|
Name |
Accession |
Description |
Interval |
E-value |
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-211 |
2.89e-154 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 427.48 E-value: 2.89e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAIARMGVVRTFQHVRLFREMTVIENLLVAQHQHLKSGVFAGLLKTPAFR 80
Cdd:PRK11300 45 TTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRTFQHVRLFREMTVIENLLVAQHQQLKTGLFSGLLKTPAFR 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 81 RAEAEALARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHK 160
Cdd:PRK11300 125 RAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHN 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1540799172 161 VSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRNNPDVIRAYLGEE 211
Cdd:PRK11300 205 VTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNPDVIKAYLGEA 255
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-211 |
1.85e-111 |
|
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: 318.91 E-value: 1.85e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAIARMGVVRTFQHVRLFREMTVIENLLVAQHQHLKSGVFAGLLKTPAFR 80
Cdd:COG0411 44 TTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLGIARTFQNPRLFPELTVLENVLVAAHARLGRGLLAALLRLPRAR 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 81 RAEAEALARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHK 160
Cdd:COG0411 124 REEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERG 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1540799172 161 VSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRNNPDVIRAYLGEE 211
Cdd:COG0411 204 ITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVRADPRVIEAYLGEE 254
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1-203 |
1.22e-87 |
|
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: 258.14 E-value: 1.22e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAIARMGVVRTFQHVRLFREMTVIENLLVAQHQHLKSGVFAGllktpAFR 80
Cdd:cd03219 40 TTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRTFQIPRLFPELTVLENVMVAAQARTGSGLLLA-----RAR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 81 RAEAEALARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHk 160
Cdd:cd03219 115 REEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERG- 193
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1540799172 161 VSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRNNPDV 203
Cdd:cd03219 194 ITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPRV 236
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-209 |
9.48e-43 |
|
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: 143.58 E-value: 9.48e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAIARMGVVrtfqHV----RLFREMTVIENLLVAQHQHLKSGVFAGLLkt 76
Cdd:COG0410 43 TTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIG----YVpegrRIFPSLTVEENLLLGAYARRDRAEVRADL-- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 77 pafrraeaealaraaewlERVG-----LLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHL 151
Cdd:COG0410 117 ------------------ERVYelfprLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEI 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1540799172 152 IVELRDRhKVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRNNPDVIRAYLG 209
Cdd:COG0410 179 IRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEVREAYLG 235
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1-200 |
6.25e-41 |
|
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: 138.34 E-value: 6.25e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAIARMGVVRTFQHVRLFREMTVIENLLVAQHQHLKSGVFAGllktpafr 80
Cdd:cd03224 40 TTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYVPEGRRIFPELTVEENLLLGAYARRRAKRKAR-------- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 81 raeaealaraaewLERV-----GLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVEL 155
Cdd:cd03224 112 -------------LERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIREL 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1540799172 156 RDRhKVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRNN 200
Cdd:cd03224 179 RDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-208 |
8.83e-41 |
|
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: 138.57 E-value: 8.83e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAI----ARMGVVrtFQHVRLFREMTVIENLLVAQHQHLKsgvfagllKT 76
Cdd:COG1127 45 SVLLKLIIGLLRPDSGEILVDGQDITGLSEKELyelrRRIGML--FQGGALFDSLTVFENVAFPLREHTD--------LS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 77 PAfrraeaEALARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELR 156
Cdd:COG1127 115 EA------EIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELR 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1540799172 157 DRHKVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRNNPD-VIRAYL 208
Cdd:COG1127 189 DELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASDDpWVRQFL 241
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1-209 |
2.26e-40 |
|
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: 137.29 E-value: 2.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAIARMGVVRTFQHVRLFREMTVIENLLVAQHQHLKSgvfagllktpafr 80
Cdd:cd03218 40 TTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYLPQEASIFRKLTVEENILAVLEIRGLS------------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 81 raEAEALARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRhK 160
Cdd:cd03218 107 --KKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDR-G 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1540799172 161 VSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRNNPDVIRAYLG 209
Cdd:cd03218 184 IGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKVYLG 232
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1-203 |
1.41e-38 |
|
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: 133.01 E-value: 1.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAG----QAIARMGVVrtFQHVRLFREMTVIENLLVAQHQHLKsgvfagllkt 76
Cdd:cd03261 40 STLLRLIVGLLRPDSGEVLIDGEDISGLSEaelyRLRRRMGML--FQSGALFDSLTVFENVAFPLREHTR---------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 77 pafrRAEAEALARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELR 156
Cdd:cd03261 108 ----LSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLK 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1540799172 157 DRHKVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRN--NPDV 203
Cdd:cd03261 184 KELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRAsdDPLV 232
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-211 |
3.98e-37 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 129.38 E-value: 3.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAIARMGVVRTFQHVRLFREMTVIENLL-VAQHQHLKSgvfagllktpaf 79
Cdd:COG1137 43 TTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLGIGYLPQEASIFRKLTVEDNILaVLELRKLSK------------ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 80 rraeAEALARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRh 159
Cdd:COG1137 111 ----KEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKER- 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1540799172 160 KVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRNNPDVIRAYLGEE 211
Cdd:COG1137 186 GIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPLVRKVYLGED 237
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1-211 |
6.68e-37 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 128.64 E-value: 6.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAIARMGVVrtFQHVRLFREMTVIENLLVaqhqhlksgvFAGLLKTPAfr 80
Cdd:COG1131 40 TTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYV--PQEPALYPDLTVRENLRF----------FARLYGLPR-- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 81 raeAEALARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRhK 160
Cdd:COG1131 106 ---KEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAE-G 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1540799172 161 VSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRNNP--DVIRAYLGEE 211
Cdd:COG1131 182 KTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLleDVFLELTGEE 234
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1-206 |
1.97e-30 |
|
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: 111.66 E-value: 1.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAIARM-GVVrtFQHVR--LFrEMTVIENllVAqhqhlksgvFaGL--LK 75
Cdd:COG1122 41 STLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKvGLV--FQNPDdqLF-APTVEED--VA---------F-GPenLG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 76 TPAfrraeAEALARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVEL 155
Cdd:COG1122 106 LPR-----EEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1540799172 156 RDRHKvSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRNNPDVIRA 206
Cdd:COG1122 181 NKEGK-TVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYELLEE 230
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1-197 |
1.61e-28 |
|
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: 106.88 E-value: 1.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAI----ARMGVVrtFQHVRLFREMTVIENLLV---AQHQHLKS--GVFA 71
Cdd:cd03256 41 STLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlrRQIGMI--FQQFNLIERLSVLENVLSgrlGRRSTWRSlfGLFP 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 72 GLLKTPAFRRaeaealaraaewLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHL 151
Cdd:cd03256 119 KEEKQRALAA------------LERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDL 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1540799172 152 IVELRDRHKVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEI 197
Cdd:cd03256 187 LKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-200 |
5.82e-28 |
|
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: 105.71 E-value: 5.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAIARMGVVrtFQHVRLFREMTVIENLLVaqhqhlksgvFAgllktPAFR 80
Cdd:COG4555 41 TTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVL--PDERGLYDRLTVRENIRY----------FA-----ELYG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 81 RAEAEALARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHK 160
Cdd:COG4555 104 LFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGK 183
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1540799172 161 VsVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRNN 200
Cdd:COG4555 184 T-VLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
1-208 |
7.60e-28 |
|
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: 104.91 E-value: 7.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAIARMGVVRTFQHVRLFREMTVIENLLV------AQHQHLKSGVFAGLl 74
Cdd:TIGR03410 40 TTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAYVPQGREIFPRLTVEENLLTglaalpRRSRKIPDEIYELF- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 75 ktPAfrraeaealaraaewlervgLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVE 154
Cdd:TIGR03410 119 --PV--------------------LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRR 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1540799172 155 LRDRHKVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIrnNPDVIRAYL 208
Cdd:TIGR03410 177 LRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL--DEDKVRRYL 228
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-207 |
8.36e-28 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 105.17 E-value: 8.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLeGLAGQAIA----RMGVVRTFQhvrlfreMTVIEnlLVAqhqhlkSGVFAgllKT 76
Cdd:COG1121 46 STLLKAILGLLPPTSGTVRLFGKPP-RRARRRIGyvpqRAEVDWDFP-------ITVRD--VVL------MGRYG---RR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 77 PAFRRAEAEALARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELR 156
Cdd:COG1121 107 GLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELR 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1540799172 157 dRHKVSVLLIEHDMKLVMGISDRIYVVNqGTPLAQGTPAEIRNNPDVIRAY 207
Cdd:COG1121 187 -REGKTILVVTHDLGAVREYFDRVLLLN-RGLVAHGPPEEVLTPENLSRAY 235
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-201 |
2.45e-27 |
|
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: 108.07 E-value: 2.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAIA----RMGVVrtFQHVR--LFREMTVIENLLVAQHQHlksgvfaGLL 74
Cdd:COG1123 305 STLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRelrrRVQMV--FQDPYssLNPRMTVGDIIAEPLRLH-------GLL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 75 KTPAfrraeaeALARAAEWLERVGL-LSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIV 153
Cdd:COG1123 376 SRAE-------RRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLR 448
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1540799172 154 ELRDRHKVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRNNP 201
Cdd:COG1123 449 DLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANP 496
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1-187 |
8.98e-27 |
|
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: 101.77 E-value: 8.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAIARM-GVVrtFQHVR--LFREmTVIE-------NLLVAQHQhlksgvf 70
Cdd:cd03225 41 STLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKvGLV--FQNPDdqFFGP-TVEEevafgleNLGLPEEE------- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 71 agllktpafrraeaeALARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDH 150
Cdd:cd03225 111 ---------------IEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLE 175
|
170 180 190
....*....|....*....|....*....|....*..
gi 1540799172 151 LIVELRDRHKvSVLLIEHDMKLVMGISDRIYVVNQGT 187
Cdd:cd03225 176 LLKKLKAEGK-TIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1-192 |
5.41e-26 |
|
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: 99.52 E-value: 5.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLeglAGQAIARMGVVRTFQHVRLFREMTVIENLLVAqhqhLKsgvfagLLKTPAfr 80
Cdd:cd03259 40 TTLLRLIAGLERPDSGEILIDGRDV---TGVPPERRNIGMVFQDYALFPHLTVAENIAFG----LK------LRGVPK-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 81 raeAEALARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHK 160
Cdd:cd03259 105 ---AEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELG 181
|
170 180 190
....*....|....*....|....*....|..
gi 1540799172 161 VSVLLIEHDMKLVMGISDRIYVVNQGTPLAQG 192
Cdd:cd03259 182 ITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1-198 |
6.48e-26 |
|
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: 99.50 E-value: 6.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAIARMGVVrtFQHVRLFREMTVIENL-LVAQhqhLKsgvfaGLLKTPAF 79
Cdd:cd03263 42 TTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC--PQFDALFDELTVREHLrFYAR---LK-----GLPKSEIK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 80 RRAEAEalaraaewLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRH 159
Cdd:cd03263 112 EEVELL--------LRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGR 183
|
170 180 190
....*....|....*....|....*....|....*....
gi 1540799172 160 kvSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIR 198
Cdd:cd03263 184 --SIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-201 |
7.25e-26 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 102.10 E-value: 7.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAgqAIAR-MGVVrtFQHVRLFREMTVIENllVAqhqhlksgvFaGL--LKTP 77
Cdd:COG3842 45 TTLLRMIAGFETPDSGRILLDGRDVTGLP--PEKRnVGMV--FQDYALFPHLTVAEN--VA---------F-GLrmRGVP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 78 AfrraeAEALARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRD 157
Cdd:COG3842 109 K-----AEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQR 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1540799172 158 RHKVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRNNP 201
Cdd:COG3842 184 ELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERP 227
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1-187 |
1.70e-25 |
|
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: 97.26 E-value: 1.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAIA---RMGVVrtFQHVRLFREMTVIENLlvaqhQHLKSGvfagllktp 77
Cdd:cd03229 40 STLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPlrrRIGMV--FQDFALFPHLTVLENI-----ALGLSG--------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 78 afrraeaealaraaewlervgllsmanrsagnlayGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRD 157
Cdd:cd03229 104 -----------------------------------GQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQA 148
|
170 180 190
....*....|....*....|....*....|
gi 1540799172 158 RHKVSVLLIEHDMKLVMGISDRIYVVNQGT 187
Cdd:cd03229 149 QLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
93-207 |
2.48e-25 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 99.45 E-value: 2.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 93 WLERVGL-LSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVLLIEHDMK 171
Cdd:TIGR04521 125 ALELVGLdEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSME 204
|
90 100 110
....*....|....*....|....*....|....*.
gi 1540799172 172 LVMGISDRIYVVNQGTPLAQGTPAEIRNNPDVIRAY 207
Cdd:TIGR04521 205 DVAEYADRVIVMHKGKIVLDGTPREVFSDVDELEKI 240
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1-186 |
5.00e-25 |
|
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: 97.18 E-value: 5.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAIAR-----MGVVrtFQHVRLFREMTVIENLLVAQHqhlksgvFAGLLK 75
Cdd:cd03255 44 STLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAfrrrhIGFV--FQSFNLLPDLTALENVELPLL-------LAGVPK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 76 TPAfrraeaeaLARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVEL 155
Cdd:cd03255 115 KER--------RERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLREL 186
|
170 180 190
....*....|....*....|....*....|.
gi 1540799172 156 RDRHKVSVLLIEHDMKLVmGISDRIYVVNQG 186
Cdd:cd03255 187 NKEAGTTIVVVTHDPELA-EYADRIIELRDG 216
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1-198 |
6.50e-25 |
|
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: 97.06 E-value: 6.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAIARMGVVrtFQHVRLFREMTVIENLLVaqhqhlksgvFAGLLKTPafr 80
Cdd:cd03265 40 TTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIV--FQDLSVDDELTGWENLYI----------HARLYGVP--- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 81 raEAEALARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHK 160
Cdd:cd03265 105 --GAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFG 182
|
170 180 190
....*....|....*....|....*....|....*...
gi 1540799172 161 VSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIR 198
Cdd:cd03265 183 MTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1-201 |
1.53e-24 |
|
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: 96.15 E-value: 1.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAgqaIARMGVVRTFQHVRLFREMTVIENLLVAqhqhLKsgvfagLLKTPAfr 80
Cdd:cd03300 40 TTLLRLIAGFETPTSGEILLDGKDITNLP---PHKRPVNTVFQNYALFPHLTVFENIAFG----LR------LKKLPK-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 81 raeAEALARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDeldHLIVELRDRHK 160
Cdd:cd03300 105 ---AEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRK---DMQLELKRLQK 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1540799172 161 ---VSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRNNP 201
Cdd:cd03300 179 elgITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEP 222
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-197 |
1.57e-24 |
|
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: 96.65 E-value: 1.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAIAR-MGVVrtFQHVRLFREMTVIENLLVAQHQHLKsgvfagllktpAF 79
Cdd:COG1120 41 STLLRALAGLLKPSSGEVLLDGRDLASLSRRELARrIAYV--PQEPPAPFGLTVRELVALGRYPHLG-----------LF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 80 RRAEAEALARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRH 159
Cdd:COG1120 108 GRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARER 187
|
170 180 190
....*....|....*....|....*....|....*...
gi 1540799172 160 KVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEI 197
Cdd:COG1120 188 GRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-205 |
1.75e-24 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 96.60 E-value: 1.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAI----ARMGVVrtFQHVRLFREMTVIENLL---VAQHQHLKS--GVFA 71
Cdd:TIGR02315 42 STLLRCINRLVEPSSGSILLEGTDITKLRGKKLrklrRRIGMI--FQHYNLIERLTVLENVLhgrLGYKPTWRSllGRFS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 72 GLLKTPAFRRaeaealaraaewLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHL 151
Cdd:TIGR02315 120 EEDKERALSA------------LERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDY 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1540799172 152 IVELRDRHKVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIrnNPDVIR 205
Cdd:TIGR02315 188 LKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL--DDEVLR 239
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1-186 |
1.84e-24 |
|
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: 94.39 E-value: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAIARMGVVrtFQHVRLFREMTVIENLLvaqhqhlksgvfagllktpafr 80
Cdd:cd03230 40 TTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYL--PEEPSLYENLTVRENLK---------------------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 81 raeaealaraaewlervglLSManrsagnlayGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHK 160
Cdd:cd03230 96 -------------------LSG----------GMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKEGK 146
|
170 180
....*....|....*....|....*.
gi 1540799172 161 vSVLLIEHDMKLVMGISDRIYVVNQG 186
Cdd:cd03230 147 -TILLSSHILEEAERLCDRVAILNNG 171
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-202 |
1.86e-24 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 98.57 E-value: 1.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAiaR-MGVVrtFQHVRLFREMTVIENllVAQHQHLKSGVFAGLLKTpaf 79
Cdd:TIGR03265 44 TTLLRIIAGLERQTAGTIYQGGRDITRLPPQK--RdYGIV--FQSYALFPNLTVADN--IAYGLKNRGMGRAEVAER--- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 80 rraeaealarAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRH 159
Cdd:TIGR03265 115 ----------VAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1540799172 160 KVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRNNPD 202
Cdd:TIGR03265 185 GVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPA 227
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-211 |
4.16e-24 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 95.51 E-value: 4.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAI----ARMGVVrtFQHVRLFREMTVIENLLV---AQHQHLKS--GVFA 71
Cdd:COG3638 43 STLLRCLNGLVEPTSGEILVDGQDVTALRGRALrrlrRRIGMI--FQQFNLVPRLSVLTNVLAgrlGRTSTWRSllGLFP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 72 GLLKTPAFRRaeaealaraaewLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHL 151
Cdd:COG3638 121 PEDRERALEA------------LERVGLADKAYQRADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDL 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 152 IVELRDRHKVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIrnNPDVIRAYLGEE 211
Cdd:COG3638 189 LRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL--TDAVLREIYGGE 246
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
94-192 |
6.17e-24 |
|
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: 94.14 E-value: 6.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 94 LERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKvSVLLIEHDMKLV 173
Cdd:cd03235 117 LERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGM-TILVVTHDLGLV 195
|
90
....*....|....*....
gi 1540799172 174 MGISDRIYVVNqGTPLAQG 192
Cdd:cd03235 196 LEYFDRVLLLN-RTVVASG 213
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-211 |
7.09e-24 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 94.96 E-value: 7.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAIARMGVVRTFQHVRLFREMTVIENLL-VAQHQHlksgvfagllktpaf 79
Cdd:PRK10895 43 TTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYLPQEASIFRRLSVYDNLMaVLQIRD--------------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 80 RRAEAEALARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRh 159
Cdd:PRK10895 108 DLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDS- 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1540799172 160 KVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRNNPDVIRAYLGEE 211
Cdd:PRK10895 187 GLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYLGED 238
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
94-204 |
1.87e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 94.73 E-value: 1.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 94 LERVGL--LSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVLLIEHDMK 171
Cdd:PRK13637 127 MNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSME 206
|
90 100 110
....*....|....*....|....*....|...
gi 1540799172 172 LVMGISDRIYVVNQGTPLAQGTPAEIRNNPDVI 204
Cdd:PRK13637 207 DVAKLADRIIVMNKGKCELQGTPREVFKEVETL 239
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-201 |
1.93e-23 |
|
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: 93.56 E-value: 1.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQaiaRMGVVRTFQHVRLFREMTVIENllVAqhqhlksgvFAGLLKTPAFR 80
Cdd:cd03296 42 TTLLRLIAGLERPDSGTILFGGEDATDVPVQ---ERNVGFVFQHYALFRHMTVFDN--VA---------FGLRVKPRSER 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 81 RAEAEALARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHK 160
Cdd:cd03296 108 PPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELH 187
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1540799172 161 VSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRNNP 201
Cdd:cd03296 188 VTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHP 228
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1-138 |
2.07e-23 |
|
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: 91.17 E-value: 2.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAI-ARMGVVrtFQHVRLFREMTVIENLLVAQHqhlksgvFAGLLKTPAf 79
Cdd:pfam00005 25 STLLKLIAGLLSPTEGTILLDGQDLTDDERKSLrKEIGYV--FQDPQLFPRLTVRENLRLGLL-------LKGLSKREK- 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1540799172 80 rraeaeaLARAAEWLERVGLLSMANRSAGN----LAYGQQRRLEIARCMVTRPELLMLDEPAA 138
Cdd:pfam00005 95 -------DARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-201 |
2.64e-23 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 95.21 E-value: 2.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKL-----------RDRhleglagqaiaRMGVVrtFQHVRLFREMTVIENllVAqhqhlksgv 69
Cdd:COG1118 42 TTLLRIIAGLETPDSGRIVLngrdlftnlppRER-----------RVGFV--FQHYALFPHMTVAEN--IA--------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 70 fAGLLKTPAFRRAEAEALARaaeWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELD 149
Cdd:COG1118 98 -FGLRVRPPSKAEIRARVEE---LLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELR 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1540799172 150 HLIVELRDRHKVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRNNP 201
Cdd:COG1118 174 RWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRP 225
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-186 |
7.54e-23 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 91.64 E-value: 7.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAIARM-----GVVrtFQHVRLFREMTVIENLLVAQhqhlksgVFAGLLK 75
Cdd:COG1136 48 STLLNILGGLDRPTSGEVLIDGQDISSLSERELARLrrrhiGFV--FQFFNLLPELTALENVALPL-------LLAGVSR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 76 TPAfrraeaeaLARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVEL 155
Cdd:COG1136 119 KER--------RERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLREL 190
|
170 180 190
....*....|....*....|....*....|.
gi 1540799172 156 RDRHKVSVLLIEHDMKLvMGISDRIYVVNQG 186
Cdd:COG1136 191 NRELGTTIVMVTHDPEL-AARADRVIRLRDG 220
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-210 |
8.49e-23 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 91.74 E-value: 8.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDrhlEGLAGQAIARMGVVRTFQHVRLFREMTVIEN----------LLVAQHQHLKSGvf 70
Cdd:COG3840 39 STLLNLIAGFLPPDSGRILWNG---QDLTALPPAERPVSMLFQENNLFPHLTVAQNiglglrpglkLTAEQRAQVEQA-- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 71 agllktpafrraeaealaraaewLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDH 150
Cdd:COG3840 114 -----------------------LERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1540799172 151 LIVELRDRHKVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEI--RNNPDVIRAYLGE 210
Cdd:COG3840 171 LVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALldGEPPPALAAYLGI 232
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-209 |
1.59e-22 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 91.21 E-value: 1.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLeGLAGQAIA----RMGVVrtFQHVRLFREMTVIENLLVAQHQHLKSGvfagllKT 76
Cdd:COG1126 41 STLLRCINLLEEPDSGTITVDGEDL-TDSKKDINklrrKVGMV--FQQFNLFPHLTVLENVTLAPIKVKKMS------KA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 77 PAfrraeaeaLARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDE-LDhLIVEL 155
Cdd:COG1126 112 EA--------EERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEvLD-VMRDL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1540799172 156 RDRHkVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRNNP--DVIRAYLG 209
Cdd:COG1126 183 AKEG-MTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPqhERTRAFLS 237
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-186 |
2.45e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 93.94 E-value: 2.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEgLAG--QAIAR-MGVVrtFQHVRLFREMTVIENLLVaqhqhlksgvfaGLLKTP 77
Cdd:COG3845 45 STLMKILYGLYQPDSGEILIDGKPVR-IRSprDAIALgIGMV--HQHFMLVPNLTVAENIVL------------GLEPTK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 78 AFRRAEAEALARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRD 157
Cdd:COG3845 110 GGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAA 189
|
170 180
....*....|....*....|....*....
gi 1540799172 158 RHKvSVLLIEHDMKLVMGISDRIYVVNQG 186
Cdd:COG3845 190 EGK-SIIFITHKLREVMAIADRVTVLRRG 217
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1-182 |
2.48e-22 |
|
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: 90.22 E-value: 2.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAgqaiARMGVVrtFQHVRLFREMTVIENLLVAqhqhLKsgvFAGLLKTPAfr 80
Cdd:cd03293 44 STLLRIIAGLERPTSGEVLVDGEPVTGPG----PDRGYV--FQQDALLPWLTVLDNVALG----LE---LQGVPKAEA-- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 81 raeaeaLARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHK 160
Cdd:cd03293 109 ------RERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETG 182
|
170 180
....*....|....*....|..
gi 1540799172 161 VSVLLIEHDMKLVMGISDRIYV 182
Cdd:cd03293 183 KTVLLVTHDIDEAVFLADRVVV 204
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-201 |
3.15e-22 |
|
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: 90.33 E-value: 3.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAG----QAIARMGVVrtFQHVRLFREMTVIENLLVAqhqhLKsgvFAGLLKT 76
Cdd:cd03258 45 STLIRCINGLERPTSGSVLVDGTDLTLLSGkelrKARRRIGMI--FQHFNLLSSRTVFENVALP----LE---IAGVPKA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 77 pafrraeaEALARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELR 156
Cdd:cd03258 116 --------EIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDIN 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1540799172 157 DRHKVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRNNP 201
Cdd:cd03258 188 RELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
93-206 |
5.13e-22 |
|
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: 93.04 E-value: 5.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 93 WLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVLLIEHDMKL 172
Cdd:COG1123 126 LLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGV 205
|
90 100 110
....*....|....*....|....*....|....
gi 1540799172 173 VMGISDRIYVVNQGTPLAQGTPAEIRNNPDVIRA 206
Cdd:COG1123 206 VAEIADRVVVMDDGRIVEDGPPEEILAAPQALAA 239
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-211 |
1.67e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 91.62 E-value: 1.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 2 TVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAIARMGVVRTFQHVRLFREMTVIENLlvaqhqhlksgvFAGLLKTPAFRR 81
Cdd:COG1129 45 TLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAGIAIIHQELNLVPNLSVAENI------------FLGREPRRGGLI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 82 AEAEALARAAEWLERVGL-LSmANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRhK 160
Cdd:COG1129 113 DWRAMRRRARELLARLGLdID-PDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQ-G 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1540799172 161 VSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIrNNPDVIRAYLGEE 211
Cdd:COG1129 191 VAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL-TEDELVRLMVGRE 240
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1-192 |
2.11e-21 |
|
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: 86.72 E-value: 2.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAIAR-MGVVRTfqhvrlfremtvienllvaqhqhlksgvfagllktpaf 79
Cdd:cd03214 39 STLLKTLAGLLKPSSGEILLDGKDLASLSPKELARkIAYVPQ-------------------------------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 80 rraeaealaraaeWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRH 159
Cdd:cd03214 81 -------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARER 147
|
170 180 190
....*....|....*....|....*....|...
gi 1540799172 160 KVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQG 192
Cdd:cd03214 148 GKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
1-201 |
6.54e-21 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 88.32 E-value: 6.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDrhlEGLAGQAIARMGVVRTFQHVRLFREMTVIENLLVAQHQHlksgvfagllKTPAfr 80
Cdd:TIGR01187 10 TTLLRLLAGFEQPDSGSIMLDG---EDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMR----------KVPR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 81 raeAEALARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHK 160
Cdd:TIGR01187 75 ---AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1540799172 161 VSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRNNP 201
Cdd:TIGR01187 152 ITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEP 192
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-211 |
1.25e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 89.07 E-value: 1.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAIARMGVVRTFQHVRLFREMTVIENLLVAQHQHLKsgVFAGLLKTPAFR 80
Cdd:PRK09700 45 STLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGIIYQELSVIDELTVLENLYIGRHLTKK--VCGVNIIDWREM 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 81 RAEAEALaraaewLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHK 160
Cdd:PRK09700 123 RVRAAMM------LLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGT 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1540799172 161 vSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRNNpDVIRAYLGEE 211
Cdd:PRK09700 197 -AIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSND-DIVRLMVGRE 245
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-169 |
1.54e-20 |
|
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: 85.22 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAIARMGVVrtFQHVRLFREMTVIENLLVAQHQHlksGVFAGLLKTPAfr 80
Cdd:COG4133 42 TTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYL--GHADGLKPELTVRENLRFWAALY---GLRADREAIDE-- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 81 raeaealaraaeWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRhK 160
Cdd:COG4133 115 ------------ALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLAR-G 181
|
....*....
gi 1540799172 161 VSVLLIEHD 169
Cdd:COG4133 182 GAVLLTTHQ 190
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-182 |
2.41e-20 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 85.91 E-value: 2.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAgqaiARMGVVrtFQHVRLFREMTVIENLLVAqhqhLKsgvFAGLLKTPAfr 80
Cdd:COG1116 51 STLLRLIAGLEKPTSGEVLVDGKPVTGPG----PDRGVV--FQEPALLPWLTVLDNVALG----LE---LRGVPKAER-- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 81 raeaeaLARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHK 160
Cdd:COG1116 116 ------RERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETG 189
|
170 180
....*....|....*....|....
gi 1540799172 161 VSVLLIEHDMK--LVMgiSDRIYV 182
Cdd:COG1116 190 KTVLFVTHDVDeaVFL--ADRVVV 211
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-202 |
4.39e-20 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 85.20 E-value: 4.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAI--ARMGVVRTFQHVRLFREMTVIENLL--VAQHQHLKsgvfAGLLKT 76
Cdd:PRK11831 47 TTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytVRKRMSMLFQSGALFTDMNVFDNVAypLREHTQLP----APLLHS 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 77 PAFRRaeaealaraaewLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELR 156
Cdd:PRK11831 123 TVMMK------------LEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELN 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1540799172 157 DRHKVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRNNPD 202
Cdd:PRK11831 191 SALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPD 236
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1-210 |
5.94e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 85.27 E-value: 5.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAG----QAI-ARMGVVRTFQHVRLFrEMTVIENLLVAQHQhlksgvfagllk 75
Cdd:PRK13641 47 STLMQHFNALLKPSSGTITIAGYHITPETGnknlKKLrKKVSLVFQFPEAQLF-ENTVLKDVEFGPKN------------ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 76 tpaFRRAEAEALARAAEWLERVGL-LSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVE 154
Cdd:PRK13641 114 ---FGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKD 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1540799172 155 LRdRHKVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRNNPD-VIRAYLGE 210
Cdd:PRK13641 191 YQ-KAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEwLKKHYLDE 246
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
2-201 |
1.25e-19 |
|
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: 84.23 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 2 TVFNCLTGFYRPSGGTI--------KLRDRHLEGLAGQaiaRMGVVrtFQHVRLFREMTVIENL---LVAQHQHLKsgvf 70
Cdd:cd03294 65 TLLRCINRLIEPTSGKVlidgqdiaAMSRKELRELRRK---KISMV--FQSFALLPHRTVLENVafgLEVQGVPRA---- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 71 agllktpafrraeaEALARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDH 150
Cdd:cd03294 136 --------------EREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQD 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1540799172 151 LIVELRDRHKVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRNNP 201
Cdd:cd03294 202 ELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNP 252
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
1-208 |
1.37e-19 |
|
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: 85.97 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAI-ARMGVVrtFQHVRLFReMTVIENLLVAQHQhlksgvfAG---LLKT 76
Cdd:COG4987 375 STLLALLLRFLDPQSGSITLGGVDLRDLDEDDLrRRIAVV--PQRPHLFD-TTLRENLRLARPD-------ATdeeLWAA 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 77 pafrraeaealaraaewLERVGLLSMANRSAGNLAY-----------GQQRRLEIARCMVTRPELLMLDEPAAGLNPKET 145
Cdd:COG4987 445 -----------------LERVGLGDWLAALPDGLDTwlgeggrrlsgGERRRLALARALLRDAPILLLDEPTEGLDAATE 507
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1540799172 146 DE-LDHLIVELRDRhkvSVLLIEHDMkLVMGISDRIYVVNQGTPLAQGTPAEIRNNPDVIRAYL 208
Cdd:COG4987 508 QAlLADLLEALAGR---TVLLITHRL-AGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLY 567
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
94-205 |
1.50e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 84.13 E-value: 1.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 94 LERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVLLIEHDMKLV 173
Cdd:PRK13636 126 LKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIV 205
|
90 100 110
....*....|....*....|....*....|..
gi 1540799172 174 MGISDRIYVVNQGTPLAQGTPAEIRNNPDVIR 205
Cdd:PRK13636 206 PLYCDNVFVMKEGRVILQGNPKEVFAEKEMLR 237
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1-197 |
2.40e-19 |
|
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: 82.61 E-value: 2.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFY-----RPSGGTIKLRDRHLEGLAGQAIA---RMGVVrtFQHVRLFReMTVIENLLVAQHQHlksgvfaG 72
Cdd:cd03260 40 STLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVDVLElrrRVGMV--FQKPNPFP-GSIYDNVAYGLRLH-------G 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 73 LLKTPAFRRAEAEAlaraaewLERVGLLSMANR--SAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDH 150
Cdd:cd03260 110 IKLKEELDERVEEA-------LRKAALWDEVKDrlHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEE 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1540799172 151 LIVELRDRHkvSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEI 197
Cdd:cd03260 183 LIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-207 |
2.87e-19 |
|
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: 82.83 E-value: 2.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRP-SGGTIKLRDRHLEGLAGQAI-ARMGVVRTFQHVRLFREMTVIENLLvaqhqhlkSGVFA--GLLKT 76
Cdd:COG1119 43 STLLSLITGDLPPtYGNDVRLFGERRGGEDVWELrKRIGLVSPALQLRFPRDETVLDVVL--------SGFFDsiGLYRE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 77 PafrraEAEALARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELR 156
Cdd:COG1119 115 P-----TDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLA 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1540799172 157 DRHKVSVLLIEHDMK-LVMGISDRIyVVNQGTPLAQGTPAEIRNNPDVIRAY 207
Cdd:COG1119 190 AEGAPTLVLVTHHVEeIPPGITHVL-LLKDGRVVAAGPKEEVLTSENLSEAF 240
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-201 |
3.02e-19 |
|
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: 82.54 E-value: 3.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAIAR-MGVVrtFQHVR--LFREMTVIEnllvaqhqhlksgvfagLLKTP 77
Cdd:COG1124 45 STLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRrVQMV--FQDPYasLHPRHTVDR-----------------ILAEP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 78 AFRRAEAEALARAAEWLERVGL-LSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELR 156
Cdd:COG1124 106 LRIHGLPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLR 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1540799172 157 DRHKVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRNNP 201
Cdd:COG1124 186 EERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGP 230
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-205 |
4.24e-19 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 82.32 E-value: 4.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLA---GQ---------AIARMGVVRTFQHVRLFREMTVIENLLVAQHQHLksg 68
Cdd:PRK10619 45 STFLRCINFLEKPSEGSIVVNGQTINLVRdkdGQlkvadknqlRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVL--- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 69 vfaGLLKTPAfrraeaeaLARAAEWLERVGLLSMAN-RSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDE 147
Cdd:PRK10619 122 ---GLSKQEA--------RERAVKYLAKVGIDERAQgKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGE 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1540799172 148 LDHLIVELRDRHKVSVlLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRNNPDVIR 205
Cdd:PRK10619 191 VLRIMQQLAEEGKTMV-VVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPR 247
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
94-205 |
6.06e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 82.43 E-value: 6.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 94 LERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELrDRHKVSVLLIEHDMKLV 173
Cdd:PRK13639 122 LKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDL-NKEGITIIISTHDVDLV 200
|
90 100 110
....*....|....*....|....*....|..
gi 1540799172 174 MGISDRIYVVNQGTPLAQGTPAEIRNNPDVIR 205
Cdd:PRK13639 201 PVYADKVYVMSDGKIIKEGTPKEVFSDIETIR 232
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-211 |
7.72e-19 |
|
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: 83.23 E-value: 7.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHL-EGLAGQAIA----RMGVVrtFQHVRLFREMTVIENLLVAQHQHLKSGvfagllK 75
Cdd:COG4148 39 TTLLRAIAGLERPDSGRIRLGGEVLqDSARGIFLPphrrRIGYV--FQEARLFPHLSVRGNLLYGRKRAPRAE------R 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 76 TPAFRRaeaealaraaeWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVEL 155
Cdd:COG4148 111 RISFDE-----------VVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1540799172 156 RDRHKVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRNNPDVIRAYLGEE 211
Cdd:COG4148 180 RDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEE 235
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1-192 |
1.06e-18 |
|
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: 80.40 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAIARMGVVRTfqhvrLFREMTVIENLLvaqhqHLKSgvFAGLLKTPAfr 80
Cdd:cd03269 40 TTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGYLPEERG-----LYPKMKVIDQLV-----YLAQ--LKGLKKEEA-- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 81 raeaeaLARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHK 160
Cdd:cd03269 106 ------RRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGK 179
|
170 180 190
....*....|....*....|....*....|..
gi 1540799172 161 vSVLLIEHDMKLVMGISDRIYVVNQGTPLAQG 192
Cdd:cd03269 180 -TVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1-186 |
1.10e-18 |
|
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: 80.27 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGlAGQAI----ARMGVVrtFQHVRLFREMTVIENLLVAQHQHLksgvfaGLLKT 76
Cdd:cd03262 40 STLLRCINLLEEPDSGTIIIDGLKLTD-DKKNInelrQKVGMV--FQQFNLFPHLTVLENITLAPIKVK------GMSKA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 77 PAfrraeaeaLARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELR 156
Cdd:cd03262 111 EA--------EERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLA 182
|
170 180 190
....*....|....*....|....*....|
gi 1540799172 157 dRHKVSVLLIEHDMKLVMGISDRIYVVNQG 186
Cdd:cd03262 183 -EEGMTMVVVTHEMGFAREVADRVIFMDDG 211
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-186 |
1.25e-18 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 80.48 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAIA----RMGVVrtFQHVRLFREMTVIENLLVA------QHQHLKSGVF 70
Cdd:COG2884 42 STLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPylrrRIGVV--FQDFRLLPDRTVYENVALPlrvtgkSRKEIRRRVR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 71 AgllktpafrraeaealaraaeWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDH 150
Cdd:COG2884 120 E---------------------VLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIME 178
|
170 180 190
....*....|....*....|....*....|....*.
gi 1540799172 151 LIVELRdRHKVSVLLIEHDMKLVMGISDRIYVVNQG 186
Cdd:COG2884 179 LLEEIN-RRGTTVLIATHDLELVDRMPKRVLELEDG 213
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-199 |
1.27e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 81.69 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAIARM----GvvrtfqhvrLFREMTVIENLL-VAQhqhLKsgvfaGLLK 75
Cdd:COG4152 41 TTTIRIILGILAPDSGEVLWDGEPLDPEDRRRIGYLpeerG---------LYPKMKVGEQLVyLAR---LK-----GLSK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 76 TPAfrraeaeaLARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVEL 155
Cdd:COG4152 104 AEA--------KRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIREL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1540799172 156 RDRhKVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRN 199
Cdd:COG4152 176 AAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRR 218
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
93-202 |
1.61e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 81.60 E-value: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 93 WLERVGL-LSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVLLIEHDMK 171
Cdd:PRK13634 128 MIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSME 207
|
90 100 110
....*....|....*....|....*....|.
gi 1540799172 172 LVMGISDRIYVVNQGTPLAQGTPAEIRNNPD 202
Cdd:PRK13634 208 DAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
93-204 |
1.78e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 81.82 E-value: 1.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 93 WLERVGL-LSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKvSVLLIEHDMK 171
Cdd:PRK13631 159 YLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNK-TVFVITHTME 237
|
90 100 110
....*....|....*....|....*....|...
gi 1540799172 172 LVMGISDRIYVVNQGTPLAQGTPAEIRNNPDVI 204
Cdd:PRK13631 238 HVLEVADEVIVMDKGKILKTGTPYEIFTDQHII 270
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-207 |
1.91e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 81.39 E-value: 1.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAIARMGVVRTFQHvrLFREMTVIENLLV-AQHQHLKSGVFAGLLKTpaf 79
Cdd:PRK13537 47 TTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVPQFDN--LDPDFTVRENLLVfGRYFGLSAAAARALVPP--- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 80 rraeaealaraaeWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETdeldHLIVE----L 155
Cdd:PRK13537 122 -------------LLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQAR----HLMWErlrsL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1540799172 156 RDRHKvSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRNNP---DVIRAY 207
Cdd:PRK13537 185 LARGK-TILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEigcDVIEIY 238
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
10-211 |
3.05e-18 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes 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 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. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 81.44 E-value: 3.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 10 FYRPSGG----TIKLRDRHLEGLAGQ-----------------AIARMGVVRTFQHVRLFREMTVIENLLVAQHqhlksg 68
Cdd:TIGR01186 24 IMGLSGSgkstTVRMLNRLIEPTAGQifidgenimkqspvelrEVRRKKIGMVFQQFALFPHMTILQNTSLGPE------ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 69 vfagLLKTPAfrraeAEALARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDEL 148
Cdd:TIGR01186 98 ----LLGWPE-----QERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLIRDSM 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1540799172 149 DHLIVELRDRHKVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRNNP--DVIRAYLGEE 211
Cdd:TIGR01186 169 QDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPanEYVEEFIGKV 233
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1-192 |
7.46e-18 |
|
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: 78.03 E-value: 7.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGqAIARMGVVRTFQHvrLFREMTVIENLLVAQHQHLKSgvfagllktpafr 80
Cdd:cd03268 40 TTTMKIILGLIKPDSGEITFDGKSYQKNIE-ALRRIGALIEAPG--FYPNLTARENLRLLARLLGIR------------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 81 raeaeaLARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHK 160
Cdd:cd03268 104 ------KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQGI 177
|
170 180 190
....*....|....*....|....*....|..
gi 1540799172 161 vSVLLIEHDMKLVMGISDRIYVVNQGTPLAQG 192
Cdd:cd03268 178 -TVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
110-187 |
7.68e-18 |
|
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: 76.90 E-value: 7.68e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1540799172 110 LAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKvSVLLIEHDMKLVMGISDRIYVVNQGT 187
Cdd:cd00267 81 LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGR-TVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
110-187 |
8.46e-18 |
|
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: 76.70 E-value: 8.46e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1540799172 110 LAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHkVSVLLIEHDMKLVMGISDRIYVVNQGT 187
Cdd:cd03216 83 LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQG-VAVIFISHRLDEVFEIADRVTVLRDGR 159
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-201 |
8.82e-18 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 80.26 E-value: 8.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLA--GQAIARMgvvrtFQHVRLFREMTVIENLLVAQHQHlksgvfagllKTPa 78
Cdd:PRK11607 59 STLLRMLAGFEQPTAGQIMLDGVDLSHVPpyQRPINMM-----FQSYALFPHMTVEQNIAFGLKQD----------KLP- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 79 frraEAEALARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDR 158
Cdd:PRK11607 123 ----KAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILER 198
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1540799172 159 HKVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRNNP 201
Cdd:PRK11607 199 VGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHP 241
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
1-186 |
1.29e-17 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 77.59 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGqaiARMGVVRTFQHVRLFREMTVIENLLVAQHQHLKsgvfagllktpafr 80
Cdd:TIGR01277 38 STLLNLIAGFIEPASGSIKVNDQSHTGLAP---YQRPVSMLFQENNLFAHLTVRQNIGLGLHPGLK-------------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 81 rAEAEALARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHK 160
Cdd:TIGR01277 101 -LNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSERQ 179
|
170 180
....*....|....*....|....*.
gi 1540799172 161 VSVLLIEHDMKLVMGISDRIYVVNQG 186
Cdd:TIGR01277 180 RTLLMVTHHLSDARAIASQIAVVSQG 205
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1-192 |
2.05e-17 |
|
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: 76.95 E-value: 2.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAIA-----RMGVVrtFQHVRLFREMTVIENLLVAQHQHLKSgvfagllk 75
Cdd:cd03297 37 STLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLppqqrKIGLV--FQQYALFPHLNVRENLAFGLKRKRNR-------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 76 tpafrraeaEALARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLnpkETDELDHLIVEL 155
Cdd:cd03297 107 ---------EDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSAL---DRALRLQLLPEL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1540799172 156 RDRHK---VSVLLIEHDMKLVMGISDRIYVVNQGTPLAQG 192
Cdd:cd03297 175 KQIKKnlnIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1-201 |
3.41e-17 |
|
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: 76.99 E-value: 3.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQaiaRMGVVRTFQHVRLFREMTVIENLLVAQHQHL--KSGVFAGLLKTPA 78
Cdd:cd03299 39 SVLLETIAGFIKPDSGKILLNGKDITNLPPE---KRDISYVPQNYALFPHMTVYKNIAYGLKKRKvdKKEIERKVLEIAE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 79 FrraeaealaraaewlerVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDR 158
Cdd:cd03299 116 M-----------------LGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1540799172 159 HKVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRNNP 201
Cdd:cd03299 179 FGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKP 221
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-186 |
3.56e-17 |
|
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: 76.78 E-value: 3.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAIARMGvvRTFQHVrlFRE--------MTVIENLLVAQHQHLKsgvfag 72
Cdd:cd03257 45 STLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRR--KEIQMV--FQDpmsslnprMTIGEQIAEPLRIHGK------ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 73 lLKTPAFRRAEAEALaraaewLERVGLLS-MANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHL 151
Cdd:cd03257 115 -LSKKEARKEAVLLL------LVGVGLPEeVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDL 187
|
170 180 190
....*....|....*....|....*....|....*
gi 1540799172 152 IVELRDRHKVSVLLIEHDMKLVMGISDRIYVVNQG 186
Cdd:cd03257 188 LKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAG 222
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-207 |
3.78e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 77.85 E-value: 3.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQ-----AIARMGVVRTFQHVRLFREmTVIENLLVAQHQHlksgvfaGLLK 75
Cdd:PRK13643 46 STLLQHLNGLLQPTEGKVTVGDIVVSSTSKQkeikpVRKKVGVVFQFPESQLFEE-TVLKDVAFGPQNF-------GIPK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 76 TPAfrraeaeaLARAAEWLERVGLL-SMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVE 154
Cdd:PRK13643 118 EKA--------EKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFES 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1540799172 155 LRDRHKvSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRNNPDVIRAY 207
Cdd:PRK13643 190 IHQSGQ-TVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDFLKAH 241
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
94-205 |
3.88e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 77.54 E-value: 3.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 94 LERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVLLIEHDMKLV 173
Cdd:PRK13652 122 LHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLV 201
|
90 100 110
....*....|....*....|....*....|..
gi 1540799172 174 MGISDRIYVVNQGTPLAQGTPAEIRNNPDVIR 205
Cdd:PRK13652 202 PEMADYIYVMDKGRIVAYGTVEEIFLQPDLLA 233
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
14-201 |
4.36e-17 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 78.20 E-value: 4.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 14 SGGTIKLR-----DRHLEG---LAGQAIARM-------GVVrtFQHVRLFREMTVIENL-----LVAQHQHLKSGVfagl 73
Cdd:PRK10851 39 SGKTTLLRiiaglEHQTSGhirFHGTDVSRLhardrkvGFV--FQHYALFRHMTVFDNIafgltVLPRRERPNAAA---- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 74 LKTPAfrraeaealaraAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIV 153
Cdd:PRK10851 113 IKAKV------------TQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLR 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1540799172 154 ELRDRHKVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRNNP 201
Cdd:PRK10851 181 QLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP 228
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1-196 |
4.41e-17 |
|
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: 78.65 E-value: 4.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAI-ARMGVVRtfQHVRLFrEMTVIENLLVAQHQHlksgvfagllkTPAf 79
Cdd:COG4988 377 STLLNLLLGFLPPYSGSILINGVDLSDLDPASWrRQIAWVP--QNPYLF-AGTIRENLRLGRPDA-----------SDE- 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 80 rraeaealaRAAEWLERVGLLSMANR-----------SAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDEL 148
Cdd:COG4988 442 ---------ELEAALEAAGLDEFVAAlpdgldtplgeGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEI 512
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1540799172 149 DHLIVELRDRHkvSVLLIEHDMKLVMgISDRIYVVNQGTPLAQGTPAE 196
Cdd:COG4988 513 LQALRRLAKGR--TVILITHRLALLA-QADRILVLDDGRIVEQGTHEE 557
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1-186 |
6.53e-17 |
|
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: 74.73 E-value: 6.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAI-ARMGVVrtFQHVRLFrEMTVIENLLvaqhqhlkSGvfagllktpaf 79
Cdd:cd03228 42 STLLKLLLRLYDPTSGEILIDGVDLRDLDLESLrKNIAYV--PQDPFLF-SGTIRENIL--------SG----------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 80 rraeaealaraaewlervgllsmanrsagnlayGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRH 159
Cdd:cd03228 100 ---------------------------------GQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAKGK 146
|
170 180
....*....|....*....|....*..
gi 1540799172 160 kvSVLLIEHDMKLVMgISDRIYVVNQG 186
Cdd:cd03228 147 --TVIVIAHRLSTIR-DADRIIVLDDG 170
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
95-205 |
7.82e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 76.57 E-value: 7.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 95 ERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVLLIEHDMKLVM 174
Cdd:PRK13632 128 KKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI 207
|
90 100 110
....*....|....*....|....*....|.
gi 1540799172 175 gISDRIYVVNQGTPLAQGTPAEIRNNPDVIR 205
Cdd:PRK13632 208 -LADKVIVFSEGKLIAQGKPKEILNNKEILE 237
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-211 |
1.64e-16 |
|
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: 75.03 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 4 FNCLTGfyrPSGG----TIKLRDRHLEG------LAGQAIARMGVVR-------TFQHVRLFREMTVIENL-LVAQhqhl 65
Cdd:cd03295 29 FLVLIG---PSGSgkttTMKMINRLIEPtsgeifIDGEDIREQDPVElrrkigyVIQQIGLFPHMTVEENIaLVPK---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 66 ksgvfagLLKTPafrraEAEALARAAEWLERVGL--LSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPK 143
Cdd:cd03295 102 -------LLKWP-----KEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPI 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 144 ETDELDHLIVELRDRHKVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRNNP--DVIRAYLGEE 211
Cdd:cd03295 170 TRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPanDFVAEFVGAD 239
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-201 |
1.80e-16 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 76.52 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQaiaRMGVVRTFQHVRLFREMTVIENllVAQHQHLKsgvfagllKTPAfr 80
Cdd:PRK09452 54 TTVLRLIAGFETPDSGRIMLDGQDITHVPAE---NRHVNTVFQSYALFPHMTVFEN--VAFGLRMQ--------KTPA-- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 81 raeAEALARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHK 160
Cdd:PRK09452 119 ---AEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLG 195
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1540799172 161 VSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRNNP 201
Cdd:PRK09452 196 ITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEP 236
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
31-208 |
3.15e-16 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 76.23 E-value: 3.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 31 QAIARMGVVRTFQHVRLFREMTVIENLLVAQHQhlkSGVFAGLLKTPAFRRaeaealaraaewLERVGLLSMANRSAGNL 110
Cdd:PRK10070 101 REVRRKKIAMVFQSFALMPHMTVLDNTAFGMEL---AGINAEERREKALDA------------LRQVGLENYAHSYPDEL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 111 AYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVLLIEHDMKLVMGISDRIYVVNQGTPLA 190
Cdd:PRK10070 166 SGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQ 245
|
170 180
....*....|....*....|
gi 1540799172 191 QGTPAEIRNNP--DVIRAYL 208
Cdd:PRK10070 246 VGTPDEILNNPanDYVRTFF 265
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-201 |
3.33e-16 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 75.49 E-value: 3.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAgqAIAR-MGVVrtFQHVRLFREMTVIENLLVAqhqhLKsgvfagLLKTPAf 79
Cdd:COG3839 43 STLLRMIAGLEDPTSGEILIGGRDVTDLP--PKDRnIAMV--FQSYALYPHMTVYENIAFP----LK------LRKVPK- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 80 rraeAEALARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRH 159
Cdd:COG3839 108 ----AEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1540799172 160 KVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRNNP 201
Cdd:COG3839 184 GTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRP 225
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
94-197 |
3.71e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 74.67 E-value: 3.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 94 LERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVLLIEHDMKLV 173
Cdd:PRK13635 125 LRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA 204
|
90 100
....*....|....*....|....
gi 1540799172 174 MGiSDRIYVVNQGTPLAQGTPAEI 197
Cdd:PRK13635 205 AQ-ADRVIVMNKGEILEEGTPEEI 227
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-210 |
7.85e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 74.48 E-value: 7.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAIARMGVVRTFQhvRLFREMTVIENLLVAQHQhlksgvfagllktpaFR 80
Cdd:PRK13536 81 STIARMILGMTSPDAGKITVLGVPVPARARLARARIGVVPQFD--NLDLEFTVRENLLVFGRY---------------FG 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 81 RAEAEALARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETdeldHLIVE----LR 156
Cdd:PRK13536 144 MSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHAR----HLIWErlrsLL 219
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1540799172 157 DRHKvSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRNNP---DVIRAYLGE 210
Cdd:PRK13536 220 ARGK-TILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHigcQVIEIYGGD 275
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
94-206 |
9.02e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 73.62 E-value: 9.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 94 LERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKvSVLLIEHDMKLV 173
Cdd:PRK13647 123 LKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGK-TVIVATHDVDLA 201
|
90 100 110
....*....|....*....|....*....|...
gi 1540799172 174 MGISDRIYVVNQGTPLAQGTPaEIRNNPDVIRA 206
Cdd:PRK13647 202 AEWADQVIVLKEGRVLAEGDK-SLLTDEDIVEQ 233
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1-186 |
9.04e-16 |
|
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: 72.88 E-value: 9.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRdrhleglaGQAIARMGVVR--TFQHVRLFREMTVIENLLVAQHQhlksgVFAGLLKTpa 78
Cdd:TIGR01184 25 STLLNLISGLAQPTSGGVILE--------GKQITEPGPDRmvVFQNYSLLPWLTVRENIALAVDR-----VLPDLSKS-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 79 frraeaEALARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDR 158
Cdd:TIGR01184 90 ------ERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQIWEE 163
|
170 180
....*....|....*....|....*...
gi 1540799172 159 HKVSVLLIEHDMKLVMGISDRIYVVNQG 186
Cdd:TIGR01184 164 HRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-201 |
1.06e-15 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 73.96 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 6 CLTGFYRPSGGTIKLRDRHLEGLAGQAI--AR--MGVVrtFQHVRLFREMTVIENllVAqhqhlksgvF----AGL---- 73
Cdd:COG1135 50 CINLLERPTSGSVLVDGVDLTALSERELraARrkIGMI--FQHFNLLSSRTVAEN--VA---------LpleiAGVpkae 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 74 -------LktpafrraeaealaraaewLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETD 146
Cdd:COG1135 117 irkrvaeL-------------------LELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTR 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1540799172 147 E-LDhLIVELRDRHKVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRNNP 201
Cdd:COG1135 178 SiLD-LLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANP 232
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
94-205 |
1.20e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 73.30 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 94 LERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVLLIEHDMKLV 173
Cdd:PRK13640 128 LADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA 207
|
90 100 110
....*....|....*....|....*....|..
gi 1540799172 174 MGiSDRIYVVNQGTPLAQGTPAEIRNNPDVIR 205
Cdd:PRK13640 208 NM-ADQVLVLDDGKLLAQGSPVEIFSKVEMLK 238
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1-192 |
1.30e-15 |
|
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: 72.23 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAIARMGVVRtfQHVRLFREMTVIENLlvaQHQHLKSGVFAGLLKtpafr 80
Cdd:cd03264 39 TTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLP--QEFGVYPNFTVREFL---DYIAWLKGIPSKEVK----- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 81 raeaealARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVEL-RDRh 159
Cdd:cd03264 109 -------ARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELgEDR- 180
|
170 180 190
....*....|....*....|....*....|...
gi 1540799172 160 kvSVLLIEHDMKLVMGISDRIYVVNQGTPLAQG 192
Cdd:cd03264 181 --IVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1-199 |
1.60e-15 |
|
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: 74.49 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIK-----LRDRHLEGLAGQaiarMGVVrtFQHVRLFrEMTVIENLLVAQHQHLKSGVFAgllk 75
Cdd:COG2274 515 STLLKLLLGLYEPTSGRILidgidLRQIDPASLRRQ----IGVV--LQDVFLF-SGTIRENITLGDPDATDEEIIE---- 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 76 tpafrraeaealaraaeWLERVGLLSMANR-----------SAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKE 144
Cdd:COG2274 584 -----------------AARLAGLHDFIEAlpmgydtvvgeGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAET 646
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1540799172 145 TDELDHLIVELrdRHKVSVLLIEHDMKLVMgISDRIYVVNQGTPLAQGTPAEIRN 199
Cdd:COG2274 647 EAIILENLRRL--LKGRTVIIIAHRLSTIR-LADRIIVLDKGRIVEDGTHEELLA 698
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
94-197 |
1.89e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 72.86 E-value: 1.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 94 LERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVLLIEHDMKLV 173
Cdd:PRK13648 127 LKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEA 206
|
90 100
....*....|....*....|....
gi 1540799172 174 MGiSDRIYVVNQGTPLAQGTPAEI 197
Cdd:PRK13648 207 ME-ADHVIVMNKGTVYKEGTPTEI 229
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
35-211 |
2.16e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 73.81 E-value: 2.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 35 RMGVVRTFQHVRLFREMTVIENLlvaqhqhlksgvFAGLLKTPAFRRAEAEALARAAEWLERVGLLSMANRSAGNLAYGQ 114
Cdd:PRK13549 81 RAGIAIIHQELALVKELSVLENI------------FLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQ 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 115 QRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRdRHKVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQgTP 194
Cdd:PRK13549 149 QQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLK-AHGIACIYISHKLNEVKAISDTICVIRDGRHIGT-RP 226
|
170
....*....|....*..
gi 1540799172 195 AEIRNNPDVIRAYLGEE 211
Cdd:PRK13549 227 AAGMTEDDIITMMVGRE 243
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
94-201 |
2.26e-15 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 73.95 E-value: 2.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 94 LERVGLL-SMANRsagnlaY------GQQRRLEIARCMVTRPELLMLDEPaaglnpkeTDELD--------HLIVELRDR 158
Cdd:COG4172 409 LEEVGLDpAARHR------YphefsgGQRQRIAIARALILEPKLLVLDEP--------TSALDvsvqaqilDLLRDLQRE 474
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1540799172 159 HKVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRNNP 201
Cdd:COG4172 475 HGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAP 517
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
110-197 |
3.11e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 72.35 E-value: 3.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 110 LAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVEL--RDRHkvsVLLIEHDMKLVMGISDRIYVVNQGT 187
Cdd:PRK13638 137 LSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIvaQGNH---VIISSHDIDLIYEISDAVYVLRQGQ 213
|
90
....*....|
gi 1540799172 188 PLAQGTPAEI 197
Cdd:PRK13638 214 ILTHGAPGEV 223
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1-192 |
3.94e-15 |
|
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: 70.98 E-value: 3.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLrdrHLEGLAGQAIARMGVVRTFQHVRLFREMTVIENLlvaqhqhlksgvfaGLLKTPAFR 80
Cdd:cd03298 38 STLLNLIAGFETPQSGRVLI---NGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNV--------------GLGLSPGLK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 81 RAEAEALARAAEwLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHK 160
Cdd:cd03298 101 LTAEDRQAIEVA-LARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETK 179
|
170 180 190
....*....|....*....|....*....|..
gi 1540799172 161 VSVLLIEHDMKLVMGISDRIYVVNQGTPLAQG 192
Cdd:cd03298 180 MTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
103-204 |
5.11e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 71.96 E-value: 5.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 103 ANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVLLIEHDMKLVMGISDRIYV 182
Cdd:PRK13645 144 VKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIV 223
|
90 100
....*....|....*....|..
gi 1540799172 183 VNQGTPLAQGTPAEIRNNPDVI 204
Cdd:PRK13645 224 MHEGKVISIGSPFEIFSNQELL 245
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-209 |
6.34e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 70.68 E-value: 6.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAIARMGVVRTFQHVRLFREMTVIENLLVAqhqhlksGVFAgllktpafr 80
Cdd:PRK11614 45 TTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIVPEGRRVFSRMTVEENLAMG-------GFFA--------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 81 raeaeALARAAEWLERV-----GLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVEL 155
Cdd:PRK11614 109 -----ERDQFQERIKWVyelfpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1540799172 156 RDRhKVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRNNPDVIRAYLG 209
Cdd:PRK11614 184 REQ-GMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAYLG 236
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-211 |
6.51e-15 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 72.55 E-value: 6.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYrPSG---GTIKLRDRHLEGLAGQAIARMGVVRTFQHVRLFREMTVIENLLVAQHQHLKsgvfAGLLKTP 77
Cdd:TIGR02633 41 STLMKILSGVY-PHGtwdGEIYWSGSPLKASNIRDTERAGIVIIHQELTLVPELSVAENIFLGNEITLP----GGRMAYN 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 78 AFRRAEAEAlaraaewLERVGLLSMAN-RSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELR 156
Cdd:TIGR02633 116 AMYLRAKNL-------LRELQLDADNVtRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLK 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1540799172 157 dRHKVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQgTPAEIRNNPDVIRAYLGEE 211
Cdd:TIGR02633 189 -AHGVACVYISHKLNEVKAVCDTICVIRDGQHVAT-KDMSTMSEDDIITMMVGRE 241
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
104-201 |
1.00e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 70.84 E-value: 1.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 104 NRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVLLIEHDMKLVMGISD--RIY 181
Cdd:PRK14258 145 HKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDftAFF 224
|
90 100
....*....|....*....|...
gi 1540799172 182 VVNQ---GTPLAQGTPAEIRNNP 201
Cdd:PRK14258 225 KGNEnriGQLVEFGLTKKIFNSP 247
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-186 |
2.63e-14 |
|
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: 67.84 E-value: 2.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAIARMGVV-----RtfQHVRLFREMTVIENLLVAQhqhlksgvfagllk 75
Cdd:cd03215 40 TELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAyvpedR--KREGLVLDLSVAENIALSS-------------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 76 tpafrraeaealaraaewlervgLLSmanrsAGNlaygQQRRLeIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVEL 155
Cdd:cd03215 104 -----------------------LLS-----GGN----QQKVV-LARWLARDPRVLILDEPTRGVDVGAKAEIYRLIREL 150
|
170 180 190
....*....|....*....|....*....|.
gi 1540799172 156 RDRHKvSVLLIEHDMKLVMGISDRIYVVNQG 186
Cdd:cd03215 151 ADAGK-AVLLISSELDELLGLCDRILVMYEG 180
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-169 |
2.76e-14 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 69.51 E-value: 2.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAgqaiARMGVVrtFQHVRLFREMTVIENLLVAqhqhLKsgvFAGLLKtpafr 80
Cdd:COG4525 47 TTLLNLIAGFLAPSSGEITLDGVPVTGPG----ADRGVV--FQKDALLPWLNVLDNVAFG----LR---LRGVPK----- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 81 raeAEALARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHK 160
Cdd:COG4525 109 ---AERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTG 185
|
....*....
gi 1540799172 161 VSVLLIEHD 169
Cdd:COG4525 186 KGVFLITHS 194
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
104-201 |
3.15e-14 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 69.30 E-value: 3.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 104 NRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHkvSVLLIEHDMKLVMGISDRIYVV 183
Cdd:COG1117 149 KKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMQQAARVSDYTAFF 226
|
90
....*....|....*...
gi 1540799172 184 NQGTPLAQGTPAEIRNNP 201
Cdd:COG1117 227 YLGELVEFGPTEQIFTNP 244
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-199 |
3.96e-14 |
|
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: 70.43 E-value: 3.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEglAGQAIARMGVVRTFQHVRLFREMTVIENLLvaqhqhlksgvFAGLLKTPAFR 80
Cdd:TIGR01257 970 TTTLSILTGLLPPTSGTVLVGGKDIE--TNLDAVRQSLGMCPQHNILFHHLTVAEHIL-----------FYAQLKGRSWE 1036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 81 RAEAEALARaaewLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIveLRDRHK 160
Cdd:TIGR01257 1037 EAQLEMEAM----LEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSG 1110
|
170 180 190
....*....|....*....|....*....|....*....
gi 1540799172 161 VSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRN 199
Cdd:TIGR01257 1111 RTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKN 1149
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1-186 |
6.39e-14 |
|
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: 67.82 E-value: 6.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAIA----RMGVVrtFQHVRLFREMTVIENLLVA------QHQHLKSGVF 70
Cdd:cd03292 41 STLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPylrrKIGVV--FQDFRLLPDRNVYENVAFAlevtgvPPREIRKRVP 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 71 AGLlktpafrraeaealaraaewlERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDH 150
Cdd:cd03292 119 AAL---------------------ELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMN 177
|
170 180 190
....*....|....*....|....*....|....*.
gi 1540799172 151 LIVELRDRhKVSVLLIEHDMKLVMGISDRIYVVNQG 186
Cdd:cd03292 178 LLKKINKA-GTTVVVATHAKELVDTTRHRVIALERG 212
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1-186 |
1.02e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 67.78 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIklrdrhLEGLAGQAIARMGVVRTFQHVRLFREMTVIENLLVAqhqhLKsgvfaGLLKTPAFR 80
Cdd:PRK11247 52 STLLRLLAGLETPSAGEL------LAGTAPLAEAREDTRLMFQDARLLPWKKVIDNVGLG----LK-----GQWRDAALQ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 81 RaeaealaraaewLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHK 160
Cdd:PRK11247 117 A------------LAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHG 184
|
170 180
....*....|....*....|....*.
gi 1540799172 161 VSVLLIEHDMKLVMGISDRIYVVNQG 186
Cdd:PRK11247 185 FTVLLVTHDVSEAVAMADRVLLIEEG 210
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-201 |
1.19e-13 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 67.47 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRD------RHLEGLAGQAIA-RMGVVRTFQHVRLFREMTVIENLLVAqhqhlkSGVFAGL 73
Cdd:PRK11264 43 TTLLRCINLLEQPEAGTIRVGDitidtaRSLSQQKGLIRQlRQHVGFVFQNFNLFPHRTVLENIIEG------PVIVKGE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 74 LKTPAfrraeaeaLARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIV 153
Cdd:PRK11264 117 PKEEA--------TARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIR 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1540799172 154 ELRDrHKVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRNNP 201
Cdd:PRK11264 189 QLAQ-EKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADP 235
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-186 |
1.23e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 68.78 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 2 TVFNCLTGFYRPSGGTIKLRDRHLE-GLAGQAIArMGVVRTFQHVRLFREMTVIENLLVAQHQHlKSGVF-AGLLKTPAf 79
Cdd:PRK11288 45 TLLKILSGNYQPDAGSILIDGQEMRfASTTAALA-AGVAIIYQELHLVPEMTVAENLYLGQLPH-KGGIVnRRLLNYEA- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 80 rraeaealaraAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRH 159
Cdd:PRK11288 122 -----------REQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEG 190
|
170 180
....*....|....*....|....*..
gi 1540799172 160 KVsVLLIEHDMKLVMGISDRIYVVNQG 186
Cdd:PRK11288 191 RV-ILYVSHRMEEIFALCDAITVFKDG 216
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
94-197 |
1.58e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 67.45 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 94 LERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVLLIEHDMKLV 173
Cdd:PRK13650 125 LELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV 204
|
90 100
....*....|....*....|....
gi 1540799172 174 mGISDRIYVVNQGTPLAQGTPAEI 197
Cdd:PRK13650 205 -ALSDRVLVMKNGQVESTSTPREL 227
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
34-202 |
1.71e-13 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 67.13 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 34 ARMGVVrtFQHVRLFREMTVIENLLVAQHQHLksgvfaGLLKTPAfrraeaeaLARAAEWLERVGLLSMANRSAGNLAYG 113
Cdd:COG4598 95 TRLGMV--FQSFNLWSHMTVLENVIEAPVHVL------GRPKAEA--------IERAEALLAKVGLADKRDAYPAHLSGG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 114 QQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKvSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGT 193
Cdd:COG4598 159 QQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGR-TMLVVTHEMGFARDVSSHVVFLHQGRIEEQGP 237
|
....*....
gi 1540799172 194 PAEIRNNPD 202
Cdd:COG4598 238 PAEVFGNPK 246
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
113-207 |
2.46e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 67.11 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 113 GQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQG 192
Cdd:PRK13646 149 GQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQT 228
|
90
....*....|....*
gi 1540799172 193 TPAEIRNNPDVIRAY 207
Cdd:PRK13646 229 SPKELFKDKKKLADW 243
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
97-197 |
3.29e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 66.66 E-value: 3.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 97 VGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVLLIEHDMKLVMGi 176
Cdd:PRK13642 128 VNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS- 206
|
90 100
....*....|....*....|.
gi 1540799172 177 SDRIYVVNQGTPLAQGTPAEI 197
Cdd:PRK13642 207 SDRILVMKAGEIIKEAAPSEL 227
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
94-197 |
6.76e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 65.88 E-value: 6.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 94 LERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVLLIEHDMKLV 173
Cdd:PRK13633 129 LKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEA 208
|
90 100
....*....|....*....|....
gi 1540799172 174 MGiSDRIYVVNQGTPLAQGTPAEI 197
Cdd:PRK13633 209 VE-ADRIIVMDSGKVVMEGTPKEI 231
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
94-210 |
1.02e-12 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 65.59 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 94 LERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVLLIEHDMKLV 173
Cdd:PRK11153 125 LELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVV 204
|
90 100 110
....*....|....*....|....*....|....*....
gi 1540799172 174 MGISDRIYVVNQGTPLAQGTPAEIRNNP--DVIRAYLGE 210
Cdd:PRK11153 205 KRICDRVAVIDAGRLVEQGTVSEVFSHPkhPLTREFIQS 243
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
104-201 |
1.58e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 64.55 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 104 NRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDrhKVSVLLIEHDMKLVMGISDRIYVV 183
Cdd:PRK14247 141 DAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKK--DMTIVLVTHFPQQAARISDYVAFL 218
|
90
....*....|....*...
gi 1540799172 184 NQGTPLAQGTPAEIRNNP 201
Cdd:PRK14247 219 YKGQIVEWGPTREVFTNP 236
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
42-201 |
2.10e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 63.96 E-value: 2.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 42 FQHVRLFREMTVIENLLVAQHQhlksgvFAGLLKTPAfrraeaeaLARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIA 121
Cdd:PRK09493 83 FQQFYLFPHLTALENVMFGPLR------VRGASKEEA--------EKQARELLAKVGLAERAHHYPSELSGGQQQRVAIA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 122 RCMVTRPELLMLDEPAAGLNPketdELDHLIVE-LRD--RHKVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIR 198
Cdd:PRK09493 149 RALAVKPKLMLFDEPTSALDP----ELRHEVLKvMQDlaEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLI 224
|
...
gi 1540799172 199 NNP 201
Cdd:PRK09493 225 KNP 227
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-201 |
2.60e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 64.74 E-value: 2.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDrhlEGLAGQAIARMGVVRTFQHVRLFREMTVIENLlvaqhqhlksGVFAGLLKTPAfr 80
Cdd:PRK11432 46 TTVLRLVAGLEKPTEGQIFIDG---EDVTHRSIQQRDICMVFQSYALFPHMSLGENV----------GYGLKMLGVPK-- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 81 raeAEALARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHK 160
Cdd:PRK11432 111 ---EERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFN 187
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1540799172 161 VSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRNNP 201
Cdd:PRK11432 188 ITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
93-200 |
4.00e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 63.95 E-value: 4.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 93 WLERVGL-LSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKvSVLLIEHDMK 171
Cdd:PRK13651 148 YIELVGLdESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLD 226
|
90 100
....*....|....*....|....*....
gi 1540799172 172 LVMGISDRIYVVNQGTPLAQGTPAEIRNN 200
Cdd:PRK13651 227 NVLEWTKRTIFFKDGKIIKDGDTYDILSD 255
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-196 |
4.26e-12 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 63.25 E-value: 4.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAIARM-GVVRtfQHVRLFREMTVIEnllvaqhqhlksgVFA-GLLktpA 78
Cdd:PRK13548 42 STLLRALSGELSPDSGEVRLNGRPLADWSPAELARRrAVLP--QHSSLSFPFTVEE-------------VVAmGRA---P 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 79 FRRAEAEALARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMV------TRPELLMLDEPAAGLNPKETDELDHLI 152
Cdd:PRK13548 104 HGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLA 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1540799172 153 VELRDRHKVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAE 196
Cdd:PRK13548 184 RQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-192 |
4.33e-12 |
|
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: 62.77 E-value: 4.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLR--DRHLEGLagQAIARMGVVrtFQHVRLFREMTVIENLlvaqhqhlksGVFAGL--LKT 76
Cdd:cd03266 45 TTTLRMLAGLLEPDAGFATVDgfDVVKEPA--EARRRLGFV--SDSTGLYDRLTARENL----------EYFAGLygLKG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 77 PAFRRAEAealaraaeWL-ERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVEL 155
Cdd:cd03266 111 DELTARLE--------ELaDRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQL 182
|
170 180 190
....*....|....*....|....*....|....*..
gi 1540799172 156 RDRHKvSVLLIEHDMKLVMGISDRIYVVNQGTPLAQG 192
Cdd:cd03266 183 RALGK-CILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
94-198 |
4.59e-12 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 63.99 E-value: 4.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 94 LERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDEL-DHLIVELRDrhKVSVLLIEHDMKL 172
Cdd:NF000106 129 LERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVwDEVRSMVRD--GATVLLTTQYMEE 206
|
90 100
....*....|....*....|....*.
gi 1540799172 173 VMGISDRIYVVNQGTPLAQGTPAEIR 198
Cdd:NF000106 207 AEQLAHELTVIDRGRVIADGKVDELK 232
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1-192 |
4.91e-12 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 62.74 E-value: 4.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKL--------RDRHLeglagqaiARMGVVRTfQHVRLFREMTVIENLLVAQHQH-LKSGVFA 71
Cdd:cd03267 61 TTTLKILSGLLQPTSGEVRVaglvpwkrRKKFL--------RRIGVVFG-QKTQLWWDLPVIDSFYLLAAIYdLPPARFK 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 72 GLLKtpafrraeaealaraaewlERVGLLSMA---NRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDEL 148
Cdd:cd03267 132 KRLD-------------------ELSELLDLEellDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENI 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1540799172 149 DHLIVELRDRHKVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQG 192
Cdd:cd03267 193 RNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
96-201 |
5.15e-12 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 63.57 E-value: 5.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 96 RVGLL-SMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVLLIEHDMKLVM 174
Cdd:PRK15079 147 KVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVK 226
|
90 100
....*....|....*....|....*..
gi 1540799172 175 GISDRIYVVNQGTPLAQGTPAEIRNNP 201
Cdd:PRK15079 227 HISDRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
93-201 |
5.59e-12 |
|
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: 63.94 E-value: 5.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 93 WLERVGLLSMANRSAgnlAY------GQQRRLEIARCMVTRPELLMLDEPaaglnpkeTDELD--------HLIVELRDR 158
Cdd:COG4172 137 LLERVGIPDPERRLD---AYphqlsgGQRQRVMIAMALANEPDLLIADEP--------TTALDvtvqaqilDLLKDLQRE 205
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1540799172 159 HKVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRNNP 201
Cdd:COG4172 206 LGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAAP 248
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-170 |
5.63e-12 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 62.79 E-value: 5.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAgqaiARMGVVrtFQHVRLFREMTVIENllVAQHQHLksgvfAGLLKTpafr 80
Cdd:PRK11248 41 TTLLNLIAGFVPYQHGSITLDGKPVEGPG----AERGVV--FQNEGLLPWRNVQDN--VAFGLQL-----AGVEKM---- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 81 raeaEALARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHK 160
Cdd:PRK11248 104 ----QRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETG 179
|
170
....*....|
gi 1540799172 161 VSVLLIEHDM 170
Cdd:PRK11248 180 KQVLLITHDI 189
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
104-197 |
8.89e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 62.45 E-value: 8.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 104 NRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRdRHKVSVLLIEHDMKLVMGISDRIYVV 183
Cdd:PRK13649 140 EKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVL 218
|
90
....*....|....
gi 1540799172 184 NQGTPLAQGTPAEI 197
Cdd:PRK13649 219 EKGKLVLSGKPKDI 232
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
35-193 |
1.05e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 61.95 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 35 RMGVVRTFQHVRLFREMTVIENLLVAQHQHLksgvfaGLLKTPAfrraeaeaLARAAEWLERVGLLSMANRSAGNLAYGQ 114
Cdd:PRK11124 81 RRNVGMVFQQYNLWPHLTVQQNLIEAPCRVL------GLSKDQA--------LARAEKLLERLRLKPYADRFPLHLSGGQ 146
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1540799172 115 QRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVlLIEHDMKLVMGISDRIYVVNQGTPLAQGT 193
Cdd:PRK11124 147 QQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQV-IVTHEVEVARKTASRVVYMENGHIVEQGD 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-186 |
1.17e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 63.11 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGL-AGQAIARmGVV-----RtfQHVRLFREMTVIENLLVAQHQHLKSGvfaGLL 74
Cdd:COG1129 292 TELARALFGADPADSGEIRLDGKPVRIRsPRDAIRA-GIAyvpedR--KGEGLVLDLSIRENITLASLDRLSRG---GLL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 75 KTPAfrraeaeALARAAEWLERVGL------LSMANRSAGNlaygQQRRLeIARCMVTRPELLMLDEPAAGLnpketD-- 146
Cdd:COG1129 366 DRRR-------ERALAEEYIKRLRIktpspeQPVGNLSGGN----QQKVV-LAKWLATDPKVLILDEPTRGI-----Dvg 428
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1540799172 147 ---ELDHLIVELRDRhKVSVLLIEHDMKLVMGISDRIYVVNQG 186
Cdd:COG1129 429 akaEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREG 470
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1-180 |
1.32e-11 |
|
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: 61.12 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEglAGQAIARMGVVrtFQHVR--LFREmTVIENLLV-AQHQHLKSGVFAGLLKTp 77
Cdd:cd03226 40 TTLAKILAGLIKESSGSILLNGKPIK--AKERRKSIGYV--MQDVDyqLFTD-SVREELLLgLKELDAGNEQAETVLKD- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 78 afrraeaealaraaewlerVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRD 157
Cdd:cd03226 114 -------------------LDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAA 174
|
170 180
....*....|....*....|...
gi 1540799172 158 RhKVSVLLIEHDMKLVMGISDRI 180
Cdd:cd03226 175 Q-GKAVIVITHDYEFLAKVCDRV 196
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
108-186 |
1.54e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.71 E-value: 1.54e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1540799172 108 GNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRdRHKVSVLLIEHDMKLVMGISDRIYVVNQG 186
Cdd:PRK10762 394 GLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFK-AEGLSIILVSSEMPEVLGMSDRILVMHEG 471
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-211 |
2.04e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 62.17 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAIARMgVVRTFQHVRLFREMTVIENLLVAQHQHLksGVFAGLLKTpafr 80
Cdd:PRK09536 43 TTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR-VASVPQDTSLSFEFDVRQVVEMGRTPHR--SRFDTWTET---- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 81 raeaeALARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHK 160
Cdd:PRK09536 116 -----DRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGK 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1540799172 161 VSVLLIeHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRnNPDVIRAYLGEE 211
Cdd:PRK09536 191 TAVAAI-HDLDLAARYCDELVLLADGRVRAAGPPADVL-TADTLRAAFDAR 239
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
110-201 |
2.08e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 61.65 E-value: 2.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 110 LAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRhkVSVLLIEHDMKLVMGISDRIYVVNQGTPL 189
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLV 241
|
90
....*....|..
gi 1540799172 190 AQGTPAEIRNNP 201
Cdd:PRK14271 242 EEGPTEQLFSSP 253
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
42-201 |
2.21e-11 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 61.18 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 42 FQHVRLFREMTVIENLLVAQHQHLksgvfaGLLKTPAfrraeaeaLARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIA 121
Cdd:COG4161 88 FQQYNLWPHLTVMENLIEAPCKVL------GLSKEQA--------REKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 122 RCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVlLIEHDMKLVMGISDRIYVVNQGTPLAQGTpAEIRNNP 201
Cdd:COG4161 154 RALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQV-IVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQP 231
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-197 |
2.31e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 60.75 E-value: 2.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDrhlEGLAGQAIARMGVVRTFQHVRLFREMTVIENLLVAQHQHLK-SGVFAGLLKTPAf 79
Cdd:PRK10771 39 STLLNLIAGFLTPASGSLTLNG---QDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGLNPGLKlNAAQREKLHAIA- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 80 rraeaealaraaewlERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRH 159
Cdd:PRK10771 115 ---------------RQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQER 179
|
170 180 190
....*....|....*....|....*....|....*...
gi 1540799172 160 KVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEI 197
Cdd:PRK10771 180 QLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1-196 |
2.99e-11 |
|
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: 60.70 E-value: 2.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAIARM-GVVrtFQHVRLFREmTVIENLLVAqHQHLKSGVFAGLLKTPAF 79
Cdd:cd03254 43 TTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMiGVV--LQDTFLFSG-TIMENIRLG-RPNATDEEVIEAAKEAGA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 80 RRAEAEalaraaewLERvGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPkETDEL--DHLIVELRD 157
Cdd:cd03254 119 HDFIMK--------LPN-GYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDT-ETEKLiqEALEKLMKG 188
|
170 180 190
....*....|....*....|....*....|....*....
gi 1540799172 158 RhkvSVLLIEHDMKLVMGiSDRIYVVNQGTPLAQGTPAE 196
Cdd:cd03254 189 R---TSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDE 223
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
104-211 |
3.38e-11 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 61.77 E-value: 3.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 104 NRSAGNLAYGQQRRLEIARCMvtRPELL----MLDEPAAGLNPKETDELDHLIVELRDRHKvSVLLIEHDMKLVmGISDR 179
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHL--GAELIgityILDEPSIGLHPQDTHKLINVIKKLRDQGN-TVLLVEHDEQMI-SLADR 546
|
90 100 110
....*....|....*....|....*....|....*....
gi 1540799172 180 IYVVNQGTP------LAQGTPAEIRNNPDVIRA-YLGEE 211
Cdd:PRK00635 547 IIDIGPGAGifggevLFNGSPREFLAKSDSLTAkYLRQE 585
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
7-172 |
3.72e-11 |
|
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: 60.14 E-value: 3.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 7 LTGFYRPSGGTIKLRDRHLEGLAGQAIAR-----MGVVrtFQHVRLFREMTVIENLLVaqhqhlksgvfagllktPAFRR 81
Cdd:COG4181 58 LAGLDRPTSGTVRLAGQDLFALDEDARARlrarhVGFV--FQSFQLLPTLTALENVML-----------------PLELA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 82 AEAEALARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKV 161
Cdd:COG4181 119 GRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGT 198
|
170
....*....|.
gi 1540799172 162 SVLLIEHDMKL 172
Cdd:COG4181 199 TLVLVTHDPAL 209
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-186 |
4.09e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 60.48 E-value: 4.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAIARMgVVRTFQHVRL--FREMTVIENLLVAQHQHLKSGVFAGLLKTpa 78
Cdd:COG1101 46 STLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKY-IGRVFQDPMMgtAPSMTIEENLALAYRRGKRRGLRRGLTKK-- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 79 frraeaeALARAAEWLERVGLlSMANR---SAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVEL 155
Cdd:COG1101 123 -------RRELFRELLATLGL-GLENRldtKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKI 194
|
170 180 190
....*....|....*....|....*....|...
gi 1540799172 156 RDRHKVSVLLIEHDMK--LVMGisDRIYVVNQG 186
Cdd:COG1101 195 VEENNLTTLMVTHNMEqaLDYG--NRLIMMHEG 225
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
94-201 |
4.31e-11 |
|
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: 60.84 E-value: 4.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 94 LERVGLLSMANRSAgnlAY------GQQRRLEIARCMVTRPELLMLDEPAAGLnpketdelD--------HLIVELRDRH 159
Cdd:COG0444 132 LERVGLPDPERRLD---RYphelsgGMRQRVMIARALALEPKLLIADEPTTAL--------DvtiqaqilNLLKDLQREL 200
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1540799172 160 KVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRNNP 201
Cdd:COG0444 201 GLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFENP 242
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
94-201 |
4.57e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 60.45 E-value: 4.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 94 LERVGLLSMA----NRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDrhKVSVLLIEHD 169
Cdd:PRK14246 134 LRKVGLWKEVydrlNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKN--EIAIVIVSHN 211
|
90 100 110
....*....|....*....|....*....|..
gi 1540799172 170 MKLVMGISDRIYVVNQGTPLAQGTPAEIRNNP 201
Cdd:PRK14246 212 PQQVARVADYVAFLYNGELVEWGSSNEIFTSP 243
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
108-186 |
4.74e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 61.28 E-value: 4.74e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1540799172 108 GNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKvSVLLIEHDMKLVMGISDRIYVVNQG 186
Cdd:PRK10982 390 GSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDK-GIIIISSEMPELLGITDRILVMSNG 467
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1-152 |
5.06e-11 |
|
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: 59.29 E-value: 5.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHL---EGLAGQAIARMGvvrtfqHVR-LFREMTVIENL--LVAQHQHLKSGVFAGLl 74
Cdd:TIGR01189 40 TTLLRILAGLLRPDSGEVRWNGTPLaeqRDEPHENILYLG------HLPgLKPELSALENLhfWAAIHGGAQRTIEDAL- 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1540799172 75 ktpafrraeaealaraaewlERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLI 152
Cdd:TIGR01189 113 --------------------AAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLL 170
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1-186 |
7.71e-11 |
|
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: 59.19 E-value: 7.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGqaiARMGVVRTFQHVRLFREMTVIENLLVAqhqhLKsgvfagLLKTPAFR 80
Cdd:cd03301 40 TTTLRMIAGLEEPTSGRIYIGGRDVTDLPP---KDRDIAMVFQNYALYPHMTVYDNIAFG----LK------LRKVPKDE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 81 RAeaealaraaewlERV-------GLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIV 153
Cdd:cd03301 107 ID------------ERVrevaellQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELK 174
|
170 180 190
....*....|....*....|....*....|...
gi 1540799172 154 ELRDRHKVSVLLIEHDMKLVMGISDRIYVVNQG 186
Cdd:cd03301 175 RLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDG 207
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
104-202 |
9.46e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 59.47 E-value: 9.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 104 NRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHkvSVLLIEHDMKLVMGISDRIYVV 183
Cdd:PRK14267 144 NDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFL 221
|
90
....*....|....*....
gi 1540799172 184 NQGTPLAQGTPAEIRNNPD 202
Cdd:PRK14267 222 YLGKLIEVGPTRKVFENPE 240
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-186 |
1.83e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 58.35 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTI--------KLRDRHLEGLAGQaiarMGVVrtFQHVRLFREMTVIENLLV------AQHQHLK 66
Cdd:PRK10908 42 STLLKLICGIERPSAGKIwfsghditRLKNREVPFLRRQ----IGMI--FQDHHLLMDRTVYDNVAIpliiagASGDDIR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 67 SGVFAGLlktpafrraeaealaraaewlERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETD 146
Cdd:PRK10908 116 RRVSAAL---------------------DKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1540799172 147 ELDHLIVELrDRHKVSVLLIEHDMKLVMGISDRIYVVNQG 186
Cdd:PRK10908 175 GILRLFEEF-NRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
113-201 |
2.32e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 59.33 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 113 GQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQG 192
Cdd:PRK15134 429 GQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQG 508
|
....*....
gi 1540799172 193 TPAEIRNNP 201
Cdd:PRK15134 509 DCERVFAAP 517
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
110-201 |
2.68e-10 |
|
nickel import ATP-binding protein NikD; This family represents the NikD 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. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 57.76 E-value: 2.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 110 LAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVLLIEHDMKLVMGISDRIYVVNQGTPL 189
Cdd:TIGR02770 126 LSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIV 205
|
90
....*....|..
gi 1540799172 190 AQGTPAEIRNNP 201
Cdd:TIGR02770 206 ERGTVKEIFYNP 217
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
104-178 |
2.88e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 58.25 E-value: 2.88e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1540799172 104 NRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHkvSVLLIEHDMKLVMGISD 178
Cdd:PRK14243 146 KQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSD 218
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
106-179 |
3.24e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 57.86 E-value: 3.24e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1540799172 106 SAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDrhKVSVLLIEHDMKLVMGISDR 179
Cdd:PRK14239 145 SALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKD--DYTMLLVTRSMQQASRISDR 216
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-206 |
4.47e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.52 E-value: 4.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAIARMGVVRTFQHVRLFREMTVIENLLVaqhqhlksgvfaGLLKTPAFR 80
Cdd:PRK15439 51 STLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYLVPQEPLLFPNLSVKENILF------------GLPKRQASM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 81 RAEAEALARAAEWLErvglLSManrSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRhK 160
Cdd:PRK15439 119 QKMKQLLAALGCQLD----LDS---SAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQ-G 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1540799172 161 VSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRNNpDVIRA 206
Cdd:PRK15439 191 VGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTD-DIIQA 235
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
94-201 |
4.85e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 57.49 E-value: 4.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 94 LERVGLL-SMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVLLIEHDMKL 172
Cdd:PRK15112 133 LRQVGLLpDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGM 212
|
90 100
....*....|....*....|....*....
gi 1540799172 173 VMGISDRIYVVNQGTPLAQGTPAEIRNNP 201
Cdd:PRK15112 213 MKHISDQVLVMHQGEVVERGSTADVLASP 241
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
113-187 |
4.87e-10 |
|
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: 57.06 E-value: 4.87e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1540799172 113 GQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRhKVSVLLIEHDMKLVMGISDRIYVVNQGT 187
Cdd:COG4778 156 GEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| BCA_ABC_TP_C |
pfam12399 |
Branched-chain amino acid ATP-binding cassette transporter; This domain family is found in ... |
189-211 |
6.23e-10 |
|
Branched-chain amino acid ATP-binding cassette transporter; This domain family is found in bacteria, archaea and eukaryotes, and is approximately 30 amino acids in length. The family is found in association with pfam00005. There is a conserved AYLG sequence motif. This family is the C terminal of an ATP dependent branched-chain amino acid transporter. This domain is essential for LPS transport, through critical interactions with Walker A and switch helix domains.
Pssm-ID: 463560 Cd Length: 25 Bit Score: 52.25 E-value: 6.23e-10
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
42-200 |
6.65e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 57.33 E-value: 6.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 42 FQHVRLFREMTVIENLLVAqhqhlksgvfaGLLKTP----AFRRAEAEALARAAEWLERVGLLSMANRSAGNLAYGQQRR 117
Cdd:PRK09984 92 FQQFNLVNRLSVLENVLIG-----------ALGSTPfwrtCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQR 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 118 LEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEI 197
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF 240
|
...
gi 1540799172 198 RNN 200
Cdd:PRK09984 241 DNE 243
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-172 |
7.11e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 56.75 E-value: 7.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAIA-----RMGVVRTFQHvrLFREMTVIENLLVAQhqhLKSGVFAGLLK 75
Cdd:PRK11629 49 STLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAelrnqKLGFIYQFHH--LLPDFTALENVAMPL---LIGKKKPAEIN 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 76 TPAFRRaeaealaraaewLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVEL 155
Cdd:PRK11629 124 SRALEM------------LAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGEL 191
|
170
....*....|....*..
gi 1540799172 156 RDRHKVSVLLIEHDMKL 172
Cdd:PRK11629 192 NRLQGTAFLVVTHDLQL 208
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
94-204 |
7.69e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 56.66 E-value: 7.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 94 LERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVLLIEHDMKLV 173
Cdd:PRK09544 105 LKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLV 184
|
90 100 110
....*....|....*....|....*....|.
gi 1540799172 174 MGISDRIYVVNQGTpLAQGTPAEIRNNPDVI 204
Cdd:PRK09544 185 MAKTDEVLCLNHHI-CCSGTPEVVSLHPEFI 214
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
100-186 |
9.05e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 57.37 E-value: 9.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 100 LSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHkVSVLLIEHDMKLVMGISDR 179
Cdd:PRK15439 394 FNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQN-VAVLFISSDLEEIEQMADR 472
|
....*..
gi 1540799172 180 IYVVNQG 186
Cdd:PRK15439 473 VLVMHQG 479
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
94-201 |
1.11e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 57.02 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 94 LERVGLLSMANRSAG---NLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVLLIEHDM 170
Cdd:PRK15134 138 LDRVGIRQAAKRLTDyphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNL 217
|
90 100 110
....*....|....*....|....*....|.
gi 1540799172 171 KLVMGISDRIYVVNQGTPLAQGTPAEIRNNP 201
Cdd:PRK15134 218 SIVRKLADRVAVMQNGRCVEQNRAATLFSAP 248
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
94-187 |
1.16e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 57.11 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 94 LERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDrHKVSVLLIEHDMKLV 173
Cdd:NF040905 124 LAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKA-QGITSIIISHKLNEI 202
|
90
....*....|....
gi 1540799172 174 MGISDRIYVVNQGT 187
Cdd:NF040905 203 RRVADSITVLRDGR 216
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
100-186 |
1.19e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 57.25 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 100 LSMANRSAGNlaygQQRRLeIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHkVSVLLIEHDMKLVMGISDR 179
Cdd:PRK13549 401 LAIARLSGGN----QQKAV-LAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQG-VAIIVISSELPEVLGLSDR 474
|
....*..
gi 1540799172 180 IYVVNQG 186
Cdd:PRK13549 475 VLVMHEG 481
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
94-182 |
1.34e-09 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 56.66 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 94 LERVGLL-SMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEP---------AAGLNpketdeldhLIVELRDRHKVSV 163
Cdd:COG4608 141 LELVGLRpEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPvsaldvsiqAQVLN---------LLEDLQDELGLTY 211
|
90
....*....|....*....
gi 1540799172 164 LLIEHDMKLVMGISDRIYV 182
Cdd:COG4608 212 LFISHDLSVVRHISDRVAV 230
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
94-198 |
1.46e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 57.06 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 94 LERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVLLIEHDMKLV 173
Cdd:NF033858 382 LERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEA 461
|
90 100
....*....|....*....|....*
gi 1540799172 174 MGiSDRIYVVNQGTPLAQGTPAEIR 198
Cdd:NF033858 462 ER-CDRISLMHAGRVLASDTPAALV 485
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
108-186 |
2.12e-09 |
|
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: 56.37 E-value: 2.12e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1540799172 108 GNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRdRHKVSVLLIEHDMKLVMGISDRIYVVNQG 186
Cdd:TIGR02633 402 GRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLA-QEGVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
93-142 |
2.41e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.18 E-value: 2.41e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1540799172 93 WLERVGL-LSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNP 142
Cdd:PRK10938 384 WLDILGIdKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDP 434
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
110-206 |
3.17e-09 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 55.88 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 110 LAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPketdELDHLIVELRDRHKVSVLLIEHDMKLVMGiSDRIYVVNQGTPL 189
Cdd:TIGR00958 618 LSGGQKQRIAIARALVRKPRVLILDEATSALDA----ECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVV 692
|
90
....*....|....*..
gi 1540799172 190 AQGTPAEIRNNPDVIRA 206
Cdd:TIGR00958 693 EMGTHKQLMEDQGCYKH 709
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-186 |
4.27e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 54.93 E-value: 4.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRH--LEGLAGQAIARM--------GVVRtfQHVRLFREMTVI------ENLLVAQHQH 64
Cdd:PRK11701 46 TTLLNALSARLAPDAGEVHYRMRDgqLRDLYALSEAERrrllrtewGFVH--QHPRDGLRMQVSaggnigERLMAVGARH 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 65 LksgvfaGLLKTPAfrraeaealaraAEWLERVGL-LSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLN-- 141
Cdd:PRK11701 124 Y------GDIRATA------------GDWLERVEIdAARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDvs 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1540799172 142 --PKETDELDHLIVELRdrhkVSVLLIEHDMKLVMGISDRIYVVNQG 186
Cdd:PRK11701 186 vqARLLDLLRGLVRELG----LAVVIVTHDLAVARLLAHRLLVMKQG 228
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1-183 |
6.42e-09 |
|
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: 54.99 E-value: 6.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGlAGQAIARMGVVRTFQHVRLFrEMTVIENLLVAQhqhlkSGVFAGLLKTPafr 80
Cdd:TIGR02857 362 STLLNLLLGFVDPTEGSIAVNGVPLAD-ADADSWRDQIAWVPQHPFLF-AGTIAENIRLAR-----PDASDAEIREA--- 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 81 raeaealaraaewLERVGLLSMAN------------RSAGnLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDEL 148
Cdd:TIGR02857 432 -------------LERAGLDEFVAalpqgldtpigeGGAG-LSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEV 497
|
170 180 190
....*....|....*....|....*....|....*
gi 1540799172 149 DHLIVELRDRHkvSVLLIEHDMKLvMGISDRIYVV 183
Cdd:TIGR02857 498 LEALRALAQGR--TVLLVTHRLAL-AALADRIVVL 529
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
113-200 |
7.77e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 54.32 E-value: 7.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 113 GQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQG 192
Cdd:COG4586 158 GQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDG 237
|
....*...
gi 1540799172 193 TPAEIRNN 200
Cdd:COG4586 238 SLEELKER 245
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
113-187 |
9.47e-09 |
|
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: 52.07 E-value: 9.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 113 GQQRRLEIARCMVTRPELLMLDEPaaglnpkeTDELD-----HLIVELRDrHKVSVLLIEHDMKLVMGISDRIYVVNQGT 187
Cdd:cd03221 74 GEKMRLALAKLLLENPNLLLLDEP--------TNHLDlesieALEEALKE-YPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
94-197 |
9.86e-09 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 53.86 E-value: 9.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 94 LERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKvSVLLIEHDMKLV 173
Cdd:PRK11231 123 MEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGK-TVVTVLHDLNQA 201
|
90 100
....*....|....*....|....
gi 1540799172 174 MGISDRIYVVNQGTPLAQGTPAEI 197
Cdd:PRK11231 202 SRYCDHLVVLANGHVMAQGTPEEV 225
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
107-186 |
1.01e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 54.41 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 107 AGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKvSVLLIEHDMKLVMGISDRIYVVNQG 186
Cdd:NF040905 402 VGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGK-GVIVISSELPELLGMCDRIYVMNEG 480
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-196 |
1.14e-08 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 54.40 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIK-----LRDRHLEGLAgqaiARMGVVrtFQHVRLFrEMTVIENLLVAQHQH--------LKS 67
Cdd:COG1132 380 STLVNLLLRFYDPTSGRILidgvdIRDLTLESLR----RQIGVV--PQDTFLF-SGTIRENIRYGRPDAtdeeveeaAKA 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 68 gvfAGLLKtpafrraeaealaraaeWLERV--GLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPkET 145
Cdd:COG1132 453 ---AQAHE-----------------FIEALpdGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDT-ET 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1540799172 146 DEL--DHLIVELRDRhkvSVLLIEHDMKLVMGiSDRIYVVNQGTPLAQGTPAE 196
Cdd:COG1132 512 EALiqEALERLMKGR---TTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTHEE 560
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-193 |
1.21e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 54.63 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLrdrhleglAGQAIArMGVVRTFQHVRLFREMTVIENLLVAQhQHLKsgVFAGLLKTPAfr 80
Cdd:TIGR01257 1979 TTTFKMLTGDTTVTSGDATV--------AGKSIL-TNISDVHQNMGYCPQFDAIDDLLTGR-EHLY--LYARLRGVPA-- 2044
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 81 raeaEALARAAEW-LERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRdRH 159
Cdd:TIGR01257 2045 ----EEIEKVANWsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSII-RE 2119
|
170 180 190
....*....|....*....|....*....|....
gi 1540799172 160 KVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGT 193
Cdd:TIGR01257 2120 GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGT 2153
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
113-201 |
1.21e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 53.96 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 113 GQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQG 192
Cdd:PRK09473 165 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 244
|
....*....
gi 1540799172 193 TPAEIRNNP 201
Cdd:PRK09473 245 NARDVFYQP 253
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
94-194 |
1.22e-08 |
|
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: 53.27 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 94 LERVGLLSMANRSAG-----------NLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPketdELDHLIVE-LRDR-HK 160
Cdd:cd03244 113 LERVGLKEFVESLPGgldtvveeggeNLSVGQRQLLCLARALLRKSKILVLDEATASVDP----ETDALIQKtIREAfKD 188
|
90 100 110
....*....|....*....|....*....|....
gi 1540799172 161 VSVLLIEHDMKLVMGiSDRIYVVNQGTPLAQGTP 194
Cdd:cd03244 189 CTVLTIAHRLDTIID-SDRILVLDKGRVVEFDSP 221
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
101-201 |
1.42e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.09 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 101 SMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVLLIEHDMKLVMGISDRI 180
Cdd:PRK10261 160 TILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRV 239
|
90 100
....*....|....*....|.
gi 1540799172 181 YVVNQGTPLAQGTPAEIRNNP 201
Cdd:PRK10261 240 LVMYQGEAVETGSVEQIFHAP 260
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
94-196 |
1.59e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 53.35 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 94 LERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKvSVLLIEHDMKLV 173
Cdd:PRK15056 127 LARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGK-TMLVSTHNLGSV 205
|
90 100
....*....|....*....|...
gi 1540799172 174 MGISDRIYVVnQGTPLAQGtPAE 196
Cdd:PRK15056 206 TEFCDYTVMV-KGTVLASG-PTE 226
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
113-201 |
1.64e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 53.43 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 113 GQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQG 192
Cdd:PRK11308 158 GQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKG 237
|
....*....
gi 1540799172 193 TPAEIRNNP 201
Cdd:PRK11308 238 TKEQIFNNP 246
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1-193 |
2.64e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 53.29 E-value: 2.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAI-ARMGVVRtfQHVRLFREmTVIENLLVAQHQ----HLkSGVfagllk 75
Cdd:PRK11160 380 STLLQLLTRAWDPQQGEILLNGQPIADYSEAALrQAISVVS--QRVHLFSA-TLRDNLLLAAPNasdeAL-IEV------ 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 76 tpafrraeaealaraaewLERVGLLSMANRSAG----------NLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKET 145
Cdd:PRK11160 450 ------------------LQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETE 511
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1540799172 146 DELDHLIVELRdRHKvSVLLIEHDMKLvMGISDRIYVVNQGTPLAQGT 193
Cdd:PRK11160 512 RQILELLAEHA-QNK-TVLMITHRLTG-LEQFDRICVMDNGQIIEQGT 556
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
94-201 |
3.97e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 52.55 E-value: 3.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 94 LERVGLL-SMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVLLIEHDMKL 172
Cdd:PRK10261 447 LERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAV 526
|
90 100
....*....|....*....|....*....
gi 1540799172 173 VMGISDRIYVVNQGTPLAQGTPAEIRNNP 201
Cdd:PRK10261 527 VERISHRVAVMYLGQIVEIGPRRAVFENP 555
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-169 |
4.01e-08 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 52.37 E-value: 4.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRhleglagqaiARMGVVRtfQHVRLFREMTVIENLLVAqHQHLKSGV--FAGLLKTPA 78
Cdd:COG0488 38 STLLKILAGELEPDSGEVSIPKG----------LRIGYLP--QEPPLDDDLTVLDTVLDG-DAELRALEaeLEELEAKLA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 79 FRRAEAEALARAAEWLERVG----------LLS-------MANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPaagln 141
Cdd:COG0488 105 EPDEDLERLAELQEEFEALGgweaearaeeILSglgfpeeDLDRPVSELSGGWRRRVALARALLSEPDLLLLDEP----- 179
|
170 180 190
....*....|....*....|....*....|..
gi 1540799172 142 pkeTDELDHLIVE-LRD---RHKVSVLLIEHD 169
Cdd:COG0488 180 ---TNHLDLESIEwLEEflkNYPGTVLVVSHD 208
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1-169 |
4.12e-08 |
|
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: 52.75 E-value: 4.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAIARmgVVRTF-QHVRLFrEMTVIENLLVAQHQHLKSGVFAGLLKtpaf 79
Cdd:TIGR02868 375 STLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRR--RVSVCaQDAHLF-DTTVRENLRLARPDATDEELWAALER---- 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 80 rraeaealARAAEWLERV--GLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRD 157
Cdd:TIGR02868 448 --------VGLADWLRALpdGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALS 519
|
170
....*....|..
gi 1540799172 158 RHkvSVLLIEHD 169
Cdd:TIGR02868 520 GR--TVVLITHH 529
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
101-197 |
4.29e-08 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 52.50 E-value: 4.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 101 SMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVLLIEHDMKLVMGISDRI 180
Cdd:TIGR03269 419 EILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRA 498
|
90
....*....|....*..
gi 1540799172 181 YVVNQGTPLAQGTPAEI 197
Cdd:TIGR03269 499 ALMRDGKIVKIGDPEEI 515
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
94-140 |
4.42e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 51.41 E-value: 4.42e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1540799172 94 LERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGL 140
Cdd:PRK13539 112 LEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
110-201 |
4.74e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 52.05 E-value: 4.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 110 LAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVLLIEHDMKLVMGISDRIYVVNQGTPL 189
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVV 233
|
90
....*....|..
gi 1540799172 190 AQGTPAEIRNNP 201
Cdd:PRK11022 234 ETGKAHDIFRAP 245
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
94-202 |
4.75e-08 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 52.34 E-value: 4.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 94 LERVGL--LSMaNRSAGNLAYGQ-QR-RLeiARCMVTRpelLM-----LDEPAAGLNPKETDELDHLIVELRDRHKvSVL 164
Cdd:COG0178 469 LVDVGLdyLTL-DRSAGTLSGGEaQRiRL--ATQIGSG---LVgvlyvLDEPSIGLHQRDNDRLIETLKRLRDLGN-TVI 541
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1540799172 165 LIEHDmKLVMGISDRI------------YVVnqgtplAQGTPAEIRNNPD 202
Cdd:COG0178 542 VVEHD-EDTIRAADYIidigpgagehggEVV------AQGTPEEILKNPD 584
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
97-209 |
6.67e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 51.33 E-value: 6.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 97 VGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVLLIEHDMKLVMGI 176
Cdd:PRK10575 135 VGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARY 214
|
90 100 110
....*....|....*....|....*....|...
gi 1540799172 177 SDRIYVVNQGTPLAQGTPAEIRnNPDVIRAYLG 209
Cdd:PRK10575 215 CDYLVALRGGEMIAQGTPAELM-RGETLEQIYG 246
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1-209 |
8.12e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 51.14 E-value: 8.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAIAR-MGVVRtfQHVRLFREMTVIENLLVAQHQHlksgvfagllkTPAF 79
Cdd:PRK10253 47 STLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARrIGLLA--QNATTPGDITVQELVARGRYPH-----------QPLF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 80 RRAEAEALARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRH 159
Cdd:PRK10253 114 TRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREK 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1540799172 160 KVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRnNPDVIRAYLG 209
Cdd:PRK10253 194 GYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV-TAELIERIYG 242
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
7-186 |
8.76e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 51.57 E-value: 8.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 7 LTGFYRPSGGTIKLRDRHLEGLAGQAIARMGVVrtfqHV---RLFR----EMTVIENLLVAQHqhlksgvfagllKTPAF 79
Cdd:COG3845 304 LAGLRPPASGSIRLDGEDITGLSPRERRRLGVA----YIpedRLGRglvpDMSVAENLILGRY------------RRPPF 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 80 rraeaealaRAAEWLERVGLLSMANR--------------SAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKET 145
Cdd:COG3845 368 ---------SRGGFLDRKAIRAFAEElieefdvrtpgpdtPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAI 438
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1540799172 146 DELDHLIVELRDRhKVSVLLIEHDMKLVMGISDRIYVVNQG 186
Cdd:COG3845 439 EFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEG 478
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
94-186 |
1.12e-07 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 50.84 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 94 LERVGL-LSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVLLIEHDMKL 172
Cdd:PRK10419 135 LRAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRL 214
|
90
....*....|....
gi 1540799172 173 VMGISDRIYVVNQG 186
Cdd:PRK10419 215 VERFCQRVMVMDNG 228
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
94-211 |
1.28e-07 |
|
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: 51.17 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 94 LERVGL--LSMaNRSAGNLAYGQQRRLEIARCMVTRPE--LLMLDEPAAGLNPKETDELDHLIVELRDRHKvSVLLIEHD 169
Cdd:TIGR00630 472 LIDVGLdyLSL-SRAAGTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHQRDNRRLINTLKRLRDLGN-TLIVVEHD 549
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1540799172 170 mKLVMGISDriYVVNQGtP---------LAQGTPAEIRNNPDVIR-AYLGEE 211
Cdd:TIGR00630 550 -EDTIRAAD--YVIDIG-PgagehggevVASGTPEEILANPDSLTgQYLSGR 597
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
94-180 |
1.59e-07 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 49.95 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 94 LERVGL--LSMaNRSAGNLAYGQQRRLEIARCMVTRPE--LLMLDEPAAGLNPKETDELDHLIVELRDrHKVSVLLIEHD 169
Cdd:cd03270 121 LVDVGLgyLTL-SRSAPTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRD-LGNTVLVVEHD 198
|
90
....*....|.
gi 1540799172 170 MKlVMGISDRI 180
Cdd:cd03270 199 ED-TIRAADHV 208
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
94-184 |
1.95e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 49.78 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 94 LERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVLLIEHDMKLV 173
Cdd:PRK10584 131 LEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLA 210
|
90
....*....|.
gi 1540799172 174 MGISDRIYVVN 184
Cdd:PRK10584 211 ARCDRRLRLVN 221
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
95-207 |
2.58e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 49.55 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 95 ERVGLLSMANRSAGNLAYGQ-QR-RLeIARCMVTRPE------LLMLDEPAAGLNPKETDELDHLIVELRdRHKVSVLLI 166
Cdd:PRK03695 112 EALGLDDKLGRSVNQLSGGEwQRvRL-AAVVLQVWPDinpagqLLLLDEPMNSLDVAQQAALDRLLSELC-QQGIAVVMS 189
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1540799172 167 EHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRNNPDVIRAY 207
Cdd:PRK03695 190 SHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVF 230
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
109-208 |
2.74e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.41 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 109 NLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVLLIEHDMKLVMGiSDRIYVVNQ--- 185
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNNpdr 1436
|
90 100
....*....|....*....|....*.
gi 1540799172 186 -GTPL-AQGTPAEIRNNPD-VIRAYL 208
Cdd:PTZ00265 1437 tGSFVqAHGTHEELLSVQDgVYKKYV 1462
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
113-192 |
3.13e-07 |
|
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: 48.46 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 113 GQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVE-LRDRhkvSVLLIEHDMKlvmGIS--DRIYVVNQGTPL 189
Cdd:cd03247 102 GERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEvLKDK---TLIWITHHLT---GIEhmDKILFLENGKII 175
|
...
gi 1540799172 190 AQG 192
Cdd:cd03247 176 MQG 178
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1-211 |
3.91e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 49.49 E-value: 3.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGlAGQAIA------RMGVVrtFQHVRLFREMTVIENLLVaqhqhlksgvfaGLL 74
Cdd:PRK11144 38 TSLINAISGLTRPQKGRIVLNGRVLFD-AEKGIClppekrRIGYV--FQDARLFPHYKVRGNLRY------------GMA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 75 KTpafrraeaealaRAAEWLERVGLLSMA---NRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLN-PKETDELDH 150
Cdd:PRK11144 103 KS------------MVAQFDKIVALLGIEpllDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKRELLPY 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1540799172 151 LiVELRDRHKVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRNNPdVIRAYLGEE 211
Cdd:PRK11144 171 L-ERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASS-AMRPWLPKE 229
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
94-141 |
3.95e-07 |
|
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: 48.64 E-value: 3.95e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1540799172 94 LERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLN 141
Cdd:cd03231 110 LARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-186 |
4.00e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 49.72 E-value: 4.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAIARM-----GVVrtFQHVRLFREMTVIENLLVaqhqhlkSGVFAGLLK 75
Cdd:PRK10535 48 STLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLrrehfGFI--FQRYHLLSHLTAAQNVEV-------PAVYAGLER 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 76 TpafrraeaEALARAAEWLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVEL 155
Cdd:PRK10535 119 K--------QRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQL 190
|
170 180 190
....*....|....*....|....*....|..
gi 1540799172 156 RDR-HkvSVLLIEHDmKLVMGISDRIYVVNQG 186
Cdd:PRK10535 191 RDRgH--TVIIVTHD-PQVAAQAERVIEIRDG 219
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
104-180 |
4.20e-07 |
|
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: 48.09 E-value: 4.20e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1540799172 104 NRSAGNLAYGQQRRLEIARCMVTRPE--LLMLDEPAAGLNPKETDELDHLIVELRDRhKVSVLLIEHDMKlVMGISDRI 180
Cdd:cd03238 82 GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDL-GNTVILIEHNLD-VLSSADWI 158
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
40-197 |
4.38e-07 |
|
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: 49.42 E-value: 4.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 40 RTFQhvrLFREMTVIENLLVAQHQHLKSGVFAgllktpafrraeaeaLARAAEWLERVGLLSMANRSAGNLAYGQQRRLE 119
Cdd:TIGR03269 117 RTFA---LYGDDTVLDNVLEALEEIGYEGKEA---------------VGRAVDLIEMVQLSHRITHIARDLSGGEKQRVV 178
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1540799172 120 IARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEI 197
Cdd:TIGR03269 179 LARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIKEEGTPDEV 256
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
28-192 |
4.42e-07 |
|
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: 48.81 E-value: 4.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 28 LAGQAIARMGVVRTFQHVRLFRemTVIENLLVAQHQHlksgvFAGLLKTPAFRRAEAEALARAAEWLERVGLLSMANRSA 107
Cdd:cd03234 69 FNGQPRKPDQFQKCVAYVRQDD--ILLPGLTVRETLT-----YTAILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 108 GNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVLLIEHDMKLVMGISDRIYVVNQGT 187
Cdd:cd03234 142 KGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGE 221
|
....*
gi 1540799172 188 PLAQG 192
Cdd:cd03234 222 IVYSG 226
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
108-186 |
5.80e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.14 E-value: 5.80e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1540799172 108 GNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRhKVSVLLIEHDMKLVMGISDRIYVVNQG 186
Cdd:PRK11288 395 MNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREG 472
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-197 |
6.56e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.85 E-value: 6.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKL--RDRHLEGLAGQAIARMGVVRtfQHVRLFREMTVIENllvaqhqhlksgVFAGLLKTPA 78
Cdd:PRK10762 44 STMMKVLTGIYTRDAGSILYlgKEVTFNGPKSSQEAGIGIIH--QELNLIPQLTIAEN------------IFLGREFVNR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 79 FRRAEaealaraaeW----------LERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDEL 148
Cdd:PRK10762 110 FGRID---------WkkmyaeadklLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1540799172 149 DHLIVELRDRHkVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEI 197
Cdd:PRK10762 181 FRVIRELKSQG-RGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADL 228
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
1-197 |
7.06e-07 |
|
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: 48.94 E-value: 7.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAIaRMGVVRTFQHVRLFREmTVIENLlvaqhqhlksgvfagllktpAFR 80
Cdd:TIGR02203 372 STLVNLIPRFYEPDSGQILLDGHDLADYTLASL-RRQVALVSQDVVLFND-TIANNI--------------------AYG 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 81 RAEAEALARAAEWLERVGLLSMANRS-----------AGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGL-NPKE---T 145
Cdd:TIGR02203 430 RTEQADRAEIERALAAAYAQDFVDKLplgldtpigenGVLLSGGQRQRLAIARALLKDAPILILDEATSALdNESErlvQ 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1540799172 146 DELDHLiveLRDRhkvSVLLIEHDMKLVMGiSDRIYVVNQGTPLAQGTPAEI 197
Cdd:TIGR02203 510 AALERL---MQGR---TTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNEL 554
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
113-197 |
9.20e-07 |
|
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: 47.52 E-value: 9.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 113 GQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRhKVSVLLIEHDMKLVMGI-SDRIYVVNQGTPLAQ 191
Cdd:cd03217 108 GEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKS 186
|
....*.
gi 1540799172 192 GtPAEI 197
Cdd:cd03217 187 G-DKEL 191
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
94-209 |
9.69e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 47.90 E-value: 9.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 94 LERVGLLSMANRSAGNLAYGQQRRLEIARCM---------VTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVL 164
Cdd:PRK13547 130 LALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVL 209
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1540799172 165 LIEHDMKLVMGISDRIYVVNQGTPLAQGTPAEIRnNPDVIRAYLG 209
Cdd:PRK13547 210 AIVHDPNLAARHADRIAMLADGAIVAHGAPADVL-TPAHIARCYG 253
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
105-197 |
1.12e-06 |
|
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: 47.48 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 105 RSAGnLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPketdELDHLIveLRDRHKVS----VLLIEHDMKLVMGiSDRI 180
Cdd:cd03252 135 QGAG-LSGGQRQRIAIARALIHNPRILIFDEATSALDY----ESEHAI--MRNMHDICagrtVIIIAHRLSTVKN-ADRI 206
|
90
....*....|....*..
gi 1540799172 181 YVVNQGTPLAQGTPAEI 197
Cdd:cd03252 207 IVMEKGRIVEQGSHDEL 223
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
7-154 |
1.51e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 47.11 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 7 LTGFYRPSGGTIKLRdrhleglaGQAIARMGVvrTFQHVRLF--------REMTVIENLLVAQHQHLKSGVFAgllktpa 78
Cdd:PRK13538 47 LAGLARPDAGEVLWQ--------GEPIRRQRD--EYHQDLLYlghqpgikTELTALENLRFYQRLHGPGDDEA------- 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1540799172 79 frraeaealaraaEW--LERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVE 154
Cdd:PRK13538 110 -------------LWeaLAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQ 174
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1-186 |
1.68e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.80 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAIARMGVVRTFQHVRLFREMTVIENLLVAQHQhlKSGVFAGLLK----T 76
Cdd:PRK10982 38 STLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQELNLVLQRSVMDNMWLGRYP--TKGMFVDQDKmyrdT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 77 PAFrraeaealaraaewLERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELR 156
Cdd:PRK10982 116 KAI--------------FDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLK 181
|
170 180 190
....*....|....*....|....*....|
gi 1540799172 157 DRhKVSVLLIEHDMKLVMGISDRIYVVNQG 186
Cdd:PRK10982 182 ER-GCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
110-201 |
2.00e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 47.49 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 110 LAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVLLIEHDMKLVMGISDRIYVVNQGTPL 189
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
90
....*....|..
gi 1540799172 190 AQGTPAEIRNNP 201
Cdd:PRK15093 239 ETAPSKELVTTP 250
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
94-198 |
2.17e-06 |
|
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: 47.47 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 94 LERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAglnpketdeldHLIVELR-----------DRHKVS 162
Cdd:COG1245 440 IKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSA-----------HLDVEQRlavakairrfaENRGKT 508
|
90 100 110
....*....|....*....|....*....|....*....
gi 1540799172 163 VLLIEHDMKLVMGISDRIYVVNqGTPLAQGT---PAEIR 198
Cdd:COG1245 509 AMVVDHDIYLIDYISDRLMVFE-GEPGVHGHasgPMDMR 546
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
113-196 |
2.48e-06 |
|
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: 46.45 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 113 GQQRRLEIARCMVTRPELLMLDEPAAGLN-PKETDELDHLIVELRDRhkvSVLLIEHDMKLVMGiSDRIYVVNQGTPLAQ 191
Cdd:cd03253 141 GEKQRVAIARAILKNPPILLLDEATSALDtHTEREIQAALRDVSKGR---TTIVIAHRLSTIVN-ADKIIVLKDGRIVER 216
|
....*
gi 1540799172 192 GTPAE 196
Cdd:cd03253 217 GTHEE 221
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
95-211 |
3.95e-06 |
|
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: 46.21 E-value: 3.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 95 ERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELrDRHKVSVLLIEHDMKLVM 174
Cdd:cd03236 125 DQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIREL-AEDDNYVLVVEHDLAVLD 203
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1540799172 175 GISDRIYVVnQGTPLAQGT---PAEIRNNPDV-IRAYLGEE 211
Cdd:cd03236 204 YLSDYIHCL-YGEPGAYGVvtlPKSVREGINEfLDGYLPTE 243
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
113-192 |
3.98e-06 |
|
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: 45.62 E-value: 3.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 113 GQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQG 192
Cdd:cd03213 115 GERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
109-196 |
4.30e-06 |
|
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: 46.07 E-value: 4.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 109 NLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNpKET-----DELDHLiveLRDRhkvSVLLIEHDMKLVMGiSDRIYVV 183
Cdd:cd03251 138 KLSGGQRQRIAIARALLKDPPILILDEATSALD-TESerlvqAALERL---MKNR---TTFVIAHRLSTIEN-ADRIVVL 209
|
90
....*....|...
gi 1540799172 184 NQGTPLAQGTPAE 196
Cdd:cd03251 210 EDGKIVERGTHEE 222
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
113-201 |
4.54e-06 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 46.05 E-value: 4.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 113 GQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQG 192
Cdd:COG4170 162 GECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESG 241
|
....*....
gi 1540799172 193 TPAEIRNNP 201
Cdd:COG4170 242 PTEQILKSP 250
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
109-193 |
5.14e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 45.26 E-value: 5.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 109 NLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVLLIEHDMKLVMGISDRIYVVnQGTP 188
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVF-EGEP 149
|
....*
gi 1540799172 189 LAQGT 193
Cdd:cd03222 150 GVYGI 154
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
94-196 |
6.25e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 46.19 E-value: 6.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 94 LERVGLLSMANRSAG------NLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVLLIE 167
Cdd:TIGR00955 145 LQALGLRKCANTRIGvpgrvkGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIH 224
|
90 100
....*....|....*....|....*....
gi 1540799172 168 HDMKLVMGISDRIYVVNQGTPLAQGTPAE 196
Cdd:TIGR00955 225 QPSSELFELFDKIILMAEGRVAYLGSPDQ 253
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
94-209 |
6.83e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 45.75 E-value: 6.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 94 LERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKvSVLLIEHDMKlV 173
Cdd:PRK13644 121 LAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGK-TIVYITHNLE-E 198
|
90 100 110
....*....|....*....|....*....|....*.
gi 1540799172 174 MGISDRIYVVNQGTPLAQGTPAEIRNNPDVirAYLG 209
Cdd:PRK13644 199 LHDADRIIVMDRGKIVLEGEPENVLSDVSL--QTLG 232
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
94-198 |
6.90e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.96 E-value: 6.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 94 LERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAglnpketdeldHLIVELR-----------DRHKVS 162
Cdd:PRK13409 438 IKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSA-----------HLDVEQRlavakairriaEEREAT 506
|
90 100 110
....*....|....*....|....*....|....*....
gi 1540799172 163 VLLIEHDMKLVMGISDRIyVVNQGTPLAQGT---PAEIR 198
Cdd:PRK13409 507 ALVVDHDIYMIDYISDRL-MVFEGEPGKHGHasgPMDMR 544
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
94-189 |
7.59e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 44.95 E-value: 7.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 94 LERVGLLSMAN--RSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVLLIEHDMK 171
Cdd:COG2401 119 LNAVGLSDAVLwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYD 198
|
90
....*....|....*....
gi 1540799172 172 LVMGIS-DRIYVVNQGTPL 189
Cdd:COG2401 199 VIDDLQpDLLIFVGYGGVP 217
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
110-201 |
1.42e-05 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 44.64 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 110 LAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVLLIEHDMKLVMGISDRIYVVNQGTpL 189
Cdd:PRK11000 134 LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGR-V 212
|
90
....*....|...
gi 1540799172 190 AQ-GTPAEIRNNP 201
Cdd:PRK11000 213 AQvGKPLELYHYP 225
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
113-186 |
1.65e-05 |
|
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: 43.74 E-value: 1.65e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1540799172 113 GQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRhKVSVLLIEHDMKLVmGISDRIYVVNQG 186
Cdd:cd03246 100 GQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAA-GATRIVIAHRPETL-ASADRILVLEDG 171
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
108-186 |
2.06e-05 |
|
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: 44.00 E-value: 2.06e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1540799172 108 GNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHkvSVLLIEHDMKLVMGiSDRIYVVNQG 186
Cdd:cd03248 149 SQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVER-ADQILVLDGG 224
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
113-196 |
2.68e-05 |
|
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: 43.68 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 113 GQQRRLEIARCMVTRPELLMLDEpaaglnpkETDELD----HLIVELRDRHKVS--VLLIEHDMKLVMGiSDRIYVVNQG 186
Cdd:cd03249 143 GQKQRIAIARALLRNPKILLLDE--------ATSALDaeseKLVQEALDRAMKGrtTIVIAHRLSTIRN-ADLIAVLQNG 213
|
90
....*....|
gi 1540799172 187 TPLAQGTPAE 196
Cdd:cd03249 214 QVVEQGTHDE 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-187 |
2.92e-05 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 43.90 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLrdrhleglaGQAIaRMGVVRtfQHVRLFR-EMTVIENLL----VAQHQHLkSGVFAGLLK 75
Cdd:COG0488 355 STLLKLLAGELEPDSGTVKL---------GETV-KIGYFD--QHQEELDpDKTVLDELRdgapGGTEQEV-RGYLGRFLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 76 TPAfrraeaealaraaEWLERVGLLSManrsagnlayGQQRRLEIARCMVTRPELLMLDEPaaglnpkeTDELD----HL 151
Cdd:COG0488 422 SGD-------------DAFKPVGVLSG----------GEKARLALAKLLLSPPNVLLLDEP--------TNHLDietlEA 470
|
170 180 190
....*....|....*....|....*....|....*.
gi 1540799172 152 IVELRDRHKVSVLLIEHDMKLVMGISDRIYVVNQGT 187
Cdd:COG0488 471 LEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGG 506
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1-193 |
4.26e-05 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 43.55 E-value: 4.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 1 TTVFNCLTGFYRPSGGTIKLRDRHLEGLAGQAIaRMGVVRT-----------FQHVRLFREMT---VIENLLVAQhqhlk 66
Cdd:PRK10790 381 STLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL-RQGVAMVqqdpvvladtfLANVTLGRDISeeqVWQALETVQ----- 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 67 sgvFAGLLKT-PAfrraeaealaraaewlervGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKET 145
Cdd:PRK10790 455 ---LAELARSlPD-------------------GLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTE 512
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1540799172 146 DELDHLIVELRDRhkVSVLLIEHDMKLVMGiSDRIYVVNQGTPLAQGT 193
Cdd:PRK10790 513 QAIQQALAAVREH--TTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGT 557
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
98-200 |
4.27e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.81 E-value: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 98 GLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKetdeLDHLIVE-LRDRHK-VSVLLIEHDMKLVMG 175
Cdd:PLN03232 1360 GLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVR----TDSLIQRtIREEFKsCTMLVIAHRLNTIID 1435
|
90 100
....*....|....*....|....*
gi 1540799172 176 iSDRIYVVNQGTPLAQGTPAEIRNN 200
Cdd:PLN03232 1436 -CDKILVLSSGQVLEYDSPQELLSR 1459
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
101-186 |
8.71e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.92 E-value: 8.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 101 SMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAaglNPKETDELDHLIVELRdRHKVSVLLIEHDMKLVMGISDRI 180
Cdd:PLN03073 619 NLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPS---NHLDLDAVEALIQGLV-LFQGGVLMVSHDEHLISGSVDEL 694
|
....*.
gi 1540799172 181 YVVNQG 186
Cdd:PLN03073 695 WVVSEG 700
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
104-186 |
1.16e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 42.08 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 104 NRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVsVLLIEHDMKLVMGISDRIYVV 183
Cdd:PRK09700 404 NQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKV-ILMVSSELPEIITVCDRIAVF 482
|
...
gi 1540799172 184 NQG 186
Cdd:PRK09700 483 CEG 485
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
105-197 |
1.37e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.12 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 105 RSAGNLAYGQQRRLEIARCM---VTRPELLMLDEPAAGLNPKETDELDHLIVELRDR-HkvSVLLIEHDMKLVMgISDri 180
Cdd:PRK00635 805 RPLSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQgH--TVVIIEHNMHVVK-VAD-- 879
|
90 100
....*....|....*....|....*
gi 1540799172 181 YVVNQGTP--------LAQGTPAEI 197
Cdd:PRK00635 880 YVLELGPEggnlggylLASCSPEEL 904
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
105-211 |
1.44e-04 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 42.14 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 105 RSAGnLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPK-ETDELDHLIVELRDRhkvSVLLIEH---DMKLVmgisDRI 180
Cdd:PRK11174 482 QAAG-LSVGQAQRLALARALLQPCQLLLLDEPTASLDAHsEQLVMQALNAASRRQ---TTLMVTHqleDLAQW----DQI 553
|
90 100 110
....*....|....*....|....*....|.
gi 1540799172 181 YVVNQGTPLAQGTPAEIRNNPDVIRAYLGEE 211
Cdd:PRK11174 554 WVMQDGQIVQQGDYAELSQAGGLFATLLAHR 584
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
98-193 |
1.60e-04 |
|
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: 41.24 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 98 GLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVLLIEHDMKLVMGIS 177
Cdd:cd03237 104 QIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLA 183
|
90
....*....|....*.
gi 1540799172 178 DRIyVVNQGTPLAQGT 193
Cdd:cd03237 184 DRL-IVFEGEPSVNGV 198
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
95-183 |
1.76e-04 |
|
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: 41.69 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 95 ERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKvSVLLIEHDMKLVM 174
Cdd:COG1245 198 EKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGK-YVLVVEHDLAILD 276
|
....*....
gi 1540799172 175 GISDRIYVV 183
Cdd:COG1245 277 YLADYVHIL 285
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
105-197 |
1.87e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.92 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 105 RSAGNLAYGQQRRLEIARCM---VTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKvSVLLIEHDMKlVMGISDriY 181
Cdd:TIGR00630 825 QPATTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGN-TVVVIEHNLD-VIKTAD--Y 900
|
90 100
....*....|....*....|....
gi 1540799172 182 VV--------NQGTPLAQGTPAEI 197
Cdd:TIGR00630 901 IIdlgpeggdGGGTVVASGTPEEV 924
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
94-211 |
3.05e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 40.95 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 94 LERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDrhKVSVLLIEHDMKLV 173
Cdd:PRK13409 197 VERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHDLAVL 274
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1540799172 174 MGISDRIYVVnQGTPLAQG---TPAEIRNNPDV-IRAYLGEE 211
Cdd:PRK13409 275 DYLADNVHIA-YGEPGAYGvvsKPKGVRVGINEyLKGYLPEE 315
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
109-194 |
3.56e-04 |
|
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: 40.09 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 109 NLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPketdELDHLIVE-LRDR-HKVSVLLIEHDMKLVMGIsDRIYVVNQG 186
Cdd:cd03369 125 NLSQGQRQLLCLARALLKRPRVLVLDEATASIDY----ATDALIQKtIREEfTNSTILTIAHRLRTIIDY-DKILVMDAG 199
|
....*...
gi 1540799172 187 TPLAQGTP 194
Cdd:cd03369 200 EVKEYDHP 207
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
94-173 |
4.26e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 39.90 E-value: 4.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 94 LERVGLLSMANRSAGNLAYgqqrRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVS-VLLIEHDMKL 172
Cdd:cd03240 110 LDMRGRCSGGEKVLASLII----RLALAETFGSNCGILALDEPTTNLDEENIEESLAEIIEERKSQKNFqLIVITHDEEL 185
|
.
gi 1540799172 173 V 173
Cdd:cd03240 186 V 186
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
94-208 |
5.25e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.44 E-value: 5.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 94 LERVGL--LSMaNRSAGNLAYGQ-QR-RL--EI-ARCM-VtrpeLLMLDEPAAGLNPKETDELDHLIVELRDRHKvSVLL 165
Cdd:PRK00349 473 LVDVGLdyLTL-SRSAGTLSGGEaQRiRLatQIgSGLTgV----LYVLDEPSIGLHQRDNDRLIETLKHLRDLGN-TLIV 546
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1540799172 166 IEHDmKLVMGISDriYVV--------NQGTPLAQGTPAEIRNNPDVIR-AYL 208
Cdd:PRK00349 547 VEHD-EDTIRAAD--YIVdigpgagvHGGEVVASGTPEEIMKNPNSLTgQYL 595
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
109-197 |
5.32e-04 |
|
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: 40.31 E-value: 5.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 109 NLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNpKETDELDHLIVELRdRHKVSVLLIEHDMKLVMGISdRIYVVNQGTP 188
Cdd:TIGR00957 1421 NLSVGQRQLVCLARALLRKTKILVLDEATAAVD-LETDNLIQSTIRTQ-FEDCTVLTIAHRLNTIMDYT-RVIVLDKGEV 1497
|
....*....
gi 1540799172 189 LAQGTPAEI 197
Cdd:TIGR00957 1498 AEFGAPSNL 1506
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
101-173 |
7.15e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.01 E-value: 7.15e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1540799172 101 SMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVLLIEHDMKLV 173
Cdd:PTZ00265 571 TLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTI 643
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
113-201 |
8.50e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 39.44 E-value: 8.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 113 GQQRRLEIARCMVTRPELLMLDEPAAGLNPKetdeLD-HLIVELRDRH---KVSVLLIEHDMKLVMGISDRIYVVNQGTP 188
Cdd:PRK11650 138 GQRQRVAMGRAIVREPAVFLFDEPLSNLDAK----LRvQMRLEIQRLHrrlKTTSLYVTHDQVEAMTLADRVVVMNGGVA 213
|
90
....*....|...
gi 1540799172 189 LAQGTPAEIRNNP 201
Cdd:PRK11650 214 EQIGTPVEVYEKP 226
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
109-192 |
9.15e-04 |
|
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: 39.11 E-value: 9.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 109 NLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNpKETDEldHLIVELRD--RHKvSVLLIEHDMKLvMGISDRIYVVNQG 186
Cdd:cd03245 140 GLSGGQRQAVALARALLNDPPILLLDEPTSAMD-MNSEE--RLKERLRQllGDK-TLIIITHRPSL-LDLVDRIIVMDSG 214
|
....*.
gi 1540799172 187 TPLAQG 192
Cdd:cd03245 215 RIVADG 220
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
109-200 |
1.27e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 39.34 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 109 NLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKEtdelDHLIVE-LRDRHK-VSVLLIEHDMKLVMGiSDRIYVVNQG 186
Cdd:PLN03130 1374 NFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRT----DALIQKtIREEFKsCTMLIIAHRLNTIID-CDRILVLDAG 1448
|
90
....*....|....
gi 1540799172 187 TPLAQGTPAEIRNN 200
Cdd:PLN03130 1449 RVVEFDTPENLLSN 1462
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
113-202 |
1.35e-03 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 38.53 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 113 GQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLIVELRDRHKVSVLLIEHDMKLVMGISDRIYVVNQGTPLAQG 192
Cdd:PRK10418 144 GMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQG 223
|
90
....*....|
gi 1540799172 193 TPAEIRNNPD 202
Cdd:PRK10418 224 DVETLFNAPK 233
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
94-152 |
1.60e-03 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 38.29 E-value: 1.60e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1540799172 94 LERVGLLSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLI 152
Cdd:PRK13543 122 LAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMI 180
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
108-169 |
2.20e-03 |
|
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: 38.38 E-value: 2.20e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1540799172 108 GNLAYGQQRRLEIARCMVTRPELLMLDEPaaglnpkeTDELDHLIVELRDRH----KVSVLLIEHD 169
Cdd:TIGR03719 160 TKLSGGERRRVALCRLLLSKPDMLLLDEP--------TNHLDAESVAWLERHlqeyPGTVVAVTHD 217
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
94-174 |
3.61e-03 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 37.86 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540799172 94 LERVGL------LSMANRSAGNLAYGQQRRLEIARCMVTRPELLMLDEPAAGLNPKETDELDHLiveLRDRHK----VSV 163
Cdd:COG4178 464 LEAVGLghlaerLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL---LREELPgttvISV 540
|
90
....*....|....*.
gi 1540799172 164 -----LLIEHDMKLVM 174
Cdd:COG4178 541 ghrstLAAFHDRVLEL 556
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
113-140 |
4.01e-03 |
|
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: 36.86 E-value: 4.01e-03
10 20
....*....|....*....|....*...
gi 1540799172 113 GQQRRLEIARCMVTRPELLMLDEPAAGL 140
Cdd:cd03233 122 GERKRVSIAEALVSRASVLCWDNSTRGL 149
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
110-140 |
5.33e-03 |
|
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: 36.45 E-value: 5.33e-03
10 20 30
....*....|....*....|....*....|.
gi 1540799172 110 LAYGQQRRLEIARCMVTRPELLMLDEPAAGL 140
Cdd:cd03232 109 LSVEQRKRLTIGVELAAKPSILFLDEPTSGL 139
|
|
| |
