239
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
25-245 |
4.16e-24 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 98.72 E-value: 4.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 25 RGLTKTYATRR----VVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTM--PMYRRSRLGV 98
Cdd:PRK11153 5 KNISKVFPQGGrtihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALseKELRKARRQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 99 GYLPQEASIFRGLTVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLL 178
Cdd:PRK11153 85 GMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLC 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521065470 179 DEPFAGVDPISVADIQNLVHHLTAR-GIGVLVTDHN---VREtlgLIDRAYIIHAGEVLTHGRANDIVNNP 245
Cdd:PRK11153 165 DEATSALDPATTRSILELLKDINRElGLTIVLITHEmdvVKR---ICDRVAVIDAGRLVEQGTVSEVFSHP 232
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
21-248 |
5.82e-24 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 99.15 E-value: 5.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 21 TLIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRLgVGY 100
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR-VAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 101 LPQEASIFRGLTVEENIRAVLEVHVK-----DKAEReQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTF 175
Cdd:PRK09536 82 VPQDTSLSFEFDVRQVVEMGRTPHRSrfdtwTETDR-AAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521065470 176 MLLDEPFAGVDPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNPEVR 248
Cdd:PRK09536 161 LLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLR 233
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
23-246 |
5.94e-24 |
|
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: 100.14 E-value: 5.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 23 IARG-LTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPvDEGTIEIDGNDVTTMPMYR----RSRLG 97
Cdd:COG4172 287 IKRGlFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRAlrplRRRMQ 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 98 VgylpqeasIF---------RgLTVEENIRAVLEVH--VKDKAEREQKLNELLEEFHIqklrkSAAVA------LSGGER 160
Cdd:COG4172 366 V--------VFqdpfgslspR-MTVGQIIAEGLRVHgpGLSAAERRARVAEALEEVGL-----DPAARhrypheFSGGQR 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 161 RRLEIARALATDPTFMLLDEPFAGVDpISV-ADIQNLVHHLTAR-GIGVLVTDHN---VREtlgLIDRAYIIHAGEVLTH 235
Cdd:COG4172 432 QRIAIARALILEPKLLVLDEPTSALD-VSVqAQILDLLRDLQREhGLAYLFISHDlavVRA---LAHRVMVMKDGKVVEQ 507
|
250
....*....|.
gi 521065470 236 GRANDIVNNPE 246
Cdd:COG4172 508 GPTEQVFDAPQ 518
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
39-241 |
8.28e-24 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 96.06 E-value: 8.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 39 GVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPvDEGTIEIDGNDVTTMPMYRRSRLGvGYLPQEASIFRGLTVEEnir 118
Cdd:COG4138 14 PISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAELARHR-AYLSQQQSPPFAMPVFQ--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 119 aVLEVHVKDKA---EREQKLNELLEEFHIQ-KLRKSAAvALSGGERRRLEIARAL-----ATDPT--FMLLDEPFAGVDP 187
Cdd:COG4138 89 -YLALHQPAGAsseAVEQLLAQLAEALGLEdKLSRPLT-QLSGGEWQRVRLAAVLlqvwpTINPEgqLLLLDEPMNSLDV 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 521065470 188 ISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDI 241
Cdd:COG4138 167 AQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEV 220
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
22-233 |
8.46e-24 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 96.41 E-value: 8.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYAT---------RRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTM--PM 90
Cdd:TIGR02769 3 LEVRDVTHTYRTgglfgakqrAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdrKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 91 YRRSRLGVGYLPQEA--SIFRGLTVEENIRAVLEvHVK--DKAEREQKLNELLEEF-----HIQKLRKSaavaLSGGERR 161
Cdd:TIGR02769 83 RRAFRRDVQLVFQDSpsAVNPRMTVRQIIGEPLR-HLTslDESEQKARIAELLDMVglrseDADKLPRQ----LSGGQLQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521065470 162 RLEIARALATDPTFMLLDEPFAGVDPISVADIQNLVHHLTAR-GIGVLVTDHNVRETLGLIDRAYIIHAGEVL 233
Cdd:TIGR02769 158 RINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAfGTAYLFITHDLRLVQSFCQRVAVMDKGQIV 230
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
27-250 |
3.90e-23 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 94.65 E-value: 3.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 27 LTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTtmpMYR-------------- 92
Cdd:PRK10619 11 LHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTIN---LVRdkdgqlkvadknql 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 93 ---RSRLGVGYlpQEASIFRGLTVEENI-RAVLEVHVKDKAEREQKLNELLEEFHI-QKLRKSAAVALSGGERRRLEIAR 167
Cdd:PRK10619 88 rllRTRLTMVF--QHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIdERAQGKYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 168 ALATDPTFMLLDEPFAGVDPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNPEV 247
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQS 245
|
...
gi 521065470 248 RRL 250
Cdd:PRK10619 246 PRL 248
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
26-214 |
5.04e-23 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 93.93 E-value: 5.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 26 GLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGN--DVTTMP---MYRRSRLGVGY 100
Cdd:PRK11124 7 GINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPsdkAIRELRRNVGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 101 LPQEASIFRGLTVEEN-IRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLD 179
Cdd:PRK11124 87 VFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFD 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 521065470 180 EPFAGVDPISVADIQNLVHHLTARGIG-VLVTdHNV 214
Cdd:PRK11124 167 EPTAALDPEITAQIVSIIRELAETGITqVIVT-HEV 201
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
37-234 |
6.74e-23 |
|
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: 93.30 E-value: 6.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 37 VNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTT-----MPMYrrsrlgvgylpQEASIFRGL 111
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEpgpdrMVVF-----------QNYSLLPWL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 112 TVEENIR-AVLEV-HVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAGVDPIS 189
Cdd:TIGR01184 70 TVRENIAlAVDRVlPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 521065470 190 VADIQNLV------HHLTArgigVLVTdHNVRETLGLIDRAYII------HAGEVLT 234
Cdd:TIGR01184 150 RGNLQEELmqiweeHRVTV----LMVT-HDVDEALLLSDRVVMLtngpaaNIGQILE 201
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
33-237 |
7.09e-23 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 97.04 E-value: 7.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 33 TRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVD---EGTIEIDGNDVTTMPMYRRSrlgvGYLPQEASIFR 109
Cdd:TIGR00955 37 RKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRAIS----AYVQQDDLFIP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 110 GLTVEE--NIRAVLEVHVK-DKAEREQKLNELLEEFHIQKLRKS------AAVALSGGERRRLEIARALATDPTFMLLDE 180
Cdd:TIGR00955 113 TLTVREhlMFQAHLRMPRRvTKKEKRERVDEVLQALGLRKCANTrigvpgRVKGLSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 521065470 181 PFAGVDPISVADIQNLVHHLTARGIGVLVTDHNVRETL-GLIDRAYIIHAGEVLTHGR 237
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELfELFDKIILMAEGRVAYLGS 250
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
26-253 |
7.79e-23 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 96.78 E-value: 7.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 26 GLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRLGVGYLPQEA 105
Cdd:PRK09700 10 GIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGIIYQEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 106 SIFRGLTVEENI-------RAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLL 178
Cdd:PRK09700 90 SVIDELTVLENLyigrhltKKVCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIM 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521065470 179 DEPFAGVDPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDiVNNPEVRRLYLG 253
Cdd:PRK09700 170 DEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSD-VSNDDIVRLMVG 243
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
21-213 |
1.21e-22 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 91.86 E-value: 1.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 21 TLIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTmPMYRRSrlgVGY 100
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDD-PDVAEA---CHY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 101 LPQEASIFRGLTVEENI---RAVLevhvkdkAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFML 177
Cdd:PRK13539 78 LGHRNAMKPALTVAENLefwAAFL-------GGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWI 150
|
170 180 190
....*....|....*....|....*....|....*..
gi 521065470 178 LDEPFAGVDPISVADIQNLV-HHLTARGIgVLVTDHN 213
Cdd:PRK13539 151 LDEPTAALDAAAVALFAELIrAHLAQGGI-VIAATHI 186
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
22-243 |
1.25e-22 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 92.84 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGndvttmpmyRRS---RLGV 98
Cdd:COG1134 27 LLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG---------RVSallELGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 99 GYLPQeasifrgLTVEENIRAVLEVHVKDKAEREQKLNEL-----LEEFHIQKLRksaavALSGGERRRLEIARALATDP 173
Cdd:COG1134 98 GFHPE-------LTGRENIYLNGRLLGLSRKEIDEKFDEIvefaeLGDFIDQPVK-----TYSSGMRARLAFAVATAVDP 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521065470 174 TFMLLDEpfagVdpISVADI------QNLVHHLTARGIGVLVTDHN---VREtlgLIDRAYIIHAGEVLTHGRANDIVN 243
Cdd:COG1134 166 DILLVDE----V--LAVGDAafqkkcLARIRELRESGRTVIFVSHSmgaVRR---LCDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
32-234 |
1.26e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 92.47 E-value: 1.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 32 ATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMP--MYRRSrlgVGYLPQEASIFr 109
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKpeIYRQQ---VSYCAQTPTLF- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 110 GLTVEENIraVLEVHVKDKAEREQKLNELLEEFHIQK--LRKSAAvALSGGERRRLEIARALATDPTFMLLDEPFAGVDP 187
Cdd:PRK10247 94 GDTVYDNL--IFPWQIRNQQPDPAIFLDDLERFALPDtiLTKNIA-ELSGGEKQRISLIRNLQFMPKVLLLDEITSALDE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 521065470 188 ISVADIQNLVHHL-TARGIGVLVTDHnvretlgliDRAYIIHAGEVLT 234
Cdd:PRK10247 171 SNKHNVNEIIHRYvREQNIAVLWVTH---------DKDEINHADKVIT 209
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
40-251 |
1.29e-22 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 93.07 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 40 VSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPvDEGTIEIDGNDVTTMPMYRRSRLGvGYLPQEASIFRGLTVEEnira 119
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAELARHR-AYLSQQQTPPFAMPVFQ---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 120 VLEVHVKDKA---EREQKLNELLEEFHIQKLRKSAAVALSGGERRR-------LEIARALATDPTFMLLDEPFAGVDPIS 189
Cdd:PRK03695 89 YLTLHQPDKTrteAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRvrlaavvLQVWPDINPAGQLLLLDEPMNSLDVAQ 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521065470 190 VADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNPEVRRLY 251
Cdd:PRK03695 169 QAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVF 230
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
18-247 |
2.16e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 93.15 E-value: 2.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 18 YQGTLIARGLTKTYATR-----RVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEG-TIEID---GNDVTTM 88
Cdd:PRK13645 3 FSKDIILDNVSYTYAKKtpfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqTIVGDyaiPANLKKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 89 PMYRRSRLGVGYLPQ--EASIFRGlTVEENIrAVLEVHV-KDKAEREQKLNELLEEFHI-QKLRKSAAVALSGGERRRLE 164
Cdd:PRK13645 83 KEVKRLRKEIGLVFQfpEYQLFQE-TIEKDI-AFGPVNLgENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 165 IARALATDPTFMLLDEPFAGVDPISVADIQNLVHHLTA-RGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVN 243
Cdd:PRK13645 161 LAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKeYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
....
gi 521065470 244 NPEV 247
Cdd:PRK13645 241 NQEL 244
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
22-241 |
2.25e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 92.76 E-value: 2.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTmpmyrrSRLGVGYL 101
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDY------SKRGLLAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 102 PQE-ASIFRG-------LTVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDP 173
Cdd:PRK13638 76 RQQvATVFQDpeqqifyTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521065470 174 TFMLLDEPFAGVDPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDI 241
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV 223
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
36-199 |
2.30e-22 |
|
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: 91.79 E-value: 2.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 36 VVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYR-RSRLGVgyLPQEASIFRGlTVE 114
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDlRSRISI--IPQDPVLFSG-TIR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 115 EN-----------IRAVLE-VHVKDK-AEREQKLNELLEEfhiqklrksAAVALSGGERRRLEIARALATDPTFMLLDEP 181
Cdd:cd03244 96 SNldpfgeysdeeLWQALErVGLKEFvESLPGGLDTVVEE---------GGENLSVGQRQLLCLARALLRKSKILVLDEA 166
|
170
....*....|....*...
gi 521065470 182 FAGVDPISVADIQNLVHH 199
Cdd:cd03244 167 TASVDPETDALIQKTIRE 184
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
34-232 |
3.13e-22 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 95.00 E-value: 3.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 34 RRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVP-VDEGTIEIDGNDVTTMPMYRRSRLGVGYLPQEAS---IFR 109
Cdd:PRK13549 275 IKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQAIAQGIAMVPEDRKrdgIVP 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 110 GLTVEENIR-AVLEVHVK----DKAEREQKLNELLEEFHIQKLRKSAAVA-LSGGERRRLEIARALATDPTFMLLDEPFA 183
Cdd:PRK13549 355 VMGVGKNITlAALDRFTGgsriDDAAELKTILESIQRLKVKTASPELAIArLSGGNQQKAVLAKCLLLNPKILILDEPTR 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 521065470 184 GVDPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEV 232
Cdd:PRK13549 435 GIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
34-232 |
4.09e-22 |
|
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: 94.89 E-value: 4.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 34 RRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVD-EGTIEIDGNDVTTMPMYRRSRLGVGYLPQEAS---IFR 109
Cdd:TIGR02633 273 RKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKrhgIVP 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 110 GLTVEENIR-AVLEVHVK----DKAEREQKLNELLEEFHIQKLRKSAAVA-LSGGERRRLEIARALATDPTFMLLDEPFA 183
Cdd:TIGR02633 353 ILGVGKNITlSVLKSFCFkmriDAAAELQIIGSAIQRLKVKTASPFLPIGrLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 521065470 184 GVDPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEV 232
Cdd:TIGR02633 433 GVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
23-257 |
5.74e-22 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 93.56 E-value: 5.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 23 IARGLTKTYATRRV-----VNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMP---MYRRS 94
Cdd:PRK10070 25 IEQGLSKEQILEKTglslgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaeLREVR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 95 RLGVGYLPQEASIFRGLTVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPT 174
Cdd:PRK10070 105 RKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 175 FMLLDEPFAGVDPISVADIQNLVHHLTARGIGVLV-TDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNPE---VRRL 250
Cdd:PRK10070 185 ILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVfISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAndyVRTF 264
|
....*..
gi 521065470 251 YLGDNFS 257
Cdd:PRK10070 265 FRGVDIS 271
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
37-246 |
5.79e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 92.08 E-value: 5.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 37 VNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYR-RSRLGVGYLPQEASiFRGLTVEE 115
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNlRRKIGMVFQNPDNQ-FVGATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 116 NIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAGVDPISVADIQN 195
Cdd:PRK13642 102 DVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMR 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 521065470 196 LVHHLTAR-GIGVLVTDHNVRETLGlIDRAYIIHAGEVLTHGRANDIVNNPE 246
Cdd:PRK13642 182 VIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSE 232
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
22-225 |
7.20e-22 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 89.86 E-value: 7.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTM-PMYRRSRLGVGY 100
Cdd:PRK13538 2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQrDEYHQDLLYLGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 101 LPqeaSIFRGLTVEENIRAVLEVHvkDKAEREQkLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDE 180
Cdd:PRK13538 82 QP---GIKTELTALENLRFYQRLH--GPGDDEA-LWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 521065470 181 PFAGVDPISVADIQNLV-HHLTARGIGVLVTDHnvreTLGLIDRAY 225
Cdd:PRK13538 156 PFTAIDKQGVARLEALLaQHAEQGGMVILTTHQ----DLPVASDKV 197
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-246 |
1.39e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 90.29 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 25 RGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVD-----EGTIEIDGNDVTTMPMYR-RSRLGV 98
Cdd:PRK14267 8 VNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDPiEVRREV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 99 GYLPQEASIFRGLTVEENIRAVLEVH--VKDKAEREQKLNELLEEF----HIQKLRKSAAVALSGGERRRLEIARALATD 172
Cdd:PRK14267 88 GMVFQYPNPFPHLTIYDNVAIGVKLNglVKSKKELDERVEWALKKAalwdEVKDRLNDYPSNLSGGQRQRLVIARALAMK 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521065470 173 PTFMLLDEPFAGVDPISVADIQNLVHHLTARGIGVLVTdHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNPE 246
Cdd:PRK14267 168 PKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVT-HSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPE 240
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
22-238 |
1.63e-21 |
|
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: 89.80 E-value: 1.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYATRR----VVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRL- 96
Cdd:COG4181 9 IELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARLr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 97 --GVGYLPQEASIFRGLTVEENIRAVLEVhvKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPT 174
Cdd:COG4181 89 arHVGFVFQSFQLLPTLTALENVMLPLEL--AGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 175 FMLLDEPFAGVDPISVADIQNLVHHLTARGiG---VLVTdHNVRetlgLI---DRAYIIHAGEVLTHGRA 238
Cdd:COG4181 167 ILFADEPTGNLDAATGEQIIDLLFELNRER-GttlVLVT-HDPA----LAarcDRVLRLRAGRLVEDTAA 230
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
21-236 |
1.76e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 90.07 E-value: 1.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 21 TLIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTT---CFYMItgLVPVDeGTIEIDGNDVTTMPMYRRSRlG 97
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTllkCFARL--LTPQS-GTVFLGDKPISMLSSRQLAR-R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 98 VGYLPQEASIFRGLTVEENI---RA-VLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDP 173
Cdd:PRK11231 78 LALLPQHHLTPEGITVRELVaygRSpWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521065470 174 TFMLLDEPFAGVDPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHG 236
Cdd:PRK11231 158 PVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQG 220
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
34-236 |
1.77e-21 |
|
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: 89.19 E-value: 1.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 34 RRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRlGVGYLPQEASIFRGlTV 113
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRR-NIGYVPQDVTLFYG-TL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 114 EENIrAVLEVHVKDkaEREQKLNEL--LEEFhIQKLRKSAA-------VALSGGERRRLEIARALATDPTFMLLDEPFAG 184
Cdd:cd03245 95 RDNI-TLGAPLADD--ERILRAAELagVTDF-VNKHPNGLDlqigergRGLSGGQRQAVALARALLNDPPILLLDEPTSA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 521065470 185 VDPISVAdiqNLVHHL--TARGIGVLVTDHNVReTLGLIDRAYIIHAGEVLTHG 236
Cdd:cd03245 171 MDMNSEE---RLKERLrqLLGDKTLIIITHRPS-LLDLVDRIIVMDSGRIVADG 220
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
40-254 |
4.10e-21 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 92.04 E-value: 4.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 40 VSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRLGVGYLP---QEASIFRGLTVEEN 116
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVYLPedrQSSGLYLDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 117 IRAvLEVHVKDKAEREQKLNELLEEFHIQ---KLR--KSAAVALSGGERRRLEIARALATDPTFMLLDEPFAGVDPISVA 191
Cdd:PRK15439 362 VCA-LTHNRRGFWIKPARENAVLERYRRAlniKFNhaEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARN 440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521065470 192 DIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEvLTHGRANDIVNNPEVRRLYLGD 254
Cdd:PRK15439 441 DIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGE-ISGALTGAAINVDTIMRLAFGE 502
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
27-230 |
5.07e-21 |
|
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: 92.38 E-value: 5.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 27 LTKTYA--TRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMpmYRRSRLGVGYLPQE 104
Cdd:TIGR01257 1943 LTKVYSgtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTN--ISDVHQNMGYCPQF 2020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 105 ASIFRGLTVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAG 184
Cdd:TIGR01257 2021 DAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTG 2100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 521065470 185 VDPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAG 230
Cdd:TIGR01257 2101 MDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
25-186 |
5.45e-21 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 90.47 E-value: 5.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 25 RGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDG---NDVTtmPMYRrsrlGVGYL 101
Cdd:PRK11000 7 RNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEkrmNDVP--PAER----GVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 102 PQEASIFRGLTVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEP 181
Cdd:PRK11000 81 FQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
....*
gi 521065470 182 FAGVD 186
Cdd:PRK11000 161 LSNLD 165
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
23-242 |
7.47e-21 |
|
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: 91.02 E-value: 7.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 23 IARGLTKTyatrrvVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEID-GNDVTTM----PMYR-RSRL 96
Cdd:TIGR03269 292 VDRGVVKA------VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMtkpgPDGRgRAKR 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 97 GVGYLPQEASIFRGLTVEENIRAVLEVHVKDKAER-------------EQKLNELLEEFHIQklrksaavaLSGGERRRL 163
Cdd:TIGR03269 366 YIGILHQEYDLYPHRTVLDNLTEAIGLELPDELARmkavitlkmvgfdEEKAEEILDKYPDE---------LSEGERHRV 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 164 EIARALATDPTFMLLDEPFAGVDPISVADIQNLVHHltAR---GIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRAND 240
Cdd:TIGR03269 437 ALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILK--AReemEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEE 514
|
..
gi 521065470 241 IV 242
Cdd:TIGR03269 515 IV 516
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
22-246 |
8.14e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 88.29 E-value: 8.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMIT---GLVP--VDEGTIEIDGNDV---TTMPMYRR 93
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmnDLNPevTITGSIVYNGHNIyspRTDTVDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 94 SRLGVGYlpQEASIFRgLTVEENIRAVLEVH-VKDKAEREQKLNELLEEFHIQKLRK----SAAVALSGGERRRLEIARA 168
Cdd:PRK14239 86 KEIGMVF--QQPNPFP-MSIYENVVYGLRLKgIKDKQVLDEAVEKSLKGASIWDEVKdrlhDSALGLSGGQQQRVCIARV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521065470 169 LATDPTFMLLDEPFAGVDPISVADIQNLVHHLTARGIGVLVTdHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNPE 246
Cdd:PRK14239 163 LATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVT-RSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPK 239
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
36-242 |
1.16e-20 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 87.54 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 36 VVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTM-PMYRRSRlgVGYLPQEASIFRGlTVE 114
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALAdPAWLRRQ--VGVVLQENVLFNR-SIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 115 ENIRAVLEVHVKDKAEREQKLNElLEEFhIQKLRK-------SAAVALSGGERRRLEIARALATDPTFMLLDEPFAGVDP 187
Cdd:cd03252 94 DNIALADPGMSMERVIEAAKLAG-AHDF-ISELPEgydtivgEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDY 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 521065470 188 ISVADIQNLVHHLTArGIGVLVTDHNVrETLGLIDRAYIIHAGEVLTHGRANDIV 242
Cdd:cd03252 172 ESEHAIMRNMHDICA-GRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGSHDELL 224
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
23-245 |
1.26e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 90.53 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 23 IARGLTK-TYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPvDEGTIEIDGndvttMPMYR--------- 92
Cdd:PRK15134 287 IRKGILKrTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDG-----QPLHNlnrrqllpv 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 93 RSRLGVGYLPQEASIFRGLTVEENIRAVLEVHVKD--KAEREQKLNELLEEFHIQ-KLRKSAAVALSGGERRRLEIARAL 169
Cdd:PRK15134 361 RHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPTlsAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARAL 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521065470 170 ATDPTFMLLDEPFAGVDPISVADIQNLVHHLTAR-GIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNP 245
Cdd:PRK15134 441 ILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAP 517
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
22-231 |
1.83e-20 |
|
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: 89.88 E-value: 1.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVD--EGTIEIDGNDVTTMPMYRRSRLGVG 99
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKASNIRDTERAGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 100 YLPQEASIFRGLTVEENIRAVLEVHVK----DKAEREQKLNELLEEFHIQKLRKSAAVA-LSGGERRRLEIARALATDPT 174
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIFLGNEITLPggrmAYNAMYLRAKNLLRELQLDADNVTRPVGdYGGGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 521065470 175 FMLLDEPFAGVDPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGE 231
Cdd:TIGR02633 162 LLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
34-237 |
2.25e-20 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 86.52 E-value: 2.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 34 RRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVT--TMPMYRRSrlgVGYLPQEASIFRGl 111
Cdd:cd03253 14 RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIRevTLDSLRRA---IGVVPQDTVLFND- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 112 TVEENIR-------------AVLEVHVKDKAER-EQKLNELLEEfhiqklrksAAVALSGGERRRLEIARALATDPTFML 177
Cdd:cd03253 90 TIGYNIRygrpdatdeevieAAKAAQIHDKIMRfPDGYDTIVGE---------RGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 178 LDEPFAGVDPISVADIQNLVHHLTARGIGVLVTdHNVRETLGlIDRAYIIHAGEVLTHGR 237
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIA-HRLSTIVN-ADKIIVLKDGRIVERGT 218
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
22-223 |
2.37e-20 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 86.33 E-value: 2.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTY-------ATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGN----DVTTMP- 89
Cdd:COG4778 5 LEVENLSKTFtlhlqggKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQASp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 90 --MYRRSRLGVGYLPQeasiF-----RGLTVEENIRAVLEVHVkDKAEREQKLNELLEEFHI-QKLRKSAAVALSGGERR 161
Cdd:COG4778 85 reILALRRRTIGYVSQ----FlrvipRVSALDVVAEPLLERGV-DREEARARARELLARLNLpERLWDLPPATFSGGEQQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521065470 162 RLEIARALATDPTFMLLDEPFAGVDPISVADIQNLVHHLTARGIGVL--VTDHNVREtlGLIDR 223
Cdd:COG4778 160 RVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgiFHDEEVRE--AVADR 221
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
22-181 |
2.50e-20 |
|
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: 84.04 E-value: 2.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDgndvttmpmyrrSRLGVGYL 101
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG------------STVKIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 102 PQeasifrgltveeniravlevhvkdkaereqklnelleefhiqklrksaavaLSGGERRRLEIARALATDPTFMLLDEP 181
Cdd:cd03221 69 EQ---------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEP 97
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
25-236 |
2.59e-20 |
|
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: 86.44 E-value: 2.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 25 RGLTKTYATR---RVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRLgVGYL 101
Cdd:cd03249 4 KNVSFRYPSRpdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQ-IGLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 102 PQEASIFRGlTVEENIR-------AVLEVHVKDKAEREQKLNELLEEFHIQKLRKsaAVALSGGERRRLEIARALATDPT 174
Cdd:cd03249 83 SQEPVLFDG-TIAENIRygkpdatDEEVEEAAKKANIHDFIMSLPDGYDTLVGER--GSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521065470 175 FMLLDEPFAGVDPISVADIQNLVHHLtARGIGVLVTDHNVrETLGLIDRAYIIHAGEVLTHG 236
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRA-MKGRTTIVIAHRL-STIRNADLIAVLQNGQVVEQG 219
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
37-249 |
3.09e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 87.21 E-value: 3.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 37 VNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMP---MYRRSRLGVGYLPQEASIFRGLTV 113
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRkglMKLRESVGMVFQDPDNQLFSASVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 114 EENIRAVLEVHVKDKaEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAGVDPISVADI 193
Cdd:PRK13636 102 QDVSFGAVNLKLPED-EVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEI 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 521065470 194 QNLVHHLTAR-GIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNPEVRR 249
Cdd:PRK13636 181 MKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEMLR 237
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
19-232 |
3.39e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 86.66 E-value: 3.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 19 QGT-LIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIeIDGN-------DVTTMpM 90
Cdd:PRK11247 9 QGTpLLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTaplaearEDTRL-M 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 91 YRRSRLgvgyLPQEasifrglTVEENIRAVLEVHVKDKAEreqklnELLEEFHIQKLRKSAAVALSGGERRRLEIARALA 170
Cdd:PRK11247 87 FQDARL----LPWK-------KVIDNVGLGLKGQWRDAAL------QALAAVGLADRANEWPAALSGGQKQRVALARALI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521065470 171 TDPTFMLLDEPFAGVDPISVADIQNLVHHLTAR-GIGVLVTDHNVRETLGLIDRAYIIHAGEV 232
Cdd:PRK11247 150 HRPGLLLLDEPLGALDALTRIEMQDLIESLWQQhGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
21-214 |
5.98e-20 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 85.94 E-value: 5.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 21 TLIA-RGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEidgndvttmpmyRRSRLGVG 99
Cdd:PRK09544 3 SLVSlENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK------------RNGKLRIG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 100 YLPQEASI--FRGLTVEENIRAVLEVHVKDkaereqkLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFML 177
Cdd:PRK09544 71 YVPQKLYLdtTLPLTVNRFLRLRPGTKKED-------ILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLV 143
|
170 180 190
....*....|....*....|....*....|....*...
gi 521065470 178 LDEPFAGVDPISVADIQNLVHHL-TARGIGVLVTDHNV 214
Cdd:PRK09544 144 LDEPTQGVDVNGQVALYDLIDQLrRELDCAVLMVSHDL 181
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
25-247 |
6.48e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 86.39 E-value: 6.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 25 RGLTKTY--ATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDE---GTIEIDGNDVTTMPMYR-RSRLGV 98
Cdd:PRK13640 9 KHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWDiREKVGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 99 GYLPQEASiFRGLTVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLL 178
Cdd:PRK13640 89 VFQNPDNQ-FVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIIL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 179 DEPFAGVDPISVADIQNLVHHLTA-RGIGVLVTDHNVRETlGLIDRAYIIHAGEVLTHGRANDIVNNPEV 247
Cdd:PRK13640 168 DESTSMLDPAGKEQILKLIRKLKKkNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVEM 236
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
40-252 |
6.91e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 86.19 E-value: 6.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 40 VSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRLGVGYLPQEASI-FRGLTVEENIR 118
Cdd:PRK13644 21 INLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGIVFQNPETqFVGRTVEEDLA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 119 AVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAGVDPISVADIQNLVH 198
Cdd:PRK13644 101 FGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIK 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 521065470 199 HLTARGIGVLVTDHNVREtLGLIDRAYIIHAGEVLTHGRANDIVNNPEVRRLYL 252
Cdd:PRK13644 181 KLHEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSLQTLGL 233
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
10-180 |
7.13e-20 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 88.48 E-value: 7.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 10 AGAADKSRYQGTLIARGLTKTYA-TRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTM 88
Cdd:PRK13657 323 PGAIDLGRVKGAVEFDDVSFSYDnSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 89 PmyRRS-RLGVGYLPQEASIFrGLTVEENIRA----VLEVHVKDKAEREQKLnelleEFHIQKLRKSAAVA------LSG 157
Cdd:PRK13657 403 T--RASlRRNIAVVFQDAGLF-NRSIEDNIRVgrpdATDEEMRAAAERAQAH-----DFIERKPDGYDTVVgergrqLSG 474
|
170 180
....*....|....*....|...
gi 521065470 158 GERRRLEIARALATDPTFMLLDE 180
Cdd:PRK13657 475 GERQRLAIARALLKDPPILILDE 497
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
5-241 |
7.19e-20 |
|
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: 88.23 E-value: 7.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 5 PGPQAAGAADKSRYQGTLIARGLTKTY--ATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDG 82
Cdd:TIGR02203 314 PPEKDTGTRAIERARGDVEFRNVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDG 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 83 NDVTTMPMyRRSRLGVGYLPQEASIFRGlTVEENIrAVLEVHVKDKAEREQKLNEL-LEEFhIQKLRK-------SAAVA 154
Cdd:TIGR02203 394 HDLADYTL-ASLRRQVALVSQDVVLFND-TIANNI-AYGRTEQADRAEIERALAAAyAQDF-VDKLPLgldtpigENGVL 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 155 LSGGERRRLEIARALATDPTFMLLDEPFAGVDPISVADIQNLVHHLTaRGIGVLVTDHNVrETLGLIDRAYIIHAGEVLT 234
Cdd:TIGR02203 470 LSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLM-QGRTTLVIAHRL-STIEKADRIVVMDDGRIVE 547
|
....*..
gi 521065470 235 HGRANDI 241
Cdd:TIGR02203 548 RGTHNEL 554
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
31-241 |
1.06e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 85.94 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 31 YATRRVVNgVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYR-----RSRLGVGYLPQEA 105
Cdd:PRK13643 17 FASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikpvRKKVGVVFQFPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 106 SIFRGlTVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQK-LRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAG 184
Cdd:PRK13643 96 QLFEE-TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 521065470 185 VDPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDI 241
Cdd:PRK13643 175 LDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDV 231
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
44-239 |
1.19e-19 |
|
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: 84.77 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 44 VRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTtmpmyrrsrlgvgYLPQEASIFRGLTVeeniRAVLEV 123
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-------------YKPQYIKADYEGTV----RDLLSS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 124 HVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAGVDP---ISVAD-IQNLVHH 199
Cdd:cd03237 85 ITKDFYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVeqrLMASKvIRRFAEN 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 521065470 200 LTArgiGVLVTDHNVRETLGLIDRaYIIHAGEVLTHGRAN 239
Cdd:cd03237 165 NEK---TAFVVEHDIIMIDYLADR-LIVFEGEPSVNGVAN 200
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-214 |
1.31e-19 |
|
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: 87.53 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 27 LTKTYatrrvvNGVSLVV-----RRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDgndvttmpmyrrsrLGVGYL 101
Cdd:COG1245 347 LTKSY------GGFSLEVeggeiREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED--------------LKISYK 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 102 PQEASIFRGLTVEENIRAVLEVHVKDKAEREqklnELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEP 181
Cdd:COG1245 407 PQYISPDYDGTVEEFLRSANTDDFGSSYYKT----EIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEP 482
|
170 180 190
....*....|....*....|....*....|....*..
gi 521065470 182 FAGVD---PISVAD-IQNLVhhlTARGIGVLVTDHNV 214
Cdd:COG1245 483 SAHLDveqRLAVAKaIRRFA---ENRGKTAMVVDHDI 516
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
32-236 |
1.52e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 85.45 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 32 ATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDG---NDVTTMPMYRRsrlgVGYLPQEA-SI 107
Cdd:PRK13635 18 AATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGmvlSEETVWDVRRQ----VGMVFQNPdNQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 108 FRGLTVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAGVDP 187
Cdd:PRK13635 94 FVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 521065470 188 ISVADIQNLVHHLTA-RGIGVLVTDHNVRETLGlIDRAYIIHAGEVLTHG 236
Cdd:PRK13635 174 RGRREVLETVRQLKEqKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEG 222
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
25-241 |
1.81e-19 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 86.33 E-value: 1.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 25 RGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTcfymitGLVPVdegtiEIDGNDVTTMP-------MYRRS-RL 96
Cdd:NF000106 17 RGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**R------GALPA-----HV*GPDAGRRPwrf*twcANRRAlRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 97 GVG-YLPQEASIFRGLTVEENIRAV---LEVHVKDKAEREqklNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATD 172
Cdd:NF000106 86 TIG*HRPVR*GRRESFSGRENLYMIgr*LDLSRKDARARA---DELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521065470 173 PTFMLLDEPFAGVDPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDI 241
Cdd:NF000106 163 PAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
36-202 |
1.93e-19 |
|
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: 82.75 E-value: 1.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 36 VVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRLGVgyLPQEASIFRGlTVEE 115
Cdd:cd03247 17 VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISV--LNQRPYLFDT-TLRN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 116 NIravlevhvkdkAEReqklnelleefhiqklrksaavaLSGGERRRLEIARALATDPTFMLLDEPFAGVDPISVADIQN 195
Cdd:cd03247 94 NL-----------GRR-----------------------FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLS 139
|
170 180
....*....|....*....|
gi 521065470 196 LV-------------HHLTA 202
Cdd:cd03247 140 LIfevlkdktliwitHHLTG 159
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
34-239 |
3.67e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 86.12 E-value: 3.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 34 RRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRLGVGYLPQ---EASIFRG 110
Cdd:PRK11288 266 PGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMLCPEdrkAEGIIPV 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 111 LTVEENIRAVLEVH-------VKDKAEREqklnelLEEFHIQKL------RKSAAVALSGGERRRLEIARALATDPTFML 177
Cdd:PRK11288 346 HSVADNINISARRHhlragclINNRWEAE------NADRFIRSLniktpsREQLIMNLSGGNQQKAILGRWLSEDMKVIL 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521065470 178 LDEPFAGVDPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEV---LTHGRAN 239
Cdd:PRK11288 420 LDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIageLAREQAT 484
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
22-245 |
3.92e-19 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 83.82 E-value: 3.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGN-----DVTTMPMYRRSRL 96
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAERRRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 97 GV---GYLPQEA------SIFRGLTVEENIRAVLEVH---VKDKAEreqklnELLEEFHIQKLR-KSAAVALSGGERRRL 163
Cdd:PRK11701 87 LRtewGFVHQHPrdglrmQVSAGGNIGERLMAVGARHygdIRATAG------DWLERVEIDAARiDDLPTTFSGGMQQRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 164 EIARALATDPTFMLLDEPFAGVDpISV-ADIQNLVHHLTAR-GIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDI 241
Cdd:PRK11701 161 QIARNLVTHPRLVFMDEPTGGLD-VSVqARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQV 239
|
....
gi 521065470 242 VNNP 245
Cdd:PRK11701 240 LDDP 243
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-236 |
4.72e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 86.03 E-value: 4.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 4 KPGPQAAGAADKSRYQGTLIARGLTKTY--ATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEID 81
Cdd:PRK11160 321 KPEVTFPTTSTAAADQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLN 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 82 GNDVTTmpmYRRSRL--GVGYLPQEASIFRGlTVEENIRAVlevhvKDKAEREQkLNELLEEFHIQKLRKSAA------- 152
Cdd:PRK11160 401 GQPIAD---YSEAALrqAISVVSQRVHLFSA-TLRDNLLLA-----APNASDEA-LIEVLQQVGLEKLLEDDKglnawlg 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 153 ---VALSGGERRRLEIARALATDPTFMLLDEPFAGVDPISVADI-QNLVHHltARGIGVLVTDHNVREtLGLIDRAYIIH 228
Cdd:PRK11160 471 eggRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQIlELLAEH--AQNKTVLMITHRLTG-LEQFDRICVMD 547
|
....*...
gi 521065470 229 AGEVLTHG 236
Cdd:PRK11160 548 NGQIIEQG 555
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
22-246 |
5.77e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 83.29 E-value: 5.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTT---CFYMITGLVPV--DEGTIEIDGNDVTTM---PMYRR 93
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTilrCFNRLNDLIPGfrVEGKVTFHGKNLYAPdvdPVEVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 94 SRLGVGYL---PQEASIFRGLTVEENIRAvLEVHVKDKAEREQKLNELLEEFHiQKLRKSAaVALSGGERRRLEIARALA 170
Cdd:PRK14243 91 RRIGMVFQkpnPFPKSIYDNIAYGARING-YKGDMDELVERSLRQAALWDEVK-DKLKQSG-LSLSGGQQQRLCIARAIA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 171 TDPTFMLLDEPFAGVDPISVADIQNLVHHLTARGIGVLVTdHNVRETLGLIDRAYIIHA---------GEVLTHGRANDI 241
Cdd:PRK14243 168 VQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVT-HNMQQAARVSDMTAFFNVeltegggryGYLVEFDRTEKI 246
|
....*
gi 521065470 242 VNNPE 246
Cdd:PRK14243 247 FNSPQ 251
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
34-246 |
6.66e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 83.56 E-value: 6.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 34 RRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYR---RSRLGVGYLPQEASIFrg 110
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLsdiRKKVGLVFQYPEYQLF-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 111 ltvEENIRavlevhvKDKAEREQKLNELLEEFHIQKLRKSAAVAL-------------SGGERRRLEIARALATDPTFML 177
Cdd:PRK13637 98 ---EETIE-------KDIAFGPINLGLSEEEIENRVKRAMNIVGLdyedykdkspfelSGGQKRRVAIAGVVAMEPKILI 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 178 LDEPFAGVDPISVADIQNLVHHLTAR-GIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNPE 246
Cdd:PRK13637 168 LDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVE 237
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
25-231 |
7.84e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 85.37 E-value: 7.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 25 RGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVD--EGTIEIDGNDVTTMPMYRRSRLGVGYLP 102
Cdd:PRK13549 9 KNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQASNIRDTERAGIAIIH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 103 QEASIFRGLTVEENI---RAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLD 179
Cdd:PRK13549 89 QELALVKELSVLENIflgNEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 521065470 180 EPFAGVDPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGE 231
Cdd:PRK13549 169 EPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
19-236 |
4.02e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 81.47 E-value: 4.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 19 QGTLIARGLTKTYAT-RRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGndvttMPMYRRSRLG 97
Cdd:PRK15056 4 QAGIVVNDVTVTWRNgHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILG-----QPTRQALQKN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 98 -VGYLPQEASI---FRGLtVEENIRAVLEVHV----KDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARAL 169
Cdd:PRK15056 79 lVAYVPQSEEVdwsFPVL-VEDVVMMGRYGHMgwlrRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521065470 170 ATDPTFMLLDEPFAGVDPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIhAGEVLTHG 236
Cdd:PRK15056 158 AQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMV-KGTVLASG 223
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
29-246 |
5.07e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 81.22 E-value: 5.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 29 KTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIdGNDVTT--------MPMyrRSRLGVGY 100
Cdd:PRK13634 15 KTPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITagkknkklKPL--RKKVGIVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 101 LPQEASIFRGlTVEENIR------AVLEVHVKDKAEREQKLNELLEEFhiqkLRKSAaVALSGGERRRLEIARALATDPT 174
Cdd:PRK13634 92 QFPEHQLFEE-TVEKDICfgpmnfGVSEEDAKQKAREMIELVGLPEEL----LARSP-FELSGGQMRRVAIAGVLAMEPE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521065470 175 FMLLDEPFAGVDPISVADIQNLVHHLTARG--IGVLVTdHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNPE 246
Cdd:PRK13634 166 VLVLDEPTAGLDPKGRKEMMEMFYKLHKEKglTTVLVT-HSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
25-209 |
5.26e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 83.25 E-value: 5.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 25 RGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTmpmyRRSRLGVG----Y 100
Cdd:NF033858 5 EGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD----ARHRRAVCpriaY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 101 LPQeasifrGL--------TVEENIR--AVLEVHvkDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALA 170
Cdd:NF033858 81 MPQ------GLgknlyptlSVFENLDffGRLFGQ--DAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALI 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 521065470 171 TDPTFMLLDEPFAGVDPISVADIQNLVHHLTAR--GIGVLV 209
Cdd:NF033858 153 HDPDLLILDEPTTGVDPLSRRQFWELIDRIRAErpGMSVLV 193
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
17-232 |
5.37e-18 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 80.89 E-value: 5.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 17 RYQGTliarGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTT-----MPMY 91
Cdd:PRK10419 12 HYAHG----GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlnraqRKAF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 92 RRSrlgVGYLPQEA--------SIfrGLTVEENIRAVLEVhvkDKAEREQKLNELLEEF-----HIQKLRKSaavaLSGG 158
Cdd:PRK10419 88 RRD---IQMVFQDSisavnprkTV--REIIREPLRHLLSL---DKAERLARASEMLRAVdlddsVLDKRPPQ----LSGG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521065470 159 ERRRLEIARALATDPTFMLLDEPFAGVDPISVADIQNLVHHLTAR-GIGVLVTDHNVRETLGLIDRAYIIHAGEV 232
Cdd:PRK10419 156 QLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
21-251 |
6.97e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 80.60 E-value: 6.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 21 TLIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRlGVGY 100
Cdd:PRK10575 11 TFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFAR-KVAY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 101 LPQEASIFRGLTVEENIR--------AVLEVHVKDKaereQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATD 172
Cdd:PRK10575 90 LPQQLPAAEGMTVRELVAigrypwhgALGRFGAADR----EKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 173 PTFMLLDEPFAGVDPISVADIQNLVHHLT-ARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNPEVRRLY 251
Cdd:PRK10575 166 SRCLLLDEPTSALDIAHQVDVLALVHRLSqERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIY 245
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-214 |
1.34e-17 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 81.78 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 27 LTKTYatrrvvNGVSLVV-----RRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDgndvttmpmyrrsrLGVGYL 101
Cdd:PRK13409 346 LTKKL------GDFSLEVeggeiYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE--------------LKISYK 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 102 PQEASIFRGLTVEENIRAvlevhVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEP 181
Cdd:PRK13409 406 PQYIKPDYDGTVEDLLRS-----ITDDLGSSYYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEP 480
|
170 180 190
....*....|....*....|....*....|....*..
gi 521065470 182 FAGVD---PISVAD-IQNLVhhlTARGIGVLVTDHNV 214
Cdd:PRK13409 481 SAHLDveqRLAVAKaIRRIA---EEREATALVVDHDI 514
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
36-215 |
1.45e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 79.09 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 36 VVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRL---GVGYLPQEASIFRGLT 112
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELrnqKLGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 113 VEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAGVDPISVAD 192
Cdd:PRK11629 104 ALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADS 183
|
170 180
....*....|....*....|....
gi 521065470 193 IQNLVHHLTAR-GIGVLVTDHNVR 215
Cdd:PRK11629 184 IFQLLGELNRLqGTAFLVVTHDLQ 207
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
33-246 |
2.30e-17 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 80.88 E-value: 2.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 33 TRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVP----VDEGTIEIDGNDVTTMPMYRRSRLgvgylpqeasif 108
Cdd:COG4172 22 TVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPdpaaHPSGSILFDGQDLLGLSERELRRI------------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 109 RG-----------------LTVEENIRAVLEVHVK-DKAEREQKLNELLEEFHIQKLRKSAAV---ALSGGERRRLEIAR 167
Cdd:COG4172 90 RGnriamifqepmtslnplHTIGKQIAEVLRLHRGlSGAAARARALELLERVGIPDPERRLDAyphQLSGGQRQRVMIAM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 168 ALATDPTFMLLDEPFAGVDPISVADIQNLVHHLTAR-GIGVLVTDHNvretLGLI----DRAYIIHAGEVLTHGRANDIV 242
Cdd:COG4172 170 ALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHD----LGVVrrfaDRVAVMRQGEIVEQGPTAELF 245
|
....
gi 521065470 243 NNPE 246
Cdd:COG4172 246 AAPQ 249
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-246 |
2.79e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 78.98 E-value: 2.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 10 AGAADKSRYQGTLIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPV-----DEGTIEIDGND 84
Cdd:PRK14271 10 SGAADVDAAAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 85 VTTMPMYRRSRLGVGYLPQEASIFRgLTVEENIRAVLEVH--VKDKAER---EQKLNELLEEFHIQKLRKSAAVALSGGE 159
Cdd:PRK14271 90 IFNYRDVLEFRRRVGMLFQRPNPFP-MSIMDNVLAGVRAHklVPRKEFRgvaQARLTEVGLWDAVKDRLSDSPFRLSGGQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 160 RRRLEIARALATDPTFMLLDEPFAGVDPISVADIQNLVHHLTARgIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRAN 239
Cdd:PRK14271 169 QQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTE 247
|
....*..
gi 521065470 240 DIVNNPE 246
Cdd:PRK14271 248 QLFSSPK 254
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
25-186 |
3.62e-17 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 79.50 E-value: 3.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 25 RGLTKTYATR-RVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTM-PMYRrsrlGVGYLP 102
Cdd:PRK11650 7 QAVRKSYDGKtQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELePADR----DIAMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 103 QEASIFRGLTVEENIRAVLEVHVKDKAEREQKLNE---LLEefhIQKL--RKSAavALSGGERRRLEIARALATDPTFML 177
Cdd:PRK11650 83 QNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEaarILE---LEPLldRKPR--ELSGGQRQRVAMGRAIVREPAVFL 157
|
....*....
gi 521065470 178 LDEPFAGVD 186
Cdd:PRK11650 158 FDEPLSNLD 166
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
37-232 |
7.34e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 79.66 E-value: 7.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 37 VNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRLGVGYLPQEAS---IFRGLTV 113
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIVYISEDRKrdgLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 114 EENIR-AVLE------VHVKDKAEReQKLNELLEEFHIQKLRKSAAVA-LSGGERRRLEIARALATDPTFMLLDEPFAGV 185
Cdd:PRK10762 348 KENMSlTALRyfsragGSLKHADEQ-QAVSDFIRLFNIKTPSMEQAIGlLSGGNQQKVAIARGLMTRPKVLILDEPTRGV 426
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 521065470 186 DPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEV 232
Cdd:PRK10762 427 DVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
19-237 |
1.14e-16 |
|
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: 76.36 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 19 QGTLIARGLTKTYATR---RVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNdvtTMPMYRRSR 95
Cdd:cd03248 9 KGIVKFQNVTFAYPTRpdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGK---PISQYEHKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 96 L--GVGYLPQEASIFRGlTVEENIRAVLE-------VHVKDKAEREQKLNELLEEFHIQKLRKSAavALSGGERRRLEIA 166
Cdd:cd03248 86 LhsKVSLVGQEPVLFAR-SLQDNIAYGLQscsfecvKEAAQKAHAHSFISELASGYDTEVGEKGS--QLSGGQKQRVAIA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521065470 167 RALATDPTFMLLDEPFAGVDPISVADIQNLVHHLTARGIgVLVTDHNvretLGLIDRAYIIhagEVLTHGR 237
Cdd:cd03248 163 RALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRT-VLVIAHR----LSTVERADQI---LVLDGGR 225
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
37-232 |
1.37e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 77.08 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 37 VNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRLgVGYLPQEA-SIFRGLTVEE 115
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHK-IGMVFQNPdNQFVGATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 116 NIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAGVDPISVADIQN 195
Cdd:PRK13650 102 DVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIK 181
|
170 180 190
....*....|....*....|....*....|....*...
gi 521065470 196 LVHHLTAR-GIGVLVTDHNVREtLGLIDRAYIIHAGEV 232
Cdd:PRK13650 182 TIKGIRDDyQMTVISITHDLDE-VALSDRVLVMKNGQV 218
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
37-246 |
1.45e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 77.10 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 37 VNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTI-----EIDGNDVTTMpmyrRSRLGVGYLPQEASiFRGL 111
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqAITDDNFEKL----RKHIGIVFQNPDNQ-FVGS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 112 TVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAGVDPISVA 191
Cdd:PRK13648 100 IVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQ 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 521065470 192 DIQNLVHHLTA-RGIGVLVTDHNVRETLGlIDRAYIIHAGEVLTHGRANDIVNNPE 246
Cdd:PRK13648 180 NLLDLVRKVKSeHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAE 234
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
27-223 |
2.43e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 75.68 E-value: 2.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 27 LTKTY-ATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTM-----PMYRRSrlgVGY 100
Cdd:PRK10908 7 VSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLknrevPFLRRQ---IGM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 101 LPQEASIFRGLTVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDE 180
Cdd:PRK10908 84 IFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 521065470 181 PFAGVDPISVADIQNLVHHLTARGIGVLVTDHNVretlGLIDR 223
Cdd:PRK10908 164 PTGNLDDALSEGILRLFEEFNRVGVTVLMATHDI----GLISR 202
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
40-252 |
2.82e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 76.41 E-value: 2.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 40 VSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYR-----RSRLGVGYLPQEASIFRGLTVE 114
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnlkklRKKVSLVFQFPEAQLFENTVLK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 115 ENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAGVDPISVADIQ 194
Cdd:PRK13641 106 DVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMM 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 521065470 195 NLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNPE-VRRLYL 252
Cdd:PRK13641 186 QLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEwLKKHYL 244
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
36-231 |
3.52e-16 |
|
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: 74.43 E-value: 3.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 36 VVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGndvttmpmyrrsrlGVGYLPQEASIFRGlTVEE 115
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--------------SIAYVSQEPWIQNG-TIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 116 NIravlevhVKDKAEREQKLNELLE----EFHIQKLRK-------SAAVALSGGERRRLEIARALATDPTFMLLDEPFAG 184
Cdd:cd03250 85 NI-------LFGKPFDEERYEKVIKacalEPDLEILPDgdlteigEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 521065470 185 VDPISVADI-QNLV-HHLTARGIGVLVTdHNVrETLGLIDRAYIIHAGE 231
Cdd:cd03250 158 VDAHVGRHIfENCIlGLLLNNKTRILVT-HQL-QLLPHADQIVVLDNGR 204
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
33-212 |
4.73e-16 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 73.82 E-value: 4.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 33 TRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMI-----TGLVpvdEGTIEIDGNDVTtmPMYRRSrlgVGYLPQEASI 107
Cdd:cd03232 19 KRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLagrktAGVI---TGEILINGRPLD--KNFQRS---TGYVEQQDVH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 108 FRGLTVEENIRavlevhvkdkaereqklnelleeFHiQKLRksaavALSGGERRRLEIARALATDPTFMLLDEPFAGVDP 187
Cdd:cd03232 91 SPNLTVREALR-----------------------FS-ALLR-----GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
170 180
....*....|....*....|....*
gi 521065470 188 ISVADIQNLVHHLTARGIGVLVTDH 212
Cdd:cd03232 142 QAAYNIVRFLKKLADSGQAILCTIH 166
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
24-181 |
6.44e-16 |
|
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: 76.90 E-value: 6.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 24 ARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIdGNDVTtmpmyrrsrlgVGYLPQ 103
Cdd:TIGR03719 325 AENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK-----------LAYVDQ 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 104 E-ASIFRGLTVEENIRAVLEVHVKDKaeREQKLNELLEEFHI-----QKLRKSaavaLSGGERRRLEIARALATDPTFML 177
Cdd:TIGR03719 393 SrDALDPNKTVWEEISGGLDIIKLGK--REIPSRAYVGRFNFkgsdqQKKVGQ----LSGGERNRVHLAKTLKSGGNVLL 466
|
....
gi 521065470 178 LDEP 181
Cdd:TIGR03719 467 LDEP 470
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
52-248 |
7.25e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 76.07 E-value: 7.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 52 LLGPNGAGKTTCFYMITGLVPVDEGTIEIDG---NDVTT---MPMYRRsrlGVGYLPQEASIFRGLTVEENIRAVLevhv 125
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAEKgicLPPEKR---RIGYVFQDARLFPHYKVRGNLRYGM---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 126 kdKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAGVD--------PIsvadIQNLV 197
Cdd:PRK11144 102 --AKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlprkrellPY----LERLA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 521065470 198 HHLTargIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNPEVR 248
Cdd:PRK11144 176 REIN---IPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAMR 223
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
36-250 |
7.83e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 75.12 E-value: 7.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 36 VVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRLGVGYLPQE------ASIfr 109
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIRNKAGMVFQNpdnqivATI-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 110 gltVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAGVDPIS 189
Cdd:PRK13633 103 ---VEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSG 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521065470 190 VADIQNLVHHLTAR-GIGVLVTDHNVRETLGlIDRAYIIHAGEVLTHGRANDIVnnPEVRRL 250
Cdd:PRK13633 180 RREVVNTIKELNKKyGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF--KEVEMM 238
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
22-245 |
1.23e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 74.44 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYATR---------RVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPM-Y 91
Cdd:PRK15112 5 LEVRNLSKTFRYRtgwfrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYsY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 92 RRSRLGVGYlpQEASifRGLTVEENIRAVLEVHVK-----DKAEREQKLNELLEEFhiqKLRKSAAV----ALSGGERRR 162
Cdd:PRK15112 85 RSQRIRMIF--QDPS--TSLNPRQRISQILDFPLRlntdlEPEQREKQIIETLRQV---GLLPDHASyyphMLAPGQKQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 163 LEIARALATDPTFMLLDEPFAGVDPISVADIQNLVHHLTAR-GIG-VLVTDHnvretLGLI----DRAYIIHAGEVLTHG 236
Cdd:PRK15112 158 LGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISyIYVTQH-----LGMMkhisDQVLVMHQGEVVERG 232
|
....*....
gi 521065470 237 RANDIVNNP 245
Cdd:PRK15112 233 STADVLASP 241
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
27-251 |
1.86e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 73.87 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 27 LTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRLgVGYLPQEAS 106
Cdd:PRK10253 13 LTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARR-IGLLAQNAT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 107 IFRGLTVEENIRAVLEVH----VKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPF 182
Cdd:PRK10253 92 TPGDITVQELVARGRYPHqplfTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 183 AGVDPISVADIQNLVHHLT-ARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNPEVRRLY 251
Cdd:PRK10253 172 TWLDISHQIDLLELLSELNrEKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIY 241
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
26-210 |
2.10e-15 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 75.36 E-value: 2.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 26 GLTKTY-ATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGlvpVDEgtiEIDGnDVTTMPMYRrsrlgVGYLPQE 104
Cdd:TIGR03719 9 RVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG---VDK---DFNG-EARPQPGIK-----VGYLPQE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 105 ASIFRGLTVEEN-------IRAVL----EVHVK--------DKAEREQ-KLNELLE-----------EFHIQKLR---KS 150
Cdd:TIGR03719 77 PQLDPTKTVRENveegvaeIKDALdrfnEISAKyaepdadfDKLAAEQaELQEIIDaadawdldsqlEIAMDALRcppWD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521065470 151 AAVA-LSGGERRRLEIARALATDPTFMLLDEPFAGVDPISVADIQNLVHHLTarGIGVLVT 210
Cdd:TIGR03719 157 ADVTkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYP--GTVVAVT 215
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
22-218 |
2.20e-15 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 72.57 E-value: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMpmyRRSRLgVGYL 101
Cdd:PRK13543 12 LAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRG---DRSRF-MAYL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 102 PQEASIFRGLTVEENIRAVLEVHvkdkAEREQKL-NELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDE 180
Cdd:PRK13543 88 GHLPGLKADLSTLENLHFLCGLH----GRRAKQMpGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDE 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 521065470 181 PFAGVDPISVADIQNLVH-HLTARGiGVLVTDHNVRETL 218
Cdd:PRK13543 164 PYANLDLEGITLVNRMISaHLRGGG-AALVTTHGAYAAP 201
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
36-186 |
2.62e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 72.89 E-value: 2.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 36 VVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRL---GVGYLPQEASIFRGLT 112
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLrakHVGFVFQSFMLIPTLN 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521065470 113 VEENIRavLEVHVKDKAEREQKLN--ELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAGVD 186
Cdd:PRK10584 105 ALENVE--LPALLRGESSRQSRNGakALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
19-218 |
2.93e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 74.84 E-value: 2.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 19 QGTLIARGLT-KTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEI-DGNDVTTMPmyRRSRL 96
Cdd:COG4178 360 DGALALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLFLP--QRPYL 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 97 GVGYL------PQEASIFRgltvEENIRAVLE-VHVKDKAEReqklneLLEEFHIQKLrksaavaLSGGERRRLEIARAL 169
Cdd:COG4178 438 PLGTLreallyPATAEAFS----DAELREALEaVGLGHLAER------LDEEADWDQV-------LSLGEQQRLAFARLL 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 521065470 170 ATDPTFMLLDEPFAGVDPISVADI-QNLVHHLtaRGIGVLVTDHnvRETL 218
Cdd:COG4178 501 LHKPDWLFLDEATSALDEENEAALyQLLREEL--PGTTVISVGH--RSTL 546
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
27-243 |
3.46e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 74.45 E-value: 3.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 27 LTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGL--------------------------------VPVD 74
Cdd:TIGR03269 6 LTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqyeptsgriiyhvalcekcgyverpskvgepCPVC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 75 EGTIEIDGNDVTTM--PMYRRSRLGVGYLPQEA-SIFRGLTVEEN-IRAVLEVHVKDKaEREQKLNELLEEFHIQKLRKS 150
Cdd:TIGR03269 86 GGTLEPEEVDFWNLsdKLRRRIRKRIAIMLQRTfALYGDDTVLDNvLEALEEIGYEGK-EAVGRAVDLIEMVQLSHRITH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 151 AAVALSGGERRRLEIARALATDPTFMLLDEPFAGVDPISVadiqNLVHH-----LTARGIGVLVTDHNVRETLGLIDRAY 225
Cdd:TIGR03269 165 IARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTA----KLVHNaleeaVKASGISMVLTSHWPEVIEDLSDKAI 240
|
250
....*....|....*...
gi 521065470 226 IIHAGEVLTHGRANDIVN 243
Cdd:TIGR03269 241 WLENGEIKEEGTPDEVVA 258
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
30-186 |
5.32e-15 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 74.37 E-value: 5.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 30 TYATR---RVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMP-MYRRSRlgVGYLPQEA 105
Cdd:TIGR00958 487 SYPNRpdvPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDhHYLHRQ--VALVGQEP 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 106 SIFRGlTVEENIRAVLevhvkDKAEREQKLNELLEEF---HIQKLRKS-------AAVALSGGERRRLEIARALATDPTF 175
Cdd:TIGR00958 565 VLFSG-SVRENIAYGL-----TDTPDEEIMAAAKAANahdFIMEFPNGydtevgeKGSQLSGGQKQRIAIARALVRKPRV 638
|
170
....*....|.
gi 521065470 176 MLLDEPFAGVD 186
Cdd:TIGR00958 639 LILDEATSALD 649
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
36-247 |
5.65e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 72.96 E-value: 5.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 36 VVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDgnDVTTMPMYRRSRLGVGYLPQEASIFRGL---- 111
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVG--DIYIGDKKNNHELITNPYSKKIKNFKELrrrv 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 112 --------------TVEENIR---AVLEVHVKDKAEREQK-LNEL-LEEFHIQKlrksAAVALSGGERRRLEIARALATD 172
Cdd:PRK13631 119 smvfqfpeyqlfkdTIEKDIMfgpVALGVKKSEAKKLAKFyLNKMgLDDSYLER----SPFGLSGGQKRRVAIAGILAIQ 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521065470 173 PTFMLLDEPFAGVDPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNPEV 247
Cdd:PRK13631 195 PEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQHI 269
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-218 |
9.04e-15 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 73.79 E-value: 9.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 19 QGTLIARGLTKTY--ATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVdEGTIEIDGN--DVTTMPMYRRS 94
Cdd:TIGR01271 1215 GGQMDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST-EGEIQIDGVswNSVTLQTWRKA 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 95 rlgVGYLPQEASIFRGL-----------TVEENIRAVLEVHVKDKAER-EQKLNELLEEfhiqklrksAAVALSGGERRR 162
Cdd:TIGR01271 1294 ---FGVIPQKVFIFSGTfrknldpyeqwSDEEIWKVAEEVGLKSVIEQfPDKLDFVLVD---------GGYVLSNGHKQL 1361
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 521065470 163 LEIARALATDPTFMLLDEPFAGVDPISVADIQNLVHHlTARGIGVLVTDHNVRETL 218
Cdd:TIGR01271 1362 MCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQ-SFSNCTVILSEHRVEALL 1416
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
20-218 |
1.32e-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: 71.42 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 20 GTLIARGLTKTY--ATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVdEGTIEIDGNDVTTMPMyRRSRLG 97
Cdd:cd03289 1 GQMTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSVPL-QKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 98 VGYLPQEASIFRGltveeNIRAVLEVHVKDKAER------EQKLNELLEEFHIQ---KLRKSAAVaLSGGERRRLEIARA 168
Cdd:cd03289 79 FGVIPQKVFIFSG-----TFRKNLDPYGKWSDEEiwkvaeEVGLKSVIEQFPGQldfVLVDGGCV-LSHGHKQLMCLARS 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 521065470 169 LATDPTFMLLDEPFAGVDPISVADIQNLVHHLTArGIGVLVTDHNVRETL 218
Cdd:cd03289 153 VLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFA-DCTVILSEHRIEAML 201
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
36-244 |
1.60e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 73.09 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 36 VVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRLgVGYLPQEASIFRGlTVEE 115
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRV-LSIIPQSPVLFSG-TVRF 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 116 NIRAVLEvhvkdkaEREQKLNELLEEFHIQKLRKSAAVAL-----------SGGERRRLEIARALATDPTFMLLDEPFAG 184
Cdd:PLN03232 1329 NIDPFSE-------HNDADLWEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATAS 1401
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 185 VDPISVADIQNLVHHlTARGIGVLVTDHNVrETLGLIDRAYIIHAGEVLTHGRANDIVNN 244
Cdd:PLN03232 1402 VDVRTDSLIQRTIRE-EFKSCTMLVIAHRL-NTIIDCDKILVLSSGQVLEYDSPQELLSR 1459
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
34-232 |
1.65e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.51 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 34 RRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRLGVGYLPQ---EASIFRG 110
Cdd:PRK09700 276 RKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYITEsrrDNGFFPN 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 111 LTVEENIrAVLE-------------VHVKDKAEREQKLNELLEefhiqklRKSAAV-----ALSGGERRRLEIARALATD 172
Cdd:PRK09700 356 FSIAQNM-AISRslkdggykgamglFHEVDEQRTAENQRELLA-------LKCHSVnqnitELSGGNQQKVLISKWLCCC 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 173 PTFMLLDEPFAGVDPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEV 232
Cdd:PRK09700 428 PEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
36-233 |
2.20e-14 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 72.45 E-value: 2.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 36 VVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTM---PMYRRSRLGVGYLPQEASIFRGLT 112
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLdadALAQLRREHFGFIFQRYHLLSHLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 113 VEENIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAGVDPISVAD 192
Cdd:PRK10535 103 AAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEE 182
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 521065470 193 IQNLVHHLTARGIGVLVTDHNvRETLGLIDRAYIIHAGEVL 233
Cdd:PRK10535 183 VMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEIV 222
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
34-241 |
2.96e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 70.54 E-value: 2.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 34 RRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYR-----RSRLGVGYLPQEASIF 108
Cdd:PRK13649 20 GRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdikqiRKKVGLVFQFPESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 109 RGlTVEENIRAVLEVHVKDKAEREQKLNELLEEFHI-QKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAGVDP 187
Cdd:PRK13649 100 EE-TVLKDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 521065470 188 ISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDI 241
Cdd:PRK13649 179 KGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
25-191 |
3.11e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 71.69 E-value: 3.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 25 RGLTKTYATRRVV-NGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGlvpVDEgtiEIDGnDVTTMPMYRrsrlgVGYLPQ 103
Cdd:PRK11819 10 NRVSKVVPPKKQIlKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG---VDK---EFEG-EARPAPGIK-----VGYLPQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 104 EASIFRGLTVEENIR-AVLEvhVKDK-----------AEREQKLNELLEEF-----HIQK----------------LR-- 148
Cdd:PRK11819 78 EPQLDPEKTVRENVEeGVAE--VKAAldrfneiyaayAEPDADFDALAAEQgelqeIIDAadawdldsqleiamdaLRcp 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 521065470 149 -KSAAVA-LSGGERRRLEIARALATDPTFMLLDEPFAGVDPISVA 191
Cdd:PRK11819 156 pWDAKVTkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVA 200
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
31-212 |
3.54e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 69.21 E-value: 3.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 31 YATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTT-MPMYRRSRLGVGYlpqEASIFR 109
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKdLCTYQKQLCFVGH---RSGINP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 110 GLTVEENirAVLEVHVKDKAereQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAGVDPIS 189
Cdd:PRK13540 88 YLTLREN--CLYDIHFSPGA---VGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS 162
|
170 180
....*....|....*....|...
gi 521065470 190 VADIQNLVHHLTARGIGVLVTDH 212
Cdd:PRK13540 163 LLTIITKIQEHRAKGGAVLLTSH 185
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
40-245 |
3.69e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 71.41 E-value: 3.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 40 VSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVdEGTIEIDGNDVTTMPM--YRRSrlgVGYLPQEASIFRGlTVEENI 117
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIELRELDPesWRKH---LSWVGQNPQLPHG-TLRDNV 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 118 RavlevhVKDKAEREQKLNELLE-----EFhIQKLR-------KSAAVALSGGERRRLEIARALATDPTFMLLDEPFAGV 185
Cdd:PRK11174 444 L------LGNPDASDEQLQQALEnawvsEF-LPLLPqgldtpiGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASL 516
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 186 DPISVADIQNLVHHLTARGIGVLVTdHNVrETLGLIDRAYIIHAGEVLTHGRANDIVNNP 245
Cdd:PRK11174 517 DAHSEQLVMQALNAASRRQTTLMVT-HQL-EDLAQWDQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
24-181 |
3.89e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 71.30 E-value: 3.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 24 ARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIdGNDVTtmpmyrrsrlgVGYLPQ 103
Cdd:PRK11819 327 AENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVK-----------LAYVDQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 104 E-ASIFRGLTVEENI---RAVLEVHVKDKAER-----------EQklnelleefhiQKLRKSaavaLSGGERRRLEIARA 168
Cdd:PRK11819 395 SrDALDPNKTVWEEIsggLDIIKVGNREIPSRayvgrfnfkggDQ-----------QKKVGV----LSGGERNRLHLAKT 459
|
170
....*....|...
gi 521065470 169 LATDPTFMLLDEP 181
Cdd:PRK11819 460 LKQGGNVLLLDEP 472
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
35-245 |
4.21e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 70.54 E-value: 4.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 35 RVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVP----VDEGTIEIDGNDVTTMPMYRRSRLgVGylPQEASIFRG 110
Cdd:PRK11022 21 RAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQRISEKERRNL-VG--AEVAMIFQD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 111 --------LTVEENIRAVLEVHVK-DKAEREQKLNELLEEFHIQKLRKSAAV---ALSGGERRRLEIARALATDPTFMLL 178
Cdd:PRK11022 98 pmtslnpcYTVGFQIMEAIKVHQGgNKKTRRQRAIDLLNQVGIPDPASRLDVyphQLSGGMSQRVMIAMAIACRPKLLIA 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521065470 179 DEPFAGVDPISVADIQNLVHHLTAR-GIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNP 245
Cdd:PRK11022 178 DEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAP 245
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
26-231 |
4.58e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.19 E-value: 4.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 26 GLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVT-TMPmyRRSRL-GVGYLPQ 103
Cdd:PRK10762 9 GIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGP--KSSQEaGIGIIHQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 104 EASIFRGLTVEENIRAVLEVHVK----DKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLD 179
Cdd:PRK10762 87 ELNLIPQLTIAENIFLGREFVNRfgriDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 521065470 180 EPFAGVDPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGE 231
Cdd:PRK10762 167 EPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
11-230 |
5.51e-14 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 71.20 E-value: 5.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 11 GAADKSRYQGTLIARGLTKTYATRRV--VNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTm 88
Cdd:PRK11176 331 GKRVIERAKGDIEFRNVTFTYPGKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRD- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 89 pmYRRSRL--GVGYLPQEASIFRGlTVEENIR-AVLEVHVKDKAEREQKLNELLEefHIQKLRK-------SAAVALSGG 158
Cdd:PRK11176 410 --YTLASLrnQVALVSQNVHLFND-TIANNIAyARTEQYSREQIEEAARMAYAMD--FINKMDNgldtvigENGVLLSGG 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521065470 159 ERRRLEIARALATDPTFMLLDEPFAGVDPISVADIQNLVHHLTaRGIGVLVTDH------NVRETLgLIDRAYIIHAG 230
Cdd:PRK11176 485 QRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQ-KNRTSLVIAHrlstieKADEIL-VVEDGEIVERG 560
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
28-212 |
5.60e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 71.06 E-value: 5.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 28 TKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVD--EGTIEIDGNDVTTMPMYRrsrlgVGYLPQEA 105
Cdd:PLN03211 75 TRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQILKR-----TGFVTQDD 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 106 SIFRGLTVEENIRAVLEVHVKDKAEREQKL---NELLEEFHIQK-----LRKSAAVALSGGERRRLEIARALATDPTFML 177
Cdd:PLN03211 150 ILYPHLTVRETLVFCSLLRLPKSLTKQEKIlvaESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLI 229
|
170 180 190
....*....|....*....|....*....|....*
gi 521065470 178 LDEPFAGVDPISVADIQNLVHHLTARGIGVLVTDH 212
Cdd:PLN03211 230 LDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMH 264
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
36-257 |
6.69e-14 |
|
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: 69.50 E-value: 6.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 36 VVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNdvttmpmyrrsrlgVGYLPQEASIFRGlTVEE 115
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--------------ISFSSQFSWIMPG-TIKE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 116 NIRAVLEV------HVKDKAEREQKLNELLEEFHIqkLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAGVDPIS 189
Cdd:cd03291 117 NIIFGVSYdeyrykSVVKACQLEEDITKFPEKDNT--VLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521065470 190 VADI-QNLVHHLTARGIGVLVTdhNVRETLGLIDRAYIIHAGEVLTHGRANDIVN-NPEVRRLYLG----DNFS 257
Cdd:cd03291 195 EKEIfESCVCKLMANKTRILVT--SKMEHLKKADKILILHEGSSYFYGTFSELQSlRPDFSSKLMGydtfDQFS 266
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
22-245 |
7.05e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 69.99 E-value: 7.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYATRR----------VVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMP-- 89
Cdd:PRK11308 6 LQAIDLKKHYPVKRglfkperlvkALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 90 --MYRRSRLGVGYLPQEASIFRGLTVEENIRAVLEVHVK-DKAEREQKLNELLeefhiqklrksAAVAL----------- 155
Cdd:PRK11308 86 aqKLLRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSlSAAERREKALAMM-----------AKVGLrpehydryphm 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 156 -SGGERRRLEIARALATDPTFMLLDEPFAGVDpISV-ADIQNLVHHLTAR-GIGVLVTDHNVRETLGLIDRAYIIHAGEV 232
Cdd:PRK11308 155 fSGGQRQRIAIARALMLDPDVVVADEPVSALD-VSVqAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGRC 233
|
250
....*....|...
gi 521065470 233 LTHGRANDIVNNP 245
Cdd:PRK11308 234 VEKGTKEQIFNNP 246
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
37-245 |
8.43e-14 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 69.75 E-value: 8.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 37 VNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVD---EGTIEIDGNDVTTMPMYRRSRLGVgylPQEASIFRG--- 110
Cdd:PRK09473 32 VNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKELNKLRA---EQISMIFQDpmt 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 111 -----LTVEENIRAVLEVHVK-DKAEREQKLNELLEEFHIQKLRKSAAV---ALSGGERRRLEIARALATDPTFMLLDEP 181
Cdd:PRK09473 109 slnpyMRVGEQLMEVLMLHKGmSKAEAFEESVRMLDAVKMPEARKRMKMyphEFSGGMRQRVMIAMALLCRPKLLIADEP 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521065470 182 FAGVDPISVADIQNLVHHL-----TArgigVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNP 245
Cdd:PRK09473 189 TTALDVTVQAQIMTLLNELkrefnTA----IIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQP 253
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
25-223 |
1.04e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 70.33 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 25 RGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTtmpmYRRSR----LGVGY 100
Cdd:PRK11288 8 DGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMR----FASTTaalaAGVAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 101 LPQEASIFRGLTVEENI-------RAVLeVHVKD-KAEREQKLNELLEEFHIQ-KLRKsaavaLSGGERRRLEIARALAT 171
Cdd:PRK11288 84 IYQELHLVPEMTVAENLylgqlphKGGI-VNRRLlNYEAREQLEHLGVDIDPDtPLKY-----LSIGQRQMVEIAKALAR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 521065470 172 DPTFMLLDEPfagVDPISVADIQNL---VHHLTARGIGVLVTDHNVRETLGLIDR 223
Cdd:PRK11288 158 NARVIAFDEP---TSSLSAREIEQLfrvIRELRAEGRVILYVSHRMEEIFALCDA 209
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
21-245 |
1.29e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 68.57 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 21 TLIARGLTkTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKT-TCFYMItGLVP----VDEGTIEIDGndvttmpmyrrsr 95
Cdd:PRK10418 4 QIELRNIA-LQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAAL-GILPagvrQTAGRVLLDG------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 96 lgvgyLPQEASIFRGLTVE---ENIRAV------LEVHVKD------KAEREQKLNELLEEFHI---QKLRKSAAVALSG 157
Cdd:PRK10418 69 -----KPVAPCALRGRKIAtimQNPRSAfnplhtMHTHAREtclalgKPADDATLTAALEAVGLenaARVLKLYPFEMSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 158 GERRRLEIARALATDPTFMLLDEPFAGVDPISVADIQNLVHHLTA-RGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHG 236
Cdd:PRK10418 144 GMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQkRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQG 223
|
....*....
gi 521065470 237 RANDIVNNP 245
Cdd:PRK10418 224 DVETLFNAP 232
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
36-257 |
1.58e-13 |
|
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: 69.94 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 36 VVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNdvttmpmyrrsrlgVGYLPQEASIFRGlTVEE 115
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR--------------ISFSPQTSWIMPG-TIKD 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 116 NIRAVLE------VHVKDKAEREQKLNELLEEFHIqkLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAGVDPIS 189
Cdd:TIGR01271 506 NIIFGLSydeyryTSVIKACQLEEDIALFPEKDKT--VLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521065470 190 VADI-QNLVHHLTARGIGVLVTDHnvRETLGLIDRAYIIHAGEVLTHGRANDIVN-NPEVRRLYLG----DNFS 257
Cdd:TIGR01271 584 EKEIfESCLCKLMSNKTRILVTSK--LEHLKKADKILLLHEGVCYFYGTFSELQAkRPDFSSLLLGleafDNFS 655
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
20-197 |
1.70e-13 |
|
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: 69.77 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 20 GTLIARGLTKTYA-TRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRLgV 98
Cdd:TIGR01193 472 GDIVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQF-I 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 99 GYLPQEASIF-------------RGLTVEENIRAVLEVHVKDKAEREQK--LNELLEEfhiqklrksaAVALSGGERRRL 163
Cdd:TIGR01193 551 NYLPQEPYIFsgsilenlllgakENVSQDEIWAACEIAEIKDDIENMPLgyQTELSEE----------GSSISGGQKQRI 620
|
170 180 190
....*....|....*....|....*....|....*
gi 521065470 164 EIARALATDPTFMLLDEPFAGVDPISVADI-QNLV 197
Cdd:TIGR01193 621 ALARALLTDSKVLILDESTSNLDTITEKKIvNNLL 655
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
33-246 |
2.60e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 68.96 E-value: 2.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 33 TRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVD-----EGTIEIDGNDV-----TTMPMYRRSRLGVGYLP 102
Cdd:PRK15134 21 VRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLlhaseQTLRGVRGNKIAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 103 QEASIFRGLTVEENIRAVLEVH--VKDKAEREQKLNeLLEEFHIQKLRKSAAV---ALSGGERRRLEIARALATDPTFML 177
Cdd:PRK15134 101 PMVSLNPLHTLEKQLYEVLSLHrgMRREAARGEILN-CLDRVGIRQAAKRLTDyphQLSGGERQRVMIAMALLTRPELLI 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 178 LDEPFAGVDPISVADIQNLVHHLTAR-GIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNPE 246
Cdd:PRK15134 180 ADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPT 249
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
34-218 |
4.09e-13 |
|
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: 65.25 E-value: 4.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 34 RRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEI-DGNDVTTMPmyRRSRLGVGYLpqeasifrglt 112
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMpEGEDLLFLP--QRPYLPLGTL----------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 113 veeniravlevhvkdkaeREQklnelleefhiqkLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAGVDPisvaD 192
Cdd:cd03223 81 ------------------REQ-------------LIYPWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDE----E 125
|
170 180
....*....|....*....|....*..
gi 521065470 193 IQNLVH-HLTARGIGVLVTDHnvRETL 218
Cdd:cd03223 126 SEDRLYqLLKELGITVISVGH--RPSL 150
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
32-245 |
4.10e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 67.81 E-value: 4.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 32 ATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMP--MYRRSRLGVGYLPQE--ASI 107
Cdd:PRK15079 32 KTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKddEWRAVRSDIQMIFQDplASL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 108 FRGLTVEENIRAVLEVH--------VKDKAE--------REQKLNELLEEFhiqklrksaavalSGGERRRLEIARALAT 171
Cdd:PRK15079 112 NPRMTIGEIIAEPLRTYhpklsrqeVKDRVKammlkvglLPNLINRYPHEF-------------SGGQCQRIGIARALIL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521065470 172 DPTFMLLDEPFAGVDpISV-ADIQNLVHHLTAR-GIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNP 245
Cdd:PRK15079 179 EPKLIICDEPVSALD-VSIqAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
23-201 |
1.38e-12 |
|
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: 64.59 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 23 IARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVD---EGTIEIDGNDVTTMPMYRRSRlgVG 99
Cdd:cd03233 9 ISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGE--II 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 100 YLPQEASIFRGLTVEENIRAVLevhvkdkaereqklnelleefhiqKLRKSAAV-ALSGGERRRLEIARALATDPTFMLL 178
Cdd:cd03233 87 YVSEEDVHFPTLTVRETLDFAL------------------------RCKGNEFVrGISGGERKRVSIAEALVSRASVLCW 142
|
170 180
....*....|....*....|...
gi 521065470 179 DEPFAGVDPISVADIQNLVHHLT 201
Cdd:cd03233 143 DNSTRGLDSSTALEILKCIRTMA 165
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
37-212 |
1.59e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 66.76 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 37 VNGVSL----VVRRGEAVGLLGPNGAGKTTCFYMITG-LVP-----VDEGTIE--IDgndvttmpMYRRSRLGvgylpqe 104
Cdd:PRK13409 85 VNGFKLyglpIPKEGKVTGILGPNGIGKTTAVKILSGeLIPnlgdyEEEPSWDevLK--------RFRGTELQ------- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 105 aSIFRGLtVEENIRAVLEVH------------VKD---KAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARAL 169
Cdd:PRK13409 150 -NYFKKL-YNGEIKVVHKPQyvdlipkvfkgkVREllkKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAAL 227
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 521065470 170 ATDPTFMLLDEPFAGVD---PISVAD-IQNLvhhltARGIGVLVTDH 212
Cdd:PRK13409 228 LRDADFYFFDEPTSYLDirqRLNVARlIREL-----AEGKYVLVVEH 269
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
36-244 |
2.14e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 66.69 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 36 VVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMP-MYRRSRLGVgyLPQEASIFRGlTVE 114
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGlMDLRKVLGI--IPQAPVLFSG-TVR 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 115 ENIRAVLEVHVKDkaereqkLNELLEEFHIQK-LRKS-----AAVALSG-----GERRRLEIARALATDPTFMLLDEPFA 183
Cdd:PLN03130 1331 FNLDPFNEHNDAD-------LWESLERAHLKDvIRRNslgldAEVSEAGenfsvGQRQLLSLARALLRRSKILVLDEATA 1403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521065470 184 GVDPISVADIQNLVHHlTARGIGVLVTDHNVrETLGLIDRAYIIHAGEVLTHGRANDIVNN 244
Cdd:PLN03130 1404 AVDVRTDALIQKTIRE-EFKSCTMLIIAHRL-NTIIDCDRILVLDAGRVVEFDTPENLLSN 1462
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
31-211 |
2.47e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 66.19 E-value: 2.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 31 YATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPvdEGTieidGNDVTTMPMYRRS-------RLGVGYLpq 103
Cdd:PRK10938 270 YNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHP--QGY----SNDLTLFGRRRGSgetiwdiKKHIGYV-- 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 104 EASIFRGLTVEENIRAVLEVHVKDK-------AEREQKL-NELLEEFHIQK-LRKSAAVALSGGERRRLEIARALATDPT 174
Cdd:PRK10938 342 SSSLHLDYRVSTSVRNVILSGFFDSigiyqavSDRQQKLaQQWLDILGIDKrTADAPFHSLSWGQQRLALIVRALVKHPT 421
|
170 180 190
....*....|....*....|....*....|....*..
gi 521065470 175 FMLLDEPFAGVDPISvadiqnlvHHLTARGIGVLVTD 211
Cdd:PRK10938 422 LLILDEPLQGLDPLN--------RQLVRRFVDVLISE 450
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
30-232 |
4.01e-12 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 65.58 E-value: 4.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 30 TYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTcFYM----------ITGlvpvdegTIEIDGNDVTTMPMYRRSRLGVG 99
Cdd:NF040905 269 LHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTE-LAMsvfgrsygrnISG-------TVFKDGKEVDVSTVSDAIDAGLA 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 100 YLPQEasifR---GLTVEENIR---------AVLEVHVKDKAEREQKLNELLEEFHIqklrKSAAVA-----LSGGERRR 162
Cdd:NF040905 341 YVTED----RkgyGLNLIDDIKrnitlanlgKVSRRGVIDENEEIKVAEEYRKKMNI----KTPSVFqkvgnLSGGNQQK 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 163 LEIARALATDPTFMLLDEPFAGVDPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEV 232
Cdd:NF040905 413 VVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRI 482
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
22-251 |
5.57e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 64.08 E-value: 5.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVD--------EGTIEIDGNDVTTMPMYRR 93
Cdd:PRK13547 2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 94 SRLGvGYLPQEASIFRGLTVEENIRAVLEVHVKDKAEREQKLNEL----LEEFHIQKLRKSAAVALSGGERRRLEIARAL 169
Cdd:PRK13547 82 ARLR-AVLPQAAQPAFAFSAREIVLLGRYPHARRAGALTHRDGEIawqaLALAGATALVGRDVTTLSGGELARVQFARVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 170 A---------TDPTFMLLDEPFAGVDPISVADIQNLVHHLTAR-GIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRAN 239
Cdd:PRK13547 161 AqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPA 240
|
250
....*....|..
gi 521065470 240 DIVNNPEVRRLY 251
Cdd:PRK13547 241 DVLTPAHIARCY 252
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
40-243 |
5.70e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 64.03 E-value: 5.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 40 VSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYR-----RSRLGVGYLPQEASIFRGlTVE 114
Cdd:PRK13646 26 VNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKyirpvRKRIGMVFQFPESQLFED-TVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 115 -------ENIRAVLEvHVKDKAEReqklneLLEEFHIQK-LRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAGVD 186
Cdd:PRK13646 105 reiifgpKNFKMNLD-EVKNYAHR------LLMDLGFSRdVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 521065470 187 PISVADIQNLVHHL-TARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVN 243
Cdd:PRK13646 178 PQSKRQVMRLLKSLqTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
34-180 |
6.14e-12 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 64.84 E-value: 6.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 34 RRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPM-YRRSRLGVgyLPQEASIFRGlT 112
Cdd:COG5265 371 RPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQaSLRAAIGI--VPQDTVLFND-T 447
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521065470 113 VEENIR----AVLEVHVKDKAEREQklnelLEEFhIQKLRKSAA-------VALSGGERRRLEIARALATDPTFMLLDE 180
Cdd:COG5265 448 IAYNIAygrpDASEEEVEAAARAAQ-----IHDF-IESLPDGYDtrvgergLKLSGGEKQRVAIARTLLKNPPILIFDE 520
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
14-181 |
7.30e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 64.91 E-value: 7.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 14 DKSRYQGTLIARGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVttmpmyrr 93
Cdd:PRK15064 312 DKKLHRNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENAN-------- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 94 srlgVGYLPQE-ASIF-RGLTV-------------EENIRAVlevhvkdkaereqkLNELLeeFHIQKLRKSAAVaLSGG 158
Cdd:PRK15064 384 ----IGYYAQDhAYDFeNDLTLfdwmsqwrqegddEQAVRGT--------------LGRLL--FSQDDIKKSVKV-LSGG 442
|
170 180
....*....|....*....|...
gi 521065470 159 ERRRLEIARALATDPTFMLLDEP 181
Cdd:PRK15064 443 EKGRMLFGKLMMQKPNVLVMDEP 465
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
33-212 |
9.80e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 64.74 E-value: 9.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 33 TRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGlvPVDEGTIEIDGNDVTTMPM---YRRSrlgVGYLPQEASIFR 109
Cdd:TIGR00956 775 KRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTGVITGGDRLVNGRPLdssFQRS---IGYVQQQDLHLP 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 110 GLTVEENIR--AVL----EVHVKDKAEREQKLNELLE-EFHIQKLRKSAAVALSGGERRRLEIARALATDPTFML-LDEP 181
Cdd:TIGR00956 850 TSTVRESLRfsAYLrqpkSVSKSEKMEYVEEVIKLLEmESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEP 929
|
170 180 190
....*....|....*....|....*....|.
gi 521065470 182 FAGVDPISVADIQNLVHHLTARGIGVLVTDH 212
Cdd:TIGR00956 930 TSGLDSQTAWSICKLMRKLADHGQAILCTIH 960
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
25-231 |
3.69e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.44 E-value: 3.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 25 RGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRLGVGYLPQE 104
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 105 ASIFRGLTVEENI---RAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEP 181
Cdd:PRK10982 82 LNLVLQRSVMDNMwlgRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 521065470 182 FAGVDPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGE 231
Cdd:PRK10982 162 TSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
36-180 |
5.23e-11 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 62.46 E-value: 5.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 36 VVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDgndvttmpmyRRSRLgvGYLPQEASIFRGLTVEE 115
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKP----------AKGKL--FYVPQRPYMTLGTLRDQ 534
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521065470 116 NIRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKS----AAVA-----LSGGERRRLEIARALATDPTFMLLDE 180
Cdd:TIGR00954 535 IIYPDSSEDMKRRGLSDKDLEQILDNVQLTHILEReggwSAVQdwmdvLSGGEKQRIAMARLFYHKPQFAILDE 608
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
33-246 |
6.77e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.80 E-value: 6.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 33 TRRV--VNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRS--RLGVGYLPQE--AS 106
Cdd:PRK10261 334 TREVhaVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQalRRDIQFIFQDpyAS 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 107 IFRGLTVEENIRAVLEVH-VKDKAEREQKLNELLEEFhiqKLRKSAAV----ALSGGERRRLEIARALATDPTFMLLDEP 181
Cdd:PRK10261 414 LDPRQTVGDSIMEPLRVHgLLPGKAAAARVAWLLERV---GLLPEHAWryphEFSGGQRQRICIARALALNPKVIIADEA 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521065470 182 FAGVDPISVADIQNLVHHLTAR-GIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNPE 246
Cdd:PRK10261 491 VSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQ 556
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
43-213 |
1.00e-10 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 60.46 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 43 VVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRLgvgylpQEasIFRGLtVEENIRAVLE 122
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDEILDEFRGSEL------QN--YFTKL-LEGDVKVIVK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 123 VHVKD---------------KAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAGVDP 187
Cdd:cd03236 93 PQYVDlipkavkgkvgellkKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180
....*....|....*....|....*.
gi 521065470 188 ISVADIQNLVHHLTARGIGVLVTDHN 213
Cdd:cd03236 173 KQRLNAARLIRELAEDDNYVLVVEHD 198
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
5-180 |
1.47e-10 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 60.97 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 5 PGPQAAGAADKSRYQgTLIARGLTKTYATRR-----VVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIE 79
Cdd:COG4615 312 AAADAAAPPAPADFQ-TLELRGVTYRYPGEDgdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEIL 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 80 IDGNDVT--TMPMYRrsrlgvgylpqeasifrgltveENIRAVL-------EVHVKDKAEREQKLNELLEEFHIQ-KLR- 148
Cdd:COG4615 391 LDGQPVTadNREAYR----------------------QLFSAVFsdfhlfdRLLGLDGEADPARARELLERLELDhKVSv 448
|
170 180 190
....*....|....*....|....*....|....*
gi 521065470 149 ---KSAAVALSGGERRRLEIARALATDPTFMLLDE 180
Cdd:COG4615 449 edgRFSTTDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
37-246 |
3.71e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 59.87 E-value: 3.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 37 VNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGndvttMPMYRRSRLGVGYLPQEASIFRGL----- 111
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDK-----MLLRRRSRQVIELSEQSAAQMRHVrgadm 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 112 ---------------TVEENIRAVLEVHvkDKAEREQKLNE---LLEEFHI---QKLRKSAAVALSGGERRRLEIARALA 170
Cdd:PRK10261 107 amifqepmtslnpvfTVGEQIAESIRLH--QGASREEAMVEakrMLDQVRIpeaQTILSRYPHQLSGGMRQRVMIAMALS 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521065470 171 TDPTFMLLDEPFAGVDPISVADIQNLVHHLTAR-GIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNPE 246
Cdd:PRK10261 185 CRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQ 261
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
110-209 |
4.23e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 59.26 E-value: 4.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 110 GLTVEEniraVLEVHVKDKAEREQklneLLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAGVDPIS 189
Cdd:PRK10938 99 GRTTAE----IIQDEVKDPARCEQ----LAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVAS 170
|
90 100
....*....|....*....|.
gi 521065470 190 VADIQNLVHHLTARGIG-VLV 209
Cdd:PRK10938 171 RQQLAELLASLHQSGITlVLV 191
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
37-212 |
6.78e-10 |
|
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: 59.03 E-value: 6.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 37 VNGVSL----VVRRGEAVGLLGPNGAGKTTCFYMITG-LVP----VDEgtiEIDGNDVttMPMYRRSRLGvgylpqeaSI 107
Cdd:COG1245 85 ENGFRLyglpVPKKGKVTGILGPNGIGKSTALKILSGeLKPnlgdYDE---EPSWDEV--LKRFRGTELQ--------DY 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 108 FRGLtVEENIRAVLEVH------------VKD---KAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATD 172
Cdd:COG1245 152 FKKL-ANGEIKVAHKPQyvdlipkvfkgtVRElleKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRD 230
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 521065470 173 PTFMLLDEPFAGVD---PISVAdiqNLVHHLTARGIGVLVTDH 212
Cdd:COG1245 231 ADFYFFDEPSSYLDiyqRLNVA---RLIRELAEEGKYVLVVEH 270
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
32-186 |
2.10e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 57.41 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 32 ATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYR-RSRLGVgyLPQEASIFRG 110
Cdd:PRK10789 326 TDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwRSRLAV--VSQTPFLFSD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 111 lTVEENIRAVLEVHVKDKAEREQKLNELLEEfhIQKLRK-------SAAVALSGGERRRLEIARALATDPTFMLLDEPFA 183
Cdd:PRK10789 404 -TVANNIALGRPDATQQEIEHVARLASVHDD--ILRLPQgydtevgERGVMLSGGQKQRISIARALLLNAEILILDDALS 480
|
...
gi 521065470 184 GVD 186
Cdd:PRK10789 481 AVD 483
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
33-237 |
4.34e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 55.42 E-value: 4.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 33 TRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITG--LVPVDEGTIEIDGNDVTTMPMYRRSRLGVGYLPQEASIFRG 110
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERAHLGIFLAFQYPIEIPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 111 LTVEENIRAVLEVHVKdkaerEQKLNEL--LEEFHI--QKLRK--------SAAV--ALSGGERRRLEIARALATDPTFM 176
Cdd:CHL00131 99 VSNADFLRLAYNSKRK-----FQGLPELdpLEFLEIinEKLKLvgmdpsflSRNVneGFSGGEKKRNEILQMALLDSELA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521065470 177 LLDEPFAGVDPISVADIQNLVHHLTARGIGVLVTDHNVRetlgLIDraYI----IHageVLTHGR 237
Cdd:CHL00131 174 ILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQR----LLD--YIkpdyVH---VMQNGK 229
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
37-229 |
5.66e-09 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 54.64 E-value: 5.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 37 VNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTI---EIDGNDVTTMPMYRRSRLGVGYLPQEASIFRGlTV 113
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsNKNESEPSFEATRSRNRYSVAYAAQKPWLLNA-TV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 114 EENI-----------RAVLEvhvkdkAEREQKLNELLEeFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPF 182
Cdd:cd03290 96 EENItfgspfnkqryKAVTD------ACSLQPDIDLLP-FGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 521065470 183 AGVDpISVADiqnlvhHLTARGIGVLVTDHnvRETLGLIDRA--YIIHA 229
Cdd:cd03290 169 SALD-IHLSD------HLMQEGILKFLQDD--KRTLVLVTHKlqYLPHA 208
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
37-244 |
5.85e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 56.05 E-value: 5.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 37 VNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNdvttmpmyrRSRLGVGylpqeASIFRGLTVEEN 116
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS---------AALIAIS-----SGLNGQLTGIEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 117 IRAVLEVHVKDKAEREQKLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAGVDPISVADIQNL 196
Cdd:PRK13545 106 IELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDK 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 521065470 197 VHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNN 244
Cdd:PRK13545 186 MNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
8-186 |
6.90e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 55.88 E-value: 6.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 8 QAAGAADKSRYQGTLIARGLTKTYAT-RRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVT 86
Cdd:PRK10790 327 QQYGNDDRPLQSGRIDIDNVSFAYRDdNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLS 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 87 TMPmYRRSRLGVGYLPQE-----ASIFRGLTVEENIRavlEVHVKDKAEREQkLNELLEEFH--IQKLRKSAAVALSGGE 159
Cdd:PRK10790 407 SLS-HSVLRQGVAMVQQDpvvlaDTFLANVTLGRDIS---EEQVWQALETVQ-LAELARSLPdgLYTPLGEQGNNLSVGQ 481
|
170 180
....*....|....*....|....*..
gi 521065470 160 RRRLEIARALATDPTFMLLDEPFAGVD 186
Cdd:PRK10790 482 KQLLALARVLVQTPQILILDEATANID 508
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
21-187 |
7.41e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 55.75 E-value: 7.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 21 TLIARGLTKTYATRRV-VNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRrsrlgvg 99
Cdd:PRK10522 322 TLELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPED------- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 100 ylpqeasiFRGLtveenIRAVL-EVHVKDK---AEREQKLNELLEEF--HIQ---KLR----KSAAVALSGGERRRLEIA 166
Cdd:PRK10522 395 --------YRKL-----FSAVFtDFHLFDQllgPEGKPANPALVEKWleRLKmahKLEledgRISNLKLSKGQKKRLALL 461
|
170 180
....*....|....*....|.
gi 521065470 167 RALATDPTFMLLDEPFAGVDP 187
Cdd:PRK10522 462 LALAEERDILLLDEWAADQDP 482
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
37-246 |
8.13e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.51 E-value: 8.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 37 VNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYRRSRLGVGYLPQE---ASIFRGLTV 113
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHGFALVTEErrsTGIYAYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 114 E-----ENIRAVLE-VHVKDKAEREQKLNELLEEFHIQKLRKSAAV-ALSGGERRRLEIARALATDPTFMLLDEPFAGVD 186
Cdd:PRK10982 344 GfnsliSNIRNYKNkVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIgSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGID 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 187 PISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYiihageVLTHGRANDIVNNPE 246
Cdd:PRK10982 424 VGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRIL------VMSNGLVAGIVDTKT 477
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
36-186 |
8.27e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 54.80 E-value: 8.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 36 VVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGL--VPVDEGTIEIDGNDVTTMPMYRRSRLGVGY-------LPQEAS 106
Cdd:PRK09580 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEGIFMafqypveIPGVSN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 107 IFRGLTVEENIRAVLEVHVKDKAEREQKLNELLEEFHIQK--LRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAG 184
Cdd:PRK09580 96 QFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMPEdlLTRSVNVGFSGGEKKRNDILQMAVLEPELCILDESDSG 175
|
..
gi 521065470 185 VD 186
Cdd:PRK09580 176 LD 177
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
24-186 |
8.47e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 55.72 E-value: 8.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 24 ARGLTKTyatrrvVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNdvttmpmyrrsrlgVGYLPQ 103
Cdd:TIGR00957 647 ARDLPPT------LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--------------VAYVPQ 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 104 EASIfRGLTVEENIravLEVHVKDKAEREQKLNE--LLEEFHI-----QKLRKSAAVALSGGERRRLEIARALATDPTFM 176
Cdd:TIGR00957 707 QAWI-QNDSLRENI---LFGKALNEKYYQQVLEAcaLLPDLEIlpsgdRTEIGEKGVNLSGGQKQRVSLARAVYSNADIY 782
|
170
....*....|
gi 521065470 177 LLDEPFAGVD 186
Cdd:TIGR00957 783 LFDDPLSAVD 792
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
43-238 |
1.28e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 52.96 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 43 VVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYrrsrlgvgylpqeasifrgltveeniravle 122
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQY------------------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 123 vhvkdkaereqklnelleefhiqklrksaaVALSGGERRRLEIARALATDPTFMLLDEPFAGVDPISVADIQNLVHHLTA 202
Cdd:cd03222 70 ------------------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSE 119
|
170 180 190
....*....|....*....|....*....|....*..
gi 521065470 203 RGI-GVLVTDHNVRETLGLIDRAYIIHaGEVLTHGRA 238
Cdd:cd03222 120 EGKkTALVVEHDLAVLDYLSDRIHVFE-GEPGVYGIA 155
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
36-255 |
1.55e-08 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 54.14 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 36 VVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMYR-RSRLGVgyLPQEASIFRGltve 114
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTlRSRLSI--ILQDPILFSG---- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 115 eNIRAVLEVHVKDKAEReqkLNELLEEFHIQKLRKSA-----AVALSGGE------RRRLEIARALATDPTFMLLDEPFA 183
Cdd:cd03288 110 -SIRFNLDPECKCTDDR---LWEALEIAQLKNMVKSLpggldAVVTEGGEnfsvgqRQLFCLARAFVRKSSILIMDEATA 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521065470 184 GVDPISVADIQNLVhhLTARGIGVLVT-DHNVretlglidrAYIIHAGEVLTHGRANdIVNNPEVRRLYLGDN 255
Cdd:cd03288 186 SIDMATENILQKVV--MTAFADRTVVTiAHRV---------STILDADLVLVLSRGI-LVECDTPENLLAQED 246
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
35-245 |
1.99e-08 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 54.14 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 35 RVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPvDEGTIEID-----GNDVTTMPMYRRSRLgVG---------- 99
Cdd:COG4170 21 KAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITK-DNWHVTADrfrwnGIDLLKLSPRERRKI-IGreiamifqep 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 100 --YLPQEASIFRGLtvEENIRA-VLEVHV-KDKAEREQKLNELLEEFHI---QKLRKSAAVALSGGERRRLEIARALATD 172
Cdd:COG4170 99 ssCLDPSAKIGDQL--IEAIPSwTFKGKWwQRFKWRKKRAIELLHRVGIkdhKDIMNSYPHELTEGECQKVMIAMAIANQ 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521065470 173 PTFMLLDEPFAGVDPISVADIQNLVHHLTA-RGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNP 245
Cdd:COG4170 177 PRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSP 250
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
33-187 |
2.80e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 52.65 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 33 TRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVP--VDEGTIEIDGNDvttmpmyrrsrlgvgyLPQEASIFRG 110
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQ----------------FGREASLIDA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 111 LTVEENIRAVLEVhvkdkaereqklnelleeFHIQKLrkSAAVA-------LSGGERRRLEIARALATDPTFMLLDEPFA 183
Cdd:COG2401 106 IGRKGDFKDAVEL------------------LNAVGL--SDAVLwlrrfkeLSTGQKFRFRLALLLAERPKLLVIDEFCS 165
|
....
gi 521065470 184 GVDP 187
Cdd:COG2401 166 HLDR 169
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
42-181 |
4.10e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.42 E-value: 4.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 42 LVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDgNDVTTmpmyrrSRL------------------GVG---- 99
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE-QDLIV------ARLqqdpprnvegtvydfvaeGIEeqae 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 100 YLPQEASIFRGLTVE---------ENIRAVLEVHvkDKAEREQKLNELLEEFHIQKLRKSAAvaLSGGERRRLEIARALA 170
Cdd:PRK11147 97 YLKRYHDISHLVETDpseknlnelAKLQEQLDHH--NLWQLENRINEVLAQLGLDPDAALSS--LSGGWLRKAALGRALV 172
|
170
....*....|.
gi 521065470 171 TDPTFMLLDEP 181
Cdd:PRK11147 173 SNPDVLLLDEP 183
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
25-230 |
7.39e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.48 E-value: 7.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 25 RGLTKTYATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVD--EGTIEIDGNDVTTMPMYRRSRLGVGYLP 102
Cdd:NF040905 5 RGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGEVCRFKDIRDSEALGIVIIH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 103 QEASIFRGLTVEENI--------RAVLevhvkDKAEREQKLNELLEEFhiqKLRKSAAVALSG---GERRRLEIARALAT 171
Cdd:NF040905 85 QELALIPYLSIAENIflgnerakRGVI-----DWNETNRRARELLAKV---GLDESPDTLVTDigvGKQQLVEIAKALSK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 521065470 172 DPTFMLLDEPFAGVDPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAG 230
Cdd:NF040905 157 DVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDG 215
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
36-186 |
1.26e-07 |
|
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: 52.26 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 36 VVNGVSLVVRRGEAVGLLGPNGAGKTTcfyMITGLVPVDE---GTIEIDGNDVTTMPMYR-RSRLGVgyLPQEASIFRGL 111
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSS---LTLGLFRINEsaeGEIIIDGLNIAKIGLHDlRFKITI--IPQDPVLFSGS 1375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 112 T----------VEENIRAVLEV-HVKD-KAEREQKLNELLEEfhiqklrksAAVALSGGERRRLEIARALATDPTFMLLD 179
Cdd:TIGR00957 1376 LrmnldpfsqySDEEVWWALELaHLKTfVSALPDKLDHECAE---------GGENLSVGQRQLVCLARALLRKTKILVLD 1446
|
....*..
gi 521065470 180 EPFAGVD 186
Cdd:TIGR00957 1447 EATAAVD 1453
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
36-246 |
1.31e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.09 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 36 VVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPMyRRSRLGVGYLPQEASIFRGlTVEE 115
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGL-RELRRQFSMIPQDPVLFDG-TVRQ 1402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 116 NIRAVLEVhvkDKAEREQKLnELLeefhiqKLRKSAAVALSGGERRRLE--------------IARA-LATDPTFMLLDE 180
Cdd:PTZ00243 1403 NVDPFLEA---SSAEVWAAL-ELV------GLRERVASESEGIDSRVLEggsnysvgqrqlmcMARAlLKKGSGFILMDE 1472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521065470 181 PFAGVDPISVADIQNLVhhLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNPE 246
Cdd:PTZ00243 1473 ATANIDPALDRQIQATV--MSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQ 1536
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
14-246 |
1.35e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 51.36 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 14 DKSRYQGTLIARGLTKTYATrrvVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGnDVTTMPMyrr 93
Cdd:PRK13546 20 NKERMKDALIPKHKNKTFFA---LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-EVSVIAI--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 94 srlgvgylpqEASIFRGLTVEENIRAVLEVHVKDKAEREQKLNELLE-----EFHIQKLRKsaavaLSGGERRRLEIARA 168
Cdd:PRK13546 93 ----------SAGLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEfselgEFIYQPVKK-----YSSGMRAKLGFSIN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521065470 169 LATDPTFMLLDEPFAGVDPISVADIQNLVHHLTARGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNPE 246
Cdd:PRK13546 158 ITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKYE 235
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
31-232 |
2.02e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 51.32 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 31 YATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEIDGNdvttmpmyrrsrLGVGYLPQEASIFrg 110
Cdd:PRK10636 322 YGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKG------------IKLGYFAQHQLEF-- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 111 LTVEEnirAVLEvHVKDKAER--EQKLNELLEEFHIQKLRKSAAVA-LSGGERRRLEIARALATDPTFMLLDEPFAGVDp 187
Cdd:PRK10636 388 LRADE---SPLQ-HLARLAPQelEQKLRDYLGGFGFQGDKVTEETRrFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD- 462
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 521065470 188 isvADI-QNLVHHLTA-RGIGVLVTD--HNVRETlglIDRAYIIHAGEV 232
Cdd:PRK10636 463 ---LDMrQALTEALIDfEGALVVVSHdrHLLRST---TDDLYLVHDGKV 505
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
35-212 |
3.88e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.00 E-value: 3.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 35 RVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVP--VDEGTIEIDGNDVTTMPMYRRSrlgvGYLPQEASIFRGLT 112
Cdd:PLN03140 894 QLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDIRISGFPKKQETFARIS----GYCEQNDIHSPQVT 969
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 113 VEENI------RAVLEVhvkDKAEREQKLNELLEEFHIQKLrKSAAVALSG------GERRRLEIARALATDPTFMLLDE 180
Cdd:PLN03140 970 VRESLiysaflRLPKEV---SKEEKMMFVDEVMELVELDNL-KDAIVGLPGvtglstEQRKRLTIAVELVANPSIIFMDE 1045
|
170 180 190
....*....|....*....|....*....|..
gi 521065470 181 PFAGVDPISVADIQNLVHHLTARGIGVLVTDH 212
Cdd:PLN03140 1046 PTSGLDARAAAIVMRTVRNTVDTGRTVVCTIH 1077
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
32-244 |
5.96e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.12 E-value: 5.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 32 ATRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITG-LVPVDEGTIEIDGNdvttmpmyrrsrlgVGYLPQEASIFRG 110
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRGT--------------VAYVPQVSWIFNA 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 111 lTVEENIR--AVLEVHVKDKAEREQKLNELLEEFHIQKLRK--SAAVALSGGERRRLEIARALATDPTFMLLDEPFAGVD 186
Cdd:PLN03130 694 -TVRDNILfgSPFDPERYERAIDVTALQHDLDLLPGGDLTEigERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521065470 187 pisvADIQNLVHHLTARG-----IGVLVTdhNVRETLGLIDRAYIIHAGEVLTHGRANDIVNN 244
Cdd:PLN03130 773 ----AHVGRQVFDKCIKDelrgkTRVLVT--NQLHFLSQVDRIILVHEGMIKEEGTYEELSNN 829
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
155-230 |
8.18e-07 |
|
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: 48.76 E-value: 8.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 155 LSGGERRRLEIARAL---ATDPTFMLLDEPFAGvdpISVADIQNLV---HHLTARGIGVLVTDHNvretLGLIDRA-YII 227
Cdd:cd03271 170 LSGGEAQRIKLAKELskrSTGKTLYILDEPTTG---LHFHDVKKLLevlQRLVDKGNTVVVIEHN----LDVIKCAdWII 242
|
...
gi 521065470 228 HAG 230
Cdd:cd03271 243 DLG 245
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
33-247 |
1.29e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 49.20 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 33 TRRVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITG-LVPVDEGTIEIDGNdvttmpmyrrsrlgVGYLPQEASIFRGl 111
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRGS--------------VAYVPQVSWIFNA- 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 112 TVEENIR--AVLEVHVKDKAEREQKLNELLEEFHIQKLRK--SAAVALSGGERRRLEIARALATDPTFMLLDEPFAGVDP 187
Cdd:PLN03232 694 TVRENILfgSDFESERYWRAIDVTALQHDLDLLPGRDLTEigERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDA 773
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521065470 188 ISVADIQN--LVHHLTARgIGVLVTdhNVRETLGLIDRAYIIHAGEVLTHGRANDIVNNPEV 247
Cdd:PLN03232 774 HVAHQVFDscMKDELKGK-TRVLVT--NQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSL 832
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
25-245 |
2.51e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 47.87 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 25 RGLTKTYATR----RVVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGlVPVDEGTIEIDG---NDVTTM---PMYRRS 94
Cdd:PRK15093 7 RNLTIEFKTSdgwvKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICG-VTKDNWRVTADRmrfDDIDLLrlsPRERRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 95 RLG--VGYLPQE--------ASIFRGLtveenIRAVLEVHVKDK-----AEREQKLNELLEEFHIQ---KLRKSAAVALS 156
Cdd:PRK15093 86 LVGhnVSMIFQEpqscldpsERVGRQL-----MQNIPGWTYKGRwwqrfGWRKRRAIELLHRVGIKdhkDAMRSFPYELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 157 GGERRRLEIARALATDPTFMLLDEPFAGVDPISVADIQNLVHHLTA-RGIGVLVTDHNVRETLGLIDRAYIIHAGEVLTH 235
Cdd:PRK15093 161 EGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDLQMLSQWADKINVLYCGQTVET 240
|
250
....*....|
gi 521065470 236 GRANDIVNNP 245
Cdd:PRK15093 241 APSKELVTTP 250
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
116-230 |
4.26e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 47.70 E-value: 4.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 116 NIRAVLEVHVKDKAER-------EQKLnELLEEFHIQKLR-KSAAVALSGGERRRLEIARAL---ATDPTFMLLDEPFAG 184
Cdd:TIGR00630 784 NIADVLDMTVEEAYEFfeavpsiSRKL-QTLCDVGLGYIRlGQPATTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTG 862
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 521065470 185 vdpISVADIQNL---VHHLTARGIGVLVTDHNvretLGLIDRA-YIIHAG 230
Cdd:TIGR00630 863 ---LHFDDIKKLlevLQRLVDKGNTVVVIEHN----LDVIKTAdYIIDLG 905
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
50-232 |
6.71e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.78 E-value: 6.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 50 VGLLGPNGAGKTTCFYMITGLVPVDEGTI--------------EIDGNDVTTMPMYRRSRLGVGYLpqeasifrgltvee 115
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTVfrsakvrmavfsqhHVDGLDLSSNPLLYMMRCFPGVP-------------- 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 116 niravlevhvkdkaerEQKLNELLEEFHIQ-KLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAGVDPISV-ADI 193
Cdd:PLN03073 604 ----------------EQKLRAHLGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVeALI 667
|
170 180 190
....*....|....*....|....*....|....*....
gi 521065470 194 QNLVhhlTARGiGVLVTDHNVRETLGLIDRAYIIHAGEV 232
Cdd:PLN03073 668 QGLV---LFQG-GVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
40-186 |
1.76e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 45.93 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 40 VSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIeidgndvttmpMYRRSrlgVGYLPQEASIFRGlTVEENIRA 119
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-----------WAERS---IAYVPQQAWIMNA-TVRGNILF 743
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521065470 120 VLEvhvkdkaEREQKLNELLE----EFHIQKLRK-------SAAVALSGGERRRLEIARALATDPTFMLLDEPFAGVD 186
Cdd:PTZ00243 744 FDE-------EDAARLADAVRvsqlEADLAQLGGgleteigEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
74-246 |
3.98e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 44.63 E-value: 3.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 74 DEGTIEIDGNDVTTMPMyRRSRLGVGYLPQEASIFrGLTVEENIRAVLEVHVKDKAEREQK---LNELLEEF------HI 144
Cdd:PTZ00265 1275 NSGKILLDGVDICDYNL-KDLRNLFSIVSQEPMLF-NMSIYENIKFGKEDATREDVKRACKfaaIDEFIESLpnkydtNV 1352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 145 QKLRKSaavaLSGGERRRLEIARALATDPTFMLLDEPFAGVDPISVADIQNLVHHLTARGigvlvtdhnvretlgliDRA 224
Cdd:PTZ00265 1353 GPYGKS----LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKA-----------------DKT 1411
|
170 180
....*....|....*....|....
gi 521065470 225 YIIHAGEVLTHGRANDIV--NNPE 246
Cdd:PTZ00265 1412 IITIAHRIASIKRSDKIVvfNNPD 1435
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
155-230 |
4.13e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 43.08 E-value: 4.13e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521065470 155 LSGGERRRLEIARALA--TDPTFMLLDEPFAGVDPISVADIQNLVHHLTARGIGVLVTDHNVRetlgLIDRA-YIIHAG 230
Cdd:cd03238 88 LSGGELQRVKLASELFsePPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLD----VLSSAdWIIDFG 162
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
154-214 |
6.44e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.05 E-value: 6.44e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521065470 154 ALSGGERRRLEIARAL---ATDPTFMLLDEPFAGvdpISVADIQNLVH---HLTARGIGVLVTDHNV 214
Cdd:PRK00635 809 SLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTG---LHTHDIKALIYvlqSLTHQGHTVVIIEHNM 872
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
54-212 |
8.37e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 42.17 E-value: 8.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 54 GPNGAGKTTCFYMITGLVPVDEGTIEIDGNDVTTMPmyrrsRLGVGYLPQEASIFRGLTVEENIRAVLEVHvkDKAEreq 133
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA-----KPYCTYIGHNLGLKLEMTVFENLKFWSEIY--NSAE--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 134 KLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAGVDPISVADIQNL-VHHLTARGIgVLVTDH 212
Cdd:PRK13541 103 TLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLiVMKANSGGI-VLLSSH 181
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
31-200 |
8.53e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.48 E-value: 8.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 31 YATRR---VVNGVSLVVRRGEAVGLLGPNGAGKTTCFYMITGLVPVDEGTIEI-DGNDVTTMPM-YRRSRLGVgyLPQEA 105
Cdd:PTZ00265 392 YDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLkWWRSKIGV--VSQDP 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 106 SIFRGlTVEENIRAVLeVHVKDKAEREQKLNE------------------------------------------------ 137
Cdd:PTZ00265 470 LLFSN-SIKNNIKYSL-YSLKDLEALSNYYNEdgndsqenknkrnscrakcagdlndmsnttdsneliemrknyqtikds 547
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521065470 138 ---------LLEEF------HIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAGVDPISVADIQNLVHHL 200
Cdd:PTZ00265 548 evvdvskkvLIHDFvsalpdKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNL 625
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
155-213 |
2.95e-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: 2.95e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521065470 155 LSGGERRRLEIARALA----TDPTFMLLDEPFAGVDPISVADIQNLVHHLTARGIGVLVTDHN 213
Cdd:cd03227 78 LSGGEKELSALALILAlaslKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHL 140
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
155-244 |
8.07e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.58 E-value: 8.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 155 LSGGERRRLEIARALATDPTFM--LLDEPFAGVDPISVADIQNLVHHLTARGIGVLVTDHNvRETLGLIDRAYI------ 226
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD-EQMISLADRIIDigpgag 555
|
90
....*....|....*...
gi 521065470 227 IHAGEVLTHGRANDIVNN 244
Cdd:PRK00635 556 IFGGEVLFNGSPREFLAK 573
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
155-213 |
1.13e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.20 E-value: 1.13e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521065470 155 LSGGERRRLEIARALATDPT--FMLLDEPFAGVDPISVADIQNLVHHLTARGIGVLVTDHN 213
Cdd:PRK00635 1388 LSDGEHYRLHLAKKISSNLTdiIYLLEDPLSGLHPQDAPTLLQLIKELVTNNNTVIATDRS 1448
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
151-246 |
1.18e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.00 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 151 AAVALSGGERRRLEIARALATDPTFML--LDEPFAGVDPISVADIQNLVHHLTARGIGVLVTDHNvRETLGLIDraYII- 227
Cdd:TIGR00630 485 AAGTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHD-EDTIRAAD--YVId 561
|
90 100
....*....|....*....|....*.
gi 521065470 228 -------HAGEVLTHGRANDIVNNPE 246
Cdd:TIGR00630 562 igpgageHGGEVVASGTPEEILANPD 587
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
34-181 |
1.37e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.84 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 34 RRVVNGVSLVVRRGEAVGLLGPNGAGKTTCF-YM----ITGL------VPVDEgtiEIDGNDVTTMPMY-----RRSRLg 97
Cdd:PLN03073 190 RDLIVDASVTLAFGRHYGLVGRNGTGKTTFLrYMamhaIDGIpkncqiLHVEQ---EVVGDDTTALQCVlntdiERTQL- 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 98 vgyLPQEASIF---RGLTVE--------ENIRAVLEVHVKDKAEREQKLNELLEEFHIQ--------------KLRKSAA 152
Cdd:PLN03073 266 ---LEEEAQLVaqqRELEFEtetgkgkgANKDGVDKDAVSQRLEEIYKRLELIDAYTAEaraasilaglsftpEMQVKAT 342
|
170 180
....*....|....*....|....*....
gi 521065470 153 VALSGGERRRLEIARALATDPTFMLLDEP 181
Cdd:PLN03073 343 KTFSGGWRMRIALARALFIEPDLLLLDEP 371
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
22-114 |
3.68e-03 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 38.23 E-value: 3.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 22 LIARGLTKTYA-----TRRVVNGV--SLVVRRGEAVGLLGPNGAGKTTCFYmitglvpvdeGTIEIDGNDVTTMPMYRRS 94
Cdd:cd05958 4 LRSPEREWTYRdllalANRIANVLvgELGIVPGNRVLLRGSNSPELVACWF----------GIQKAGAIAVATMPLLRPK 73
|
90 100
....*....|....*....|
gi 521065470 95 RLgvGYLPQEASIFRGLTVE 114
Cdd:cd05958 74 EL--AYILDKARITVALCAH 91
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
46-224 |
3.76e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 36.97 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 46 RGEAVGLLGPNGAGKTTCFYMITG-LVPVDEGTIEIDGNDvttmpmyrrsrlgvgylpqeasifrgltveeniravlevh 124
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALAReLGPPGGGVIYIDGED---------------------------------------- 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 125 vkdkaereqkLNELLEEFHIQKLRKSAAVALSGGERRRLEIARALATDPTFMLLDEPFAGVDPISVADIQNLVH------ 198
Cdd:smart00382 41 ----------ILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrllll 110
|
170 180
....*....|....*....|....*.
gi 521065470 199 HLTARGIGVLVTDHNVRETLGLIDRA 224
Cdd:smart00382 111 LKSEKNLTVILTTNDEKDLGPALLRR 136
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
154-241 |
4.94e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 38.27 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 154 ALSGGERRRLEIARAL---ATDPTFMLLDEPFAGVDPISVADIQNLVHHLTARGIGVLVTDHNVRetlgLIDRA-YII-- 227
Cdd:PRK00635 1699 SLSLSEKIAIKIAKFLylpPKHPTLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDPA----LLKQAdYLIem 1774
|
90 100
....*....|....*....|
gi 521065470 228 ------HAGEVLTHGRANDI 241
Cdd:PRK00635 1775 gpgsgkTGGKILFSGPPKDI 1794
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
151-236 |
8.93e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 36.47 E-value: 8.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521065470 151 AAVALSGGERRRLEIARALATDPTFML--LDEPFAGVDPISVADIQNLVHHLTARGIGVLVTDHNvRETLGLIDraYII- 227
Cdd:cd03270 134 SAPTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHD-EDTIRAAD--HVId 210
|
90
....*....|....*.
gi 521065470 228 -------HAGEVLTHG 236
Cdd:cd03270 211 igpgagvHGGEIVAQG 226
|
|
| |
