|
Name |
Accession |
Description |
Interval |
E-value |
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
13-254 |
9.77e-121 |
|
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: 344.66 E-value: 9.77e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 13 LLDVNGIEVIYNHvILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKgergdVTKGYIQYRDERIERLSPAELV 92
Cdd:COG0410 3 MLEVENLHAGYGG-IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLP-----PRSGSIRFDGEDITGLPPHRIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 93 KRGVVQVMEGRHCFAHLTIEENLLTGAYTRElSRGDISIALERVYQYFPRLKQRRGSQAGYTSGGEQQMTAIGRALMASP 172
Cdd:COG0410 77 RLGIGYVPEGRRIFPSLTVEENLLLGAYARR-DRAEVRADLERVYELFPRLKERRRQRAGTLSGGEQQMLAIGRALMSRP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 173 NMILLDEPSMGLAPQIVEEIFEIVRDLNqREGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDLAQNEDVKEFYL 252
Cdd:COG0410 156 KLLLLDEPSLGLAPLIVEEIFEIIRRLN-REGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEVREAYL 234
|
..
gi 695928685 253 GI 254
Cdd:COG0410 235 GV 236
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
14-244 |
9.86e-100 |
|
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: 290.87 E-value: 9.86e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 14 LDVNGIEVIYNHvILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKgergdVTKGYIQYRDERIERLSPAELVK 93
Cdd:cd03224 1 LEVENLNAGYGK-SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLP-----PRSGSIRFDGRDITGLPPHERAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 94 RGVVQVMEGRHCFAHLTIEENLLTGAYTRElsRGDISIALERVYQYFPRLKQRRGSQAGYTSGGEQQMTAIGRALMASPN 173
Cdd:cd03224 75 AGIGYVPEGRRIFPELTVEENLLLGAYARR--RAKRKARLERVYELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695928685 174 MILLDEPSMGLAPQIVEEIFEIVRDLNqREGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDLAQN 244
Cdd:cd03224 153 LLLLDEPSEGLAPKIVEEIFEAIRELR-DEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
11-253 |
5.88e-65 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 203.19 E-value: 5.88e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 11 KVLLDVNGIEVIYNHvILVLKGVSLRVPEGKIVALLGANGAGKTTTLravsNLLKGERgDVTKGYIQYRDERIERLSPAE 90
Cdd:PRK11614 3 KVMLSFDKVSAHYGK-IQALHEVSLHINQGEIVTLIGANGAGKTTLL----GTLCGDP-RATSGRIVFDGKDITDWQTAK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 91 LVKRGVVQVMEGRHCFAHLTIEENLLTGAYTRElsRGDISIALERVYQYFPRLKQRRGSQAGYTSGGEQQMTAIGRALMA 170
Cdd:PRK11614 77 IMREAVAIVPEGRRVFSRMTVEENLAMGGFFAE--RDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 171 SPNMILLDEPSMGLAPQIVEEIFEIVRDLNQrEGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDLAQNEDVKEF 250
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPIIIQQIFDTIEQLRE-QGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSA 233
|
...
gi 695928685 251 YLG 253
Cdd:PRK11614 234 YLG 236
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
14-247 |
5.67e-47 |
|
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: 156.83 E-value: 5.67e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 14 LDVNGIEVIYNHViLVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKgergdVTKGYIQYRDERIERLSPAELVK 93
Cdd:cd03219 1 LEVRGLTKRFGGL-VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLR-----PTSGSVLFDGEDITGLPPHEIAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 94 RGVV---QVMEgrhCFAHLTIEENLLTGAYTRE-------LSRGDISIALERVYQY--FPRLKQRRGSQAGYTSGGEQQM 161
Cdd:cd03219 75 LGIGrtfQIPR---LFPELTVLENVMVAAQARTgsglllaRARREEREARERAEELleRVGLADLADRPAGELSYGQQRR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 162 TAIGRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQReGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDL 241
Cdd:cd03219 152 LEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEV 230
|
....*.
gi 695928685 242 AQNEDV 247
Cdd:cd03219 231 RNNPRV 236
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
29-253 |
7.50e-46 |
|
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: 154.43 E-value: 7.50e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKgergdVTKGYIQYRDERIERLSPAELVKRGVV---QVMegrHC 105
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYR-----PTSGRILFDGRDITGLPPHRIARLGIArtfQNP---RL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 106 FAHLTIEENLLTGAYTRELSRGDISI-------------------ALERVyqyfpRLKQRRGSQAGYTSGGEQQMTAIGR 166
Cdd:COG0411 91 FPELTVLENVLVAAHARLGRGLLAALlrlprarreereareraeeLLERV-----GLADRADEPAGNLSYGQQRRLEIAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 167 ALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDLAQNED 246
Cdd:COG0411 166 ALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVRADPR 245
|
....*..
gi 695928685 247 VKEFYLG 253
Cdd:COG0411 246 VIEAYLG 252
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
29-253 |
6.02e-42 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 144.02 E-value: 6.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKgergdVTKGYIQYRDERIERLSPAELVKRGV--------Vqvm 100
Cdd:COG1137 18 VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVK-----PDSGRIFLDGEDITHLPMHKRARLGIgylpqeasI--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 101 egrhcFAHLTIEENLLTGAYTRELSRGDISIALERVYQYFpRLKQRRGSQAGYTSGGEQQMTAIGRALMASPNMILLDEP 180
Cdd:COG1137 90 -----FRKLTVEDNILAVLELRKLSKKEREERLEELLEEF-GITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695928685 181 SMGLAPQIVEEIFEIVRDLNQReGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDLAQNEDVKEFYLG 253
Cdd:COG1137 164 FAGVDPIAVADIQKIIRHLKER-GIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPLVRKVYLG 235
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
14-253 |
2.30e-41 |
|
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: 142.30 E-value: 2.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 14 LDVNGIEVIYNHViLVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKgergdVTKGYIQYRDERIERLSPAELVK 93
Cdd:cd03218 1 LRAENLSKRYGKR-KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVK-----PDSGKILLDGQDITKLPMHKRAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 94 RGVVQVMEGRHCFAHLTIEENLLTGAYTRELSRGDISIALERVYQYFpRLKQRRGSQAGYTSGGEQQMTAIGRALMASPN 173
Cdd:cd03218 75 LGIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEF-HITHLRKSKASSLSGGERRRVEIARALATNPK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 174 MILLDEPSMGLAPQIVEEIFEIVRDLNQReGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDLAQNEDVKEFYLG 253
Cdd:cd03218 154 FLLLDEPFAGVDPIAVQDIQKIIKILKDR-GIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKVYLG 232
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
13-251 |
9.61e-41 |
|
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: 141.33 E-value: 9.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 13 LLDVNGIEVIYNHVIlVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTkgyiqYRDERIERLSPAELV 92
Cdd:COG1120 1 MLEAENLSVGYGGRP-VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVL-----LDGRDLASLSRRELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 93 KR-GVV-QVMEGRhcfAHLTIEENLLTGAY-----TRELSRGDISI---ALERV------YQYFPRLkqrrgsqagytSG 156
Cdd:COG1120 75 RRiAYVpQEPPAP---FGLTVRELVALGRYphlglFGRPSAEDREAveeALERTglehlaDRPVDEL-----------SG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 157 GEQQMTAIGRALMASPNMILLDEPSMGLAP--QIveEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILENGRVMM 234
Cdd:COG1120 141 GERQRVLIARALAQEPPLLLLDEPTSHLDLahQL--EVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVA 218
|
250
....*....|....*..
gi 695928685 235 DGAASDLAQNEDVKEFY 251
Cdd:COG1120 219 QGPPEEVLTPELLEEVY 235
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
14-260 |
1.56e-37 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 132.49 E-value: 1.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 14 LDVNGIEVIYNHVIlVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKgergdVTKGYIQYRDERIERLSPAelVK 93
Cdd:COG1131 1 IEVRGLTKRYGDKT-ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLR-----PTSGEVRVLGEDVARDPAE--VR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 94 R--GVvqVMEGRHCFAHLTIEENLLTGAYTRELSRGDISIALERVYQYFpRLKQRRGSQAGYTSGGEQQMTAIGRALMAS 171
Cdd:COG1131 73 RriGY--VPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELF-GLTDAADRKVGTLSGGMKQRLGLALALLHD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 172 PNMILLDEPSMGLAPQIVEEIFEIVRDLNqREGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDLAQN--EDVke 249
Cdd:COG1131 150 PELLILDEPTSGLDPEARRELWELLRELA-AEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARllEDV-- 226
|
250
....*....|.
gi 695928685 250 fYLGISSGERK 260
Cdd:COG1131 227 -FLELTGEEAR 236
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
14-251 |
2.30e-36 |
|
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: 129.61 E-value: 2.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 14 LDVNGIEVIYNHVILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGergdvTKGYIQYRDERIERLSPAEL-- 91
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEP-----TSGSVLIDGTDINKLKGKALrq 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 92 VKRGVVQVMEGRHCFAHLTIEENLLTG--AYT-------RELSRGDISIA---LERVyQYFPRLKQRrgsqAGYTSGGEQ 159
Cdd:cd03256 76 LRRQIGMIFQQFNLIERLSVLENVLSGrlGRRstwrslfGLFPKEEKQRAlaaLERV-GLLDKAYQR----ADQLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 160 QMTAIGRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAAS 239
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPA 230
|
250
....*....|..
gi 695928685 240 DLaQNEDVKEFY 251
Cdd:cd03256 231 EL-TDEVLDEIY 241
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
13-252 |
6.24e-36 |
|
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: 128.44 E-value: 6.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 13 LLDVNGIEVIYNHViLVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTKGYIQYRDERIErlspaelV 92
Cdd:COG4555 1 MIEVENLSKKYGKV-PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-------A 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 93 KRGVVQVMEGRHCFAHLTIEENLltgAYTRELSRGDISIALERVYQYFPRL---KQRRGSQAGYtSGGEQQMTAIGRALM 169
Cdd:COG4555 73 RRQIGVLPDERGLYDRLTVRENI---RYFAELYGLFDEELKKRIEELIELLgleEFLDRRVGEL-STGMKKKVALARALV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 170 ASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQrEGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDLAQ---NED 246
Cdd:COG4555 149 HDPKVLLLDEPTNGLDVMARRLLREILRALKK-EGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREeigEEN 227
|
....*.
gi 695928685 247 VKEFYL 252
Cdd:COG4555 228 LEDAFV 233
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
29-253 |
8.43e-36 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 128.16 E-value: 8.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTkgyiqYRDERIERLSPAELVKRGVVQVMEGRHCFAH 108
Cdd:TIGR04406 16 VVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKIL-----IDGQDITHLPMHERARLGIGYLPQEASIFRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 109 LTIEENLLTGAYTRE-LSRGDISIALERVYQYFpRLKQRRGSQAGYTSGGEQQMTAIGRALMASPNMILLDEPSMGLAPQ 187
Cdd:TIGR04406 91 LTVEENIMAVLEIRKdLDRAEREERLEALLEEF-QISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAGVDPI 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695928685 188 IVEEIFEIVRDLNQReGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDLAQNEDVKEFYLG 253
Cdd:TIGR04406 170 AVGDIKKIIKHLKER-GIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVRRVYLG 234
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
14-246 |
2.82e-35 |
|
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: 126.29 E-value: 2.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 14 LDVNGIEVIYNHVILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTkgyiqYRDERIERLSPAELVK 93
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVL-----VDGKDITKKNLRELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 94 R-GVV-Q------VMEgrhcfahlTIEENLLTGAYTRELSRGDISI----ALERVyqyfpRLKQRRGSQAGYTSGGEQQM 161
Cdd:COG1122 76 KvGLVfQnpddqlFAP--------TVEEDVAFGPENLGLPREEIRErveeALELV-----GLEHLADRPPHELSGGQKQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 162 TAIGRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQrEGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDL 241
Cdd:COG1122 143 VAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNK-EGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
....*
gi 695928685 242 AQNED 246
Cdd:COG1122 222 FSDYE 226
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
15-236 |
2.01e-34 |
|
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: 122.54 E-value: 2.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 15 DVNGIEVIYNHVIlVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTkgyiqYRDERIERLSPAELVKR 94
Cdd:cd03214 1 EVENLSVGYGGRT-VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIL-----LDGKDLASLSPKELARK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 95 -GVV-QVMEgrhcfahltieenlLTGaytrelsrgdisiALERVYQYFPRLkqrrgsqagytSGGEQQMTAIGRALMASP 172
Cdd:cd03214 75 iAYVpQALE--------------LLG-------------LAHLADRPFNEL-----------SGGERQRVLLARALAQEP 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695928685 173 NMILLDEPSMGLAP--QIveEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILENGRVMMDG 236
Cdd:cd03214 117 PILLLDEPTSHLDIahQI--ELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
14-232 |
2.84e-34 |
|
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: 122.12 E-value: 2.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 14 LDVNGIEVIYNHVIlVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKgergdVTKGYIQYRDERIERlsPAELVK 93
Cdd:cd03230 1 IEVRNLSKRYGKKT-ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLK-----PDSGEIKVLGKDIKK--EPEEVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 94 RGVVQVMEGRHCFAHLTIEENLltgaytrELSRGdisialervyqyfprLKQRrgsqagytsggeqqmTAIGRALMASPN 173
Cdd:cd03230 73 RRIGYLPEEPSLYENLTVRENL-------KLSGG---------------MKQR---------------LALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 695928685 174 MILLDEPSMGLAPQIVEEIFEIVRDLNQrEGVSFLLAEQNTNIALRYADYGYILENGRV 232
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKK-EGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
16-231 |
6.00e-33 |
|
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: 119.88 E-value: 6.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 16 VNGIEVIYNH-VILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKgergdVTKGYIQYRDERIERLSPAELVKR 94
Cdd:cd03225 2 LKNLSFSYPDgARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLG-----PTSGEVLVDGKDLTKLSLKELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 95 -GVV-QvmEGRHCFAHLTIEENLLTGAYTRELSRGDISIALERVYQYFpRLKQRRGSQAGYTSGGEQQMTAIGRALMASP 172
Cdd:cd03225 77 vGLVfQ--NPDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELV-GLEGLRDRSPFTLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 695928685 173 NMILLDEPSMGLAPQIVEEIFEIVRDLNQrEGVSFLLAEQNTNIALRYADYGYILENGR 231
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKA-EGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
14-236 |
7.55e-32 |
|
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: 116.85 E-value: 7.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 14 LDVNGIEVIYNHVIlVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTKGyiqyrDERIERLSPAelvK 93
Cdd:cd03259 1 LELKGLSKTYGSVR-ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILID-----GRDVTGVPPE---R 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 94 RGVVQVMEGRHCFAHLTIEENLLTGAYTRELSRGDISialERVYQY-----FPRLKQRRGSQagyTSGGEQQMTAIGRAL 168
Cdd:cd03259 72 RNIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIR---ARVRELlelvgLEGLLNRYPHE---LSGGQQQRVALARAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695928685 169 MASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILENGRVMMDG 236
Cdd:cd03259 146 AREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
10-253 |
1.19e-31 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 117.40 E-value: 1.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 10 SKVLLDVNGIEVIYNHvILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGergdvTKGYIQYRDERIERLSPA 89
Cdd:PRK11300 2 SQPLLSVSGLMMRFGG-LLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKP-----TGGTILLRGQHIEGLPGH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 90 ELVKRGVVQVMEGRHCFAHLTIEENLLTgAYTRELSRGDIS-------------IALERVYQYFPR--LKQRRGSQAGYT 154
Cdd:PRK11300 76 QIARMGVVRTFQHVRLFREMTVIENLLV-AQHQQLKTGLFSgllktpafrraesEALDRAATWLERvgLLEHANRQAGNL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 155 SGGEQQMTAIGRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILENGRVMM 234
Cdd:PRK11300 155 AYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLA 234
|
250
....*....|....*....
gi 695928685 235 DGAASDLAQNEDVKEFYLG 253
Cdd:PRK11300 235 NGTPEEIRNNPDVIKAYLG 253
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
14-231 |
3.99e-31 |
|
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: 113.82 E-value: 3.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 14 LDVNGIEVIYNHVIlVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTkgyiqYRDERIERLSPAELVK 93
Cdd:cd03229 1 LELKNVSKRYGQKT-VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSIL-----IDGEDLTDLEDELPPL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 94 RGVVQVMEGRHC-FAHLTIEENlltgaytrelsrgdISIALervyqyfprlkqrrgsqagytSGGEQQMTAIGRALMASP 172
Cdd:cd03229 75 RRRIGMVFQDFAlFPHLTVLEN--------------IALGL---------------------SGGQQQRVALARALAMDP 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 695928685 173 NMILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILENGR 231
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
14-232 |
6.48e-31 |
|
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: 114.51 E-value: 6.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 14 LDVNGIEVIYNH---VILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKgergdVTKGYIQYRDERIERLSPAE 90
Cdd:cd03255 1 IELKNLSKTYGGggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDR-----PTSGEVRVDGTDISKLSEKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 91 LVK-R----GVVqvmegrhcF------AHLTIEENLLTGAY----TRELSRGDISIALERVyqyfpRLKQRRGSQAGYTS 155
Cdd:cd03255 76 LAAfRrrhiGFV--------FqsfnllPDLTALENVELPLLlagvPKKERRERAEELLERV-----GLGDRLNHYPSELS 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695928685 156 GGEQQMTAIGRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIAlRYADYGYILENGRV 232
Cdd:cd03255 143 GGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
11-232 |
2.59e-30 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 113.21 E-value: 2.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 11 KVLLDVNGIEVIY---NHVILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKgergdVTKGYIQYRDERIERLS 87
Cdd:COG1136 2 SPLLELRNLTKSYgtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDR-----PTSGEVLIDGQDISSLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 88 PAELVK-R----GVV-QvmeGRHCFAHLTIEEN-----LLTGAYTRElSRGDISIALERVyqyfpRLKQRRGSQAGYTSG 156
Cdd:COG1136 77 ERELARlRrrhiGFVfQ---FFNLLPELTALENvalplLLAGVSRKE-RRERARELLERV-----GLGDRLDHRPSQLSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695928685 157 GEQQMTAIGRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIAlRYADYGYILENGRV 232
Cdd:COG1136 148 GQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELA-ARADRVIRLRDGRI 222
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
29-250 |
2.95e-29 |
|
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: 110.84 E-value: 2.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKgergdVTKGYIQYRDERIERLSPAELV---KR-GVVqvmegrh 104
Cdd:COG1127 20 VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLR-----PDSGEILVDGQDITGLSEKELYelrRRiGML------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 105 cFAH------LTIEENLltgAYT-RELSRGDISIALERVyqyfpRLK-QRRG-SQAGYT-----SGGEQQMTAIGRALMA 170
Cdd:COG1127 88 -FQGgalfdsLTVFENV---AFPlREHTDLSEAEIRELV-----LEKlELVGlPGAADKmpselSGGMRKRVALARALAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 171 SPNMILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDLAQNED--VK 248
Cdd:COG1127 159 DPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASDDpwVR 238
|
..
gi 695928685 249 EF 250
Cdd:COG1127 239 QF 240
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
30-180 |
3.57e-29 |
|
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: 108.12 E-value: 3.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 30 LKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTkgyiqyRDERIERLSPAELVKRGVVQVMEGRHCFAHL 109
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTIL------LDGQDLTDDERKSLRKEIGYVFQDPQLFPRL 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695928685 110 TIEENLLTGAYTRELSRGDISialERVYQYFPRL------KQRRGSQAGYTSGGEQQMTAIGRALMASPNMILLDEP 180
Cdd:pfam00005 75 TVRENLRLGLLLKGLSKREKD---ARAEEALEKLglgdlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
14-232 |
1.70e-28 |
|
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: 106.74 E-value: 1.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 14 LDVNGIEVIYNHVIlVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKgergdVTKGYIQYRDERIERLSPAELVK 93
Cdd:cd03216 1 LELRGITKRFGGVK-ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYK-----PDSGEILVDGKEVSFASPRDARR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 94 RGVvqvmegrhcfahltieenlltgaytrelsrgdisialERVYQYfprlkqrrgsqagytSGGEQQMTAIGRALMASPN 173
Cdd:cd03216 75 AGI-------------------------------------AMVYQL---------------SVGERQMVEIARALARNAR 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 695928685 174 MILLDEPSMGLAPQIVEEIFEIVRDLnQREGVSFLLAEQNTNIALRYADYGYILENGRV 232
Cdd:cd03216 103 LLILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-244 |
1.81e-28 |
|
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: 113.46 E-value: 1.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 3 VASPTPPSKVLLDVNGIEVIYN----HVILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKgergdVTKGYIQY 78
Cdd:COG1123 250 AAPAAAAAEPLLEVRNLSKRYPvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLR-----PTSGSILF 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 79 RDERIERLSPAELVK-RGVVQVMegrhcF--------AHLTIEENL-----LTGAYTRELSRGDISIALERVyQYFPRLK 144
Cdd:COG1123 325 DGKDLTKLSRRSLRElRRRVQMV-----FqdpysslnPRMTVGDIIaeplrLHGLLSRAERRERVAELLERV-GLPPDLA 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 145 QRRGSQagyTSGGEQQMTAIGRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYG 224
Cdd:COG1123 399 DRYPHE---LSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRV 475
|
250 260
....*....|....*....|
gi 695928685 225 YILENGRVMMDGAASDLAQN 244
Cdd:COG1123 476 AVMYDGRIVEDGPTEEVFAN 495
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
29-231 |
1.82e-28 |
|
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: 106.56 E-value: 1.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKgergdVTKGYIQYRDERIERLSPAELVKRgvvqvmegrhcfah 108
Cdd:cd00267 14 ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLK-----PTSGEILIDGKDIAKLPLEELRRR-------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 109 ltieenlltgaytrelsrgdISialervyqYFPRLkqrrgsqagytSGGEQQMTAIGRALMASPNMILLDEPSMGLAPQI 188
Cdd:cd00267 75 --------------------IG--------YVPQL-----------SGGQRQRVALARALLLNPDLLLLDEPTSGLDPAS 115
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 695928685 189 VEEIFEIVRDLNQrEGVSFLLAEQNTNIALRYADYGYILENGR 231
Cdd:cd00267 116 RERLLELLRELAE-EGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
13-244 |
2.16e-28 |
|
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: 113.07 E-value: 2.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 13 LLDVNGIEVIYNH-VILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLkGERGDVTkGYIQYRDERIERLSPAEL 91
Cdd:COG1123 4 LLEVRDLSVRYPGgDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLL-PHGGRIS-GEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 92 VKRGVVQVMEGRHCFAHLTIEENLLTGAYTRELSRGDI----SIALERVyqyfpRLKQRRGSQAGYTSGGEQQMTAIGRA 167
Cdd:COG1123 82 GRRIGMVFQDPMTQLNPVTVGDQIAEALENLGLSRAEArarvLELLEAV-----GLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695928685 168 LMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDLAQN 244
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
16-236 |
2.68e-28 |
|
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: 107.62 E-value: 2.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 16 VNGIEVIYNHVIlVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTKGYIQYRDER-----------IE 84
Cdd:cd03235 2 VEDLTVSYGGHP-VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERkrigyvpqrrsID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 85 RLSPaelvkrgvvqvmegrhcfahLTIEENLLTGAYT-----RELSRGDISI---ALERVyqyfpRLKQRRGSQAGYTSG 156
Cdd:cd03235 81 RDFP--------------------ISVRDVVLMGLYGhkglfRRLSKADKAKvdeALERV-----GLSELADRQIGELSG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 157 GEQQMTAIGRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNqREGVSFLLAEQNTNIALRYADYgYILENGRVMMDG 236
Cdd:cd03235 136 GQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELR-REGMTILVVTHDLGLVLEYFDR-VLLLNRTVVASG 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
29-250 |
4.38e-28 |
|
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: 107.59 E-value: 4.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVtkgyiQYRDERIERLSPAEL--VKRGVVQVMEGRHCF 106
Cdd:cd03261 15 VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEV-----LIDGEDISGLSEAELyrLRRRMGMLFQSGALF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 107 AHLTIEENLL-----TGAYTRELSRGDISIALERVyqyfpRLKQRRGSQAGYTSGGEQQMTAIGRALMASPNMILLDEPS 181
Cdd:cd03261 90 DSLTVFENVAfplreHTRLSEEEIREIVLEKLEAV-----GLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPT 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695928685 182 MGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDL--AQNEDVKEF 250
Cdd:cd03261 165 AGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELraSDDPLVRQF 235
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
13-251 |
5.26e-28 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 107.48 E-value: 5.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 13 LLDVNGIEVIYNHViLVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKgergdVTKGYIQYRDERIERlspaelv 92
Cdd:COG1121 6 AIELENLTVSYGGR-PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLP-----PTSGTVRLFGKPPRR------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 93 KRGVV----QvmegRHCFAH---LTIEENLLTGAYTRE-----LSRGDISI---ALERVyqyfpRLKQRRGSQAGYTSGG 157
Cdd:COG1121 73 ARRRIgyvpQ----RAEVDWdfpITVRDVVLMGRYGRRglfrrPSRADREAvdeALERV-----GLEDLADRPIGELSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 158 EQQMTAIGRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNqREGVSFLLAEQNTNIALRYADYGYILeNGRVMMDGA 237
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELR-REGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGP 221
|
250
....*....|....
gi 695928685 238 ASDLAQNEDVKEFY 251
Cdd:COG1121 222 PEEVLTPENLSRAY 235
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
29-236 |
4.60e-27 |
|
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: 104.22 E-value: 4.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVT-KGyiQYRDERIERLSpaelvKRGVvqVMEGRHCFA 107
Cdd:cd03268 15 VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITfDG--KSYQKNIEALR-----RIGA--LIEAPGFYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 108 HLTIEENLLTGAYTRELSRGDISIALERVyqyfpRLKQRRGSQAGYTSGGEQQMTAIGRALMASPNMILLDEPSMGLAPQ 187
Cdd:cd03268 86 NLTARENLRLLARLLGIRKKRIDEVLDVV-----GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 695928685 188 IVEEIFEIVRDLNqREGVSFLLA----EQNTNIALRYAdygyILENGRVMMDG 236
Cdd:cd03268 161 GIKELRELILSLR-DQGITVLISshllSEIQKVADRIG----IINKGKLIEEG 208
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
10-241 |
5.18e-27 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 107.49 E-value: 5.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 10 SKVLLDVNGIEVIYNHVIlVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLkgergDVTKGYIQYRDERIERLSPA 89
Cdd:COG3842 2 AMPALELENVSKRYGDVT-ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFE-----TPDSGRILLDGRDVTGLPPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 90 elvKRGVVQVMEGrhcFA---HLTIEENLLTGAYTRELSRGDI----SIALERVyqyfpRLK---QRRGSQagyTSGGEQ 159
Cdd:COG3842 76 ---KRNVGMVFQD---YAlfpHLTVAENVAFGLRMRGVPKAEIrarvAELLELV-----GLEglaDRYPHQ---LSGGQQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 160 QMTAIGRALMASPNMILLDEPSMGLAPQIVEEI-FEIvRDLNQREGVSFLLA-----EqntniALRYADYGYILENGRVM 233
Cdd:COG3842 142 QRVALARALAPEPRVLLLDEPLSALDAKLREEMrEEL-RRLQRELGITFIYVthdqeE-----ALALADRIAVMNDGRIE 215
|
....*...
gi 695928685 234 MDGAASDL 241
Cdd:COG3842 216 QVGTPEEI 223
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
29-253 |
1.03e-26 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 104.21 E-value: 1.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTkgyiqYRDERIERLSPAELVKRGVVQVMEGRHCFAH 108
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNII-----IDDEDISLLPLHARARRGIGYLPQEASIFRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 109 LTIEENLLTGAYTRE-LSRGDISIALERVYQYFpRLKQRRGSQAGYTSGGEQQMTAIGRALMASPNMILLDEPSMGLAPQ 187
Cdd:PRK10895 93 LSVYDNLMAVLQIRDdLSAEQREDRANELMEEF-HIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPI 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695928685 188 IVEEIFEIVRDLNQReGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDLAQNEDVKEFYLG 253
Cdd:PRK10895 172 SVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYLG 236
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
30-241 |
1.75e-26 |
|
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: 103.22 E-value: 1.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 30 LKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVT-KGYIQYRDerierlsPAElVKRGVVQVMEGRHCFAH 108
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATvAGHDVVRE-------PRE-VRRRIGIVFQDLSVDDE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 109 LTIEENLLTGAYTRELSRGDISIALERVYQYFpRLKQRRGSQAGYTSGGEQQMTAIGRALMASPNMILLDEPSMGLAPQI 188
Cdd:cd03265 88 LTGWENLYIHARLYGVPGAERRERIDELLDFV-GLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 695928685 189 VEEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDL 241
Cdd:cd03265 167 RAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
13-243 |
3.29e-26 |
|
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: 102.96 E-value: 3.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 13 LLDVNGIEVIY---NHVILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTkgyiqYRDERIERLSPA 89
Cdd:COG1124 1 MLEVRNLSVSYgqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVT-----FDGRPVTRRRRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 90 ELvkRGVVQVM--------EGRHcfahlTIEENLLTGAytRELSRGDISIALERVYQYF---PRLKQRRGSQagyTSGGE 158
Cdd:COG1124 76 AF--RRRVQMVfqdpyaslHPRH-----TVDRILAEPL--RIHGLPDREERIAELLEQVglpPSFLDRYPHQ---LSGGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 159 QQMTAIGRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAA 238
Cdd:COG1124 144 RQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTV 223
|
....*
gi 695928685 239 SDLAQ 243
Cdd:COG1124 224 ADLLA 228
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
26-236 |
4.81e-26 |
|
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: 101.68 E-value: 4.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 26 VILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVT-KGYIQYRDerierlsPAElVKRGVVQVMEGRH 104
Cdd:cd03266 17 TVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATvDGFDVVKE-------PAE-ARRRLGFVSDSTG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 105 CFAHLTIEENLLTGAYTRELSRGDISIALERVYQYFpRLKQRRGSQAGYTSGGEQQMTAIGRALMASPNMILLDEPSMGL 184
Cdd:cd03266 89 LYDRLTARENLEYFAGLYGLKGDELTARLEELADRL-GMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 695928685 185 APQIVEEIFEIVRDLnQREGVSFLLAEQNTNIALRYADYGYILENGRVMMDG 236
Cdd:cd03266 168 DVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
30-261 |
5.67e-26 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 102.78 E-value: 5.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 30 LKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTK----GYIQYRDERIERLSPAELVKRGVVqvMEGRHC 105
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGSHiellGRTVQREGRLARDIRKSRANTGYI--FQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 106 FAHLTIEENLLTGAYTrelsrgdiSIALERV-YQYFPRLKQRRGSQA--------------GYTSGGEQQMTAIGRALMA 170
Cdd:PRK09984 98 VNRLSVLENVLIGALG--------STPFWRTcFSWFTREQKQRALQAltrvgmvhfahqrvSTLSGGQQQRVAIARALMQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 171 SPNMILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDLaQNEDVKEF 250
Cdd:PRK09984 170 QAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF-DNERFDHL 248
|
250
....*....|.
gi 695928685 251 YLGISSGERKS 261
Cdd:PRK09984 249 YRSINRVEENA 259
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
29-209 |
1.14e-25 |
|
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: 100.68 E-value: 1.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTKGYIQYRDERIErlspAELVKRGVVQVMEGRHCFAH 108
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKN----INELRQKVGMVFQQFNLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 109 LTIEENLLTG-AYTRELSRGDisiALERVYQYFPR--LKQRRGSQAGYTSGGEQQMTAIGRALMASPNMILLDEPSMGLA 185
Cdd:cd03262 91 LTVLENITLApIKVKGMSKAE---AEERALELLEKvgLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALD 167
|
170 180
....*....|....*....|....
gi 695928685 186 PQIVEEIFEIVRDLNQrEGVSFLL 209
Cdd:cd03262 168 PELVGEVLDVMKDLAE-EGMTMVV 190
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
28-236 |
1.21e-25 |
|
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: 100.66 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 28 LVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVT-KGYiqyrderiERLSPAELVKRGVVQVMEGRHCF 106
Cdd:cd03263 16 PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYiNGY--------SIRTDRKAARQSLGYCPQFDALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 107 AHLTIEENLLTGAYTRELSRGDISIALERVYQYFpRLKQRRGSQAGYTSGGEQQMTAIGRALMASPNMILLDEPSMGLAP 186
Cdd:cd03263 88 DELTVREHLRFYARLKGLPKSEIKEEVELLLRVL-GLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 695928685 187 QIVEEIFEIVRDLnqREGVSFLLAEQNTNIALRYADYGYILENGRVMMDG 236
Cdd:cd03263 167 ASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
14-232 |
2.02e-25 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 99.89 E-value: 2.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 14 LDVNGIEVIYNHVILvLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTkgyiqYRDERIERLSPAELVK 93
Cdd:COG4619 1 LELEGLSFRVGGKPI-LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIY-----LDGKPLSAMPPPEWRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 94 rgvvQVMegrHCFAHL-----TIEENLLTGAYTREL--SRGDISIALERVYqyFPR--LKQrrgsQAGYTSGGEQQMTAI 164
Cdd:COG4619 75 ----QVA---YVPQEPalwggTVRDNLPFPFQLRERkfDRERALELLERLG--LPPdiLDK----PVERLSGGERQRLAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695928685 165 GRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILENGRV 232
Cdd:COG4619 142 IRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
12-251 |
3.56e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 100.62 E-value: 3.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 12 VLLDVNGIEVIYNHViLVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTkgyIQYRDerIERLSPAEL 91
Cdd:PRK13548 1 AMLEARNLSVRLGGR-TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVR---LNGRP--LADWSPAEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 92 VK-RGVV-QVmegrhcfAHL----TIEENLLTGAYTRELSRGD----ISIALERV------YQYFPRLkqrrgsqagytS 155
Cdd:PRK13548 75 ARrRAVLpQH-------SSLsfpfTVEEVVAMGRAPHGLSRAEddalVAAALAQVdlahlaGRDYPQL-----------S 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 156 GGEQQMTAIGRALM------ASPNMILLDEP--SMGLAPQIveEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYIL 227
Cdd:PRK13548 137 GGEQQRVQLARVLAqlwepdGPPRWLLLDEPtsALDLAHQH--HVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLL 214
|
250 260
....*....|....*....|....
gi 695928685 228 ENGRVMMDGAASDLAQNEDVKEFY 251
Cdd:PRK13548 215 HQGRLVADGTPAEVLTPETLRRVY 238
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
14-243 |
4.05e-25 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 100.09 E-value: 4.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 14 LDVNGIEVIYnHVILVLKGVSLRVPEGKIVALLGANGAGKTTTLRaVSNLLKGERgdvtKGYIQYRDERI---ERLSPAE 90
Cdd:COG4161 3 IQLKNINCFY-GSHQALFDINLECPSGETLVLLGPSGAGKSSLLR-VLNLLETPD----SGQLNIAGHQFdfsQKPSEKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 91 --LVKRGVVQVMEGRHCFAHLTIEENLLTgAYTR--ELSRgdiSIALERVYQYFPRLK--QRRGSQAGYTSGGEQQMTAI 164
Cdd:COG4161 77 irLLRQKVGMVFQQYNLWPHLTVMENLIE-APCKvlGLSK---EQAREKAMKLLARLRltDKADRFPLHLSGGQQQRVAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695928685 165 GRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQrEGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDLAQ 243
Cdd:COG4161 153 ARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQ-TGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDASHFTQ 230
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
14-241 |
5.25e-25 |
|
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: 99.23 E-value: 5.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 14 LDVNGIEVIYNHVIlVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKgergdVTKGYIQYRDERIERLSPAelvK 93
Cdd:cd03300 1 IELENVSKFYGGFV-ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFET-----PTSGEILLDGKDITNLPPH---K 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 94 RGVVQVMEGRHCFAHLTIEENLLTGAYTRELSRGDISialERVYQY--FPRLK---QRRGSQagyTSGGEQQMTAIGRAL 168
Cdd:cd03300 72 RPVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIK---ERVAEAldLVQLEgyaNRKPSQ---LSGGQQQRVAIARAL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695928685 169 MASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDL 241
Cdd:cd03300 146 VNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
29-250 |
5.62e-25 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 99.40 E-value: 5.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTKGYIQYRDERI-ERLspaelVKRGVVQVMEGRHCFA 107
Cdd:PRK09493 16 VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVdERL-----IRQEAGMVFQQFYLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 108 HLTIEENLLTGA-YTRELSRGDI-SIALE---RVyqyfpRLKQRRGSQAGYTSGGEQQMTAIGRALMASPNMILLDEPSM 182
Cdd:PRK09493 91 HLTALENVMFGPlRVRGASKEEAeKQAREllaKV-----GLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTS 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695928685 183 GLAPQIVEEIFEIVRDLNQrEGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDLAQN---EDVKEF 250
Cdd:PRK09493 166 ALDPELRHEVLKVMQDLAE-EGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNppsQRLQEF 235
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
22-238 |
5.79e-25 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 98.97 E-value: 5.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 22 IYNHVILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAvsnLLKGERgdVTKGYIQYRDERIERLSPAEL--VKR--GVV 97
Cdd:COG2884 10 RYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKL---LYGEER--PTSGQVLVNGQDLSRLKRREIpyLRRriGVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 98 qvmegrhcF------AHLTIEENL-----LTGaYTRELSRGDISIALERVyqyfpRLKQRRGSQAGYTSGGEQQMTAIGR 166
Cdd:COG2884 85 --------FqdfrllPDRTVYENValplrVTG-KSRKEIRRRVREVLDLV-----GLSDKAKALPHELSGGEQQRVAIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695928685 167 ALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQReGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAA 238
Cdd:COG2884 151 ALVNRPELLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRLVRDEAR 221
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
14-254 |
8.18e-25 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 98.67 E-value: 8.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 14 LDVNGIEVIYNHVILVLkgvSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTkgyIQYRDerIERLSPAElvk 93
Cdd:COG3840 2 LRLDDLTYRYGDFPLRF---DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRIL---WNGQD--LTALPPAE--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 94 RGVVQVMEGRHCFAHLTIEENLLTG-----AYTRElSRGDISIALERVYQYfpRLKQRRGSQagyTSGGEQQMTAIGRAL 168
Cdd:COG3840 71 RPVSMLFQENNLFPHLTVAQNIGLGlrpglKLTAE-QRAQVEQALERVGLA--GLLDRLPGQ---LSGGQRQRVALARCL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 169 MASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDLAQNEDVK 248
Cdd:COG3840 145 VRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPP 224
|
....*...
gi 695928685 249 EF--YLGI 254
Cdd:COG3840 225 ALaaYLGI 232
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
29-232 |
8.24e-25 |
|
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: 98.79 E-value: 8.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTKGYIQYRDERI-ERLSPAELVKRGVVQVMEGRHCFa 107
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLLDGKDIyDLDVDVLELRRRVGMVFQKPNPF- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 108 HLTIEENL-----LTGAYTRELSRGDISIALERVYqYFPRLKQRrgSQAGYTSGGEQQMTAIGRALMASPNMILLDEPSM 182
Cdd:cd03260 94 PGSIYDNVayglrLHGIKLKEELDERVEEALRKAA-LWDEVKDR--LHALGLSGGQQQRLCLARALANEPEVLLLDEPTS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 695928685 183 GLAPQIVEEIFEIVRDLNQREGVsfLLAEQNTNIALRYADYGYILENGRV 232
Cdd:cd03260 171 ALDPISTAKIEELIAELKKEYTI--VIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
10-241 |
2.81e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 101.25 E-value: 2.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 10 SKVLLDVNGIEVIYNHViLVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDvtkgyIQYRDERIERLSPA 89
Cdd:COG1129 1 AEPLLEMRGISKSFGGV-KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGE-----ILLDGEPVRFRSPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 90 ELVKRGVVQVMEGRHCFAHLTIEENLLTGaytRELSRG---DISIALERVYQYFPRLKQRR--GSQAGYTSGGEQQMTAI 164
Cdd:COG1129 75 DAQAAGIAIIHQELNLVPNLSVAENIFLG---REPRRGgliDWRAMRRRARELLARLGLDIdpDTPVGDLSVAQQQLVEI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 165 GRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLnQREGVSFL-----LAEqntniALRYADYGYILENGRVMMDGAAS 239
Cdd:COG1129 152 ARALSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIyishrLDE-----VFEIADRVTVLRDGRLVGTGPVA 225
|
..
gi 695928685 240 DL 241
Cdd:COG1129 226 EL 227
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-253 |
2.93e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 97.88 E-value: 2.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 5 SPTPPSKVLLDVNGIEVIYNHVIlVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKgergdVTKGYIQYRDERIE 84
Cdd:COG4674 2 SLDTMHGPILYVEDLTVSFDGFK-ALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTR-----PDSGSVLFGGTDLT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 85 RLSPAELVKRGVvqvmeGRH-----CFAHLTIEENL---------LTGAYTRELSRGD---ISIALERVyqyfpRLKQRR 147
Cdd:COG4674 76 GLDEHEIARLGI-----GRKfqkptVFEELTVFENLelalkgdrgVFASLFARLTAEErdrIEEVLETI-----GLTDKA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 148 GSQAGYTSGGEQQMTAIGRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQREGV-------SFL--LAEQNTnial 218
Cdd:COG4674 146 DRLAGLLSHGQKQWLEIGMLLAQDPKLLLLDEPVAGMTDAETERTAELLKSLAGKHSVvvvehdmEFVrqIARKVT---- 221
|
250 260 270
....*....|....*....|....*....|....*
gi 695928685 219 ryadygyILENGRVMMDGAASDLAQNEDVKEFYLG 253
Cdd:COG4674 222 -------VLHQGSVLAEGSLDEVQADPRVIEVYLG 249
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
13-222 |
6.08e-24 |
|
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: 96.01 E-value: 6.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 13 LLDVNGIEVIYNHViLVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTkgyiqYRDERIERlsPAELV 92
Cdd:COG4133 2 MLEAENLSCRRGER-LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVL-----WNGEPIRD--AREDY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 93 KRGVVQVMEGRHCFAHLTIEENL--LTGAYTRELSRGDISIALERVyqyfpRLKQRRGSQAGYTSGGEQQMTAIGRALMA 170
Cdd:COG4133 74 RRRLAYLGHADGLKPELTVRENLrfWAALYGLRADREAIDEALEAV-----GLAGLADLPVRQLSAGQKRRVALARLLLS 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 695928685 171 SPNMILLDEPSMGLAPQIVEEIFEIVRDLNQReGVSFLLAeqnTNIALRYAD 222
Cdd:COG4133 149 PAPLWLLDEPFTALDAAGVALLAELIAAHLAR-GGAVLLT---THQPLELAA 196
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
23-250 |
9.05e-24 |
|
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: 96.22 E-value: 9.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 23 YNHVILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLkgergDVTKGYIQYRDERIERLSPAELvKRGVVQVMEG 102
Cdd:cd03295 10 YGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLI-----EPTSGEIFIDGEDIREQDPVEL-RRKIGYVIQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 103 RHCFAHLTIEENL-----LTGaYTRELSRGDISIALERVYQYFPRLKQRRGSQagyTSGGEQQMTAIGRALMASPNMILL 177
Cdd:cd03295 84 IGLFPHMTVEENIalvpkLLK-WPKEKIRERADELLALVGLDPAEFADRYPHE---LSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695928685 178 DEPSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDL---AQNEDVKEF 250
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEIlrsPANDFVAEF 235
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
29-250 |
1.19e-23 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 95.83 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAVsNLLkgERgdVTKGYIQYRDERIErLSPAEL--VKRGVVQVMEGRHCF 106
Cdd:COG1126 16 VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCI-NLL--EE--PDSGTITVDGEDLT-DSKKDInkLRRKVGMVFQQFNLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 107 AHLTIEENLLTG-AYTRELSRGD-ISIA---LERVyqyfpRLKQRRGSQAGYTSGGEQQMTAIGRALMASPNMILLDEPS 181
Cdd:COG1126 90 PHLTVLENVTLApIKVKKMSKAEaEERAmelLERV-----GLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPT 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695928685 182 MGLAPQIVEEIFEIVRDLnQREGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDL---AQNEDVKEF 250
Cdd:COG1126 165 SALDPELVGEVLDVMRDL-AKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFfenPQHERTRAF 235
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
16-243 |
2.90e-23 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 95.08 E-value: 2.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 16 VNGIEVIYNhVILVLKGVSLRVPEGKIVALLGANGAGKTTTLRaVSNLLKGER-GDVTKGYIQYRDERIERLSPAELVKR 94
Cdd:PRK11124 5 LNGINCFYG-AHQALFDITLDCPQGETLVLLGPSGAGKSSLLR-VLNLLEMPRsGTLNIAGNHFDFSKTPSDKAIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 95 GVVQVMEGRHCFAHLTIEENLLTgAYTR--ELSRgdiSIALERVYQYFPRLkqRRGSQAG----YTSGGEQQMTAIGRAL 168
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLIE-APCRvlGLSK---DQALARAEKLLERL--RLKPYADrfplHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695928685 169 MASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQrEGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDLAQ 243
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDPEITAQIVSIIRELAE-TGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASCFTQ 230
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
33-246 |
3.37e-23 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 97.10 E-value: 3.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 33 VSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTKGYIQYRDERIERLSPAElvKRGVVQVMEGRHCFAHLTIE 112
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPE--KRRIGYVFQEARLFPHLSVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 113 ENLLTGaYTRelSRG-DISIALERVYQYF---PRLKQRRGSqagyTSGGEQQMTAIGRALMASPNMILLDEPSMGLAPQI 188
Cdd:TIGR02142 94 GNLRYG-MKR--ARPsERRISFERVIELLgigHLLGRLPGR----LSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPR 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 695928685 189 VEEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDLAQNED 246
Cdd:TIGR02142 167 KYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPD 224
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
13-236 |
3.38e-23 |
|
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: 94.49 E-value: 3.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 13 LLDVNGIEVIY---NHVILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKgergdVTKGYIQYRDERIERLSPA 89
Cdd:cd03257 1 LLEVKNLSVSFptgGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLK-----PTSGSIIFDGKDLLKLSRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 90 ELVKRG-VVQVMegrhcFAH--------LTIEENLLTGAYTRELSRGDiSIALERVYQYF------PRLKQRRGSQagyT 154
Cdd:cd03257 76 LRKIRRkEIQMV-----FQDpmsslnprMTIGEQIAEPLRIHGKLSKK-EARKEAVLLLLvgvglpEEVLNRYPHE---L 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 155 SGGEQQMTAIGRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILENGRVMM 234
Cdd:cd03257 147 SGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVE 226
|
..
gi 695928685 235 DG 236
Cdd:cd03257 227 EG 228
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
10-241 |
3.99e-23 |
|
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: 94.57 E-value: 3.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 10 SKVLLDVNGIeviynhvILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVsNLLkgERGdvTKGYIQYRDERIERLSPA 89
Cdd:cd03258 8 SKVFGDTGGK-------VTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCI-NGL--ERP--TSGSVLVDGTDLTLLSGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 90 ELVK--RGVVQVMEGRHCFAHLTIEENLltgAYTRELSRGDISIALERVYQY--FPRLKQRRGSQAGYTSGGEQQMTAIG 165
Cdd:cd03258 76 ELRKarRRIGMIFQHFNLLSSRTVFENV---ALPLEIAGVPKAEIEERVLELleLVGLEDKADAYPAQLSGGQKQRVGIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695928685 166 RALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDL 241
Cdd:cd03258 153 RALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
8-251 |
4.27e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 96.03 E-value: 4.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 8 PPSKVLLDVNGIEVIYNHViLVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDvtkgyIQYRDERIERLS 87
Cdd:PRK13537 2 PMSVAPIDFRNVEKRYGDK-LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGS-----ISLCGEPVPSRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 88 PAELVKRGVVQVMEGRHcfAHLTIEENLLTGAYTRELSRGDISIALERVYQyFPRLKQRRGSQAGYTSGGEQQMTAIGRA 167
Cdd:PRK13537 76 RHARQRVGVVPQFDNLD--PDFTVRENLLVFGRYFGLSAAAARALVPPLLE-FAKLENKADAKVGELSGGMKRRLTLARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 168 LMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQReGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDLAQNE-- 245
Cdd:PRK13537 153 LVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEig 231
|
....*..
gi 695928685 246 -DVKEFY 251
Cdd:PRK13537 232 cDVIEIY 238
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
30-241 |
6.51e-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: 93.94 E-value: 6.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 30 LKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTKGyiqyrDERIERLSPAElvkRGVVQVMEGRHCFAHL 109
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFG-----GEDATDVPVQE---RNVGFVFQHYALFRHM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 110 TIEENLLTGAYTRELSRGDISIALERVYQYFPRLKQRRGSQAGYT---SGGEQQMTAIGRALMASPNMILLDEPSMGLAP 186
Cdd:cd03296 90 TVFDNVAFGLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPaqlSGGQRQRVALARALAVEPKVLLLDEPFGALDA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 695928685 187 QIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDL 241
Cdd:cd03296 170 KVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
15-232 |
9.62e-23 |
|
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: 92.71 E-value: 9.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 15 DVNGIEVIYNHVILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTKGyiqyrderIERLSPAELVKR 94
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLN--------GKPIKAKERRKS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 95 gVVQVME--GRHCFAHlTIEENLLTGAYTRELSRGDISIALERVYQYFPRLKQRRGsqagyTSGGEQQMTAIGRALMASP 172
Cdd:cd03226 73 -IGYVMQdvDYQLFTD-SVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLS-----LSGGQKQRLAIAAALLSGK 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 173 NMILLDEPSMGLAPQIVEEIFEIVRDLnQREGVSFLLAEQNTNIALRYADYGYILENGRV 232
Cdd:cd03226 146 DLLIFDEPTSGLDYKNMERVGELIREL-AAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
14-254 |
1.71e-22 |
|
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: 92.78 E-value: 1.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 14 LDVNGIEVIYNHviLVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDvtkgyIQYRDERIERLSPAelvK 93
Cdd:cd03299 1 LKVENLSKDWKE--FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGK-----ILLNGKDITNLPPE---K 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 94 RGVVQVMEGRHCFAHLTIEENLLTGAYTRELSRGDISialERVYQYFPRLKQRR--GSQAGYTSGGEQQMTAIGRALMAS 171
Cdd:cd03299 71 RDISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIE---RKVLEIAEMLGIDHllNRKPETLSGGEQQRVAIARALVVN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 172 PNMILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDL---AQNEDVK 248
Cdd:cd03299 148 PKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVfkkPKNEFVA 227
|
....*.
gi 695928685 249 EFyLGI 254
Cdd:cd03299 228 EF-LGF 232
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
13-251 |
2.75e-22 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 92.87 E-value: 2.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 13 LLDVNGIEVIYNHVILvLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTkgyiqYRDERIERLSPAELV 92
Cdd:COG4559 1 MLEAENLSVRLGGRTL-LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVR-----LNGRPLAAWSPWELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 93 K-RGVV-QvmegrHC---FAhLTIEENLLTGAYTRELSRGD----ISIALERV------YQYFPRLkqrrgsqagytSGG 157
Cdd:COG4559 75 RrRAVLpQ-----HSslaFP-FTVEEVVALGRAPHGSSAAQdrqiVREALALVglahlaGRSYQTL-----------SGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 158 EQQMTAIGRAL-------MASPNMILLDEP--SMGLAPQIveEIFEIVRDLNQReGVSFLLAEQNTNIALRYADYGYILE 228
Cdd:COG4559 138 EQQRVQLARVLaqlwepvDGGPRWLFLDEPtsALDLAHQH--AVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLH 214
|
250 260
....*....|....*....|...
gi 695928685 229 NGRVMMDGAASDLAQNEDVKEFY 251
Cdd:COG4559 215 QGRLVAQGTPEEVLTDELLERVY 237
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
8-180 |
3.22e-22 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 92.46 E-value: 3.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 8 PPSKVLLDVNGIEVIYNHV---ILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTkgyiqYRDERIE 84
Cdd:COG1116 2 SAAAPALELRGVSKRFPTGgggVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVL-----VDGKPVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 85 RLSPaelvKRGVV-QvmEGRhCFAHLTIEENLLTGAYTRELSRGDisiALERVYQYFPR--LKQRRGSqagYT---SGGE 158
Cdd:COG1116 77 GPGP----DRGVVfQ--EPA-LLPWLTVLDNVALGLELRGVPKAE---RRERARELLELvgLAGFEDA---YPhqlSGGM 143
|
170 180
....*....|....*....|..
gi 695928685 159 QQMTAIGRALMASPNMILLDEP 180
Cdd:COG1116 144 RQRVAIARALANDPEVLLMDEP 165
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-245 |
3.46e-22 |
|
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: 95.60 E-value: 3.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 4 ASPTPPSKVLLDVNGIEVIY-NHVILVLKGVSLRVPEGKIVALLGANGAGKTTTLravsNLLKGERgDVTKGYIQYRDER 82
Cdd:COG4987 324 EPAPAPGGPSLELEDVSFRYpGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLL----ALLLRFL-DPQSGSITLGGVD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 83 IERLSPAELvkRGVVQVMEGR-HCFAHlTIEENLLTGAytRELSRGDISIALERVY--QYFPRLKQ----RRGSQAGYTS 155
Cdd:COG4987 399 LRDLDEDDL--RRRIAVVPQRpHLFDT-TLRENLRLAR--PDATDEELWAALERVGlgDWLAALPDgldtWLGEGGRRLS 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 156 GGEQQMTAIGRALMASPNMILLDEPSMGL----APQIVEEIFEIVRDlnqRegvSFLLAEQNTnIALRYADYGYILENGR 231
Cdd:COG4987 474 GGERRRLALARALLRDAPILLLDEPTEGLdaatEQALLADLLEALAG---R---TVLLITHRL-AGLERMDRILVLEDGR 546
|
250
....*....|....
gi 695928685 232 VMMDGAASDLAQNE 245
Cdd:COG4987 547 IVEQGTHEELLAQN 560
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
29-233 |
6.30e-22 |
|
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: 90.78 E-value: 6.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKgergdVTKGYIQYRDERIERLSPAElvkRGVVQVMEGRHCFAH 108
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEE-----PTSGRIYIGGRDVTDLPPKD---RDIAMVFQNYALYPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 109 LTIEENLLTGAYTRELSRGDISialERVYQYFPRLK-----QRRGSQagyTSGGEQQMTAIGRALMASPNMILLDEPSMG 183
Cdd:cd03301 87 MTVYDNIAFGLKLRKVPKDEID---ERVREVAELLQiehllDRKPKQ---LSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 695928685 184 LAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILENGRVM 233
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
28-257 |
1.35e-21 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 90.98 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 28 LVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDvtkgyIQYRDERIERLSPAEL--VKRGVVQVMEGRHC 105
Cdd:PRK11831 21 CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGE-----ILFDGENIPAMSRSRLytVRKRMSMLFQSGAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 106 FAHLTIEENLltgAY-----TR---ELSRGDISIALERVyqyfpRLKQRRGSQAGYTSGGEQQMTAIGRALMASPNMILL 177
Cdd:PRK11831 96 FTDMNVFDNV---AYplrehTQlpaPLLHSTVMMKLEAV-----GLRGAAKLMPSELSGGMARRAALARAIALEPDLIMF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 178 DEPSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDLAQNED--VKEFYLGIS 255
Cdd:PRK11831 168 DEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDprVRQFLDGIA 247
|
..
gi 695928685 256 SG 257
Cdd:PRK11831 248 DG 249
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
11-209 |
1.41e-21 |
|
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: 89.03 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 11 KVLLDVNGIeviynHVILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTkgyiqYRDERIERLSPAE 90
Cdd:cd03215 2 EPVLEVRGL-----SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEIT-----LDGKPVTRRSPRD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 91 LVKRGVVQVMEGRH---CFAHLTIEENLLtgaytrelsrgdISIALervyqyfprlkqrrgsqagytSGGEQQMTAIGRA 167
Cdd:cd03215 72 AIRAGIAYVPEDRKregLVLDLSVAENIA------------LSSLL---------------------SGGNQQKVVLARW 118
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 695928685 168 LMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNqREGVSFLL 209
Cdd:cd03215 119 LARDPRVLILDEPTRGVDVGAKAEIYRLIRELA-DAGKAVLL 159
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
14-236 |
2.03e-21 |
|
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: 89.26 E-value: 2.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 14 LDVNGIEVIYNHVIlVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTKGYIQYRDERIERLS--PAEl 91
Cdd:cd03269 1 LEVENVTKRFGRVT-ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGylPEE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 92 vkRGVVQVMegrhcfahlTIEENLLTGAYTRELSRGDisiALERVYQYFPRLK--QRRGSQAGYTSGGEQQMTAIGRALM 169
Cdd:cd03269 79 --RGLYPKM---------KVIDQLVYLAQLKGLKKEE---ARRRIDEWLERLElsEYANKRVEELSKGNQQKVQFIAAVI 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695928685 170 ASPNMILLDEPSMGLAPQIVEEIFEIVRDLnQREGVSFLLAEQNTNIALRYADYGYILENGRVMMDG 236
Cdd:cd03269 145 HDPELLILDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
34-236 |
2.05e-21 |
|
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: 89.47 E-value: 2.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 34 SLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTKGYIQYrderierlSPAELVKRGVVQVMEGRHCFAHLTIEE 113
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV--------TAAPPADRPVSMLFQENNLFAHLTVEQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 114 N----LLTGAYTRELSRGDISIALERVYqyFPRLKQRRgsqAGYTSGGEQQMTAIGRALMASPNMILLDEPSMGLAPQIV 189
Cdd:cd03298 90 NvglgLSPGLKLTAEDRQAIEVALARVG--LAGLEKRL---PGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 695928685 190 EEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILENGRVMMDG 236
Cdd:cd03298 165 AEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
39-236 |
2.67e-21 |
|
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: 88.89 E-value: 2.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 39 EGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTKGYIQYRDERIERLSPAElvKRGVVQVMEGRHCFAHLTIEENLLTG 118
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQ--QRKIGLVFQQYALFPHLNVRENLAFG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 119 ayTRELSRGDISIALERVYQYF--PRLKQRRGSQagyTSGGEQQMTAIGRALMASPNMILLDEPSMGLAPQIVEEIFEIV 196
Cdd:cd03297 100 --LKRKRNREDRISVDELLDLLglDHLLNRYPAQ---LSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPEL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 695928685 197 RDLNQREGVSFLLAEQNTNIALRYADYGYILENGRVMMDG 236
Cdd:cd03297 175 KQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
29-250 |
2.75e-21 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 89.81 E-value: 2.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTKGYIQYRDERieRLSPAELVKRGVVQ----VMEGRH 104
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTAR--SLSQQKGLIRQLRQhvgfVFQNFN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 105 CFAHLTIEENLLTGAYTRELSRGDISIALERVYQYFPRLKQRRGSQAGYTSGGEQQMTAIGRALMASPNMILLDEPSMGL 184
Cdd:PRK11264 96 LFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSAL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695928685 185 APQIVEEIFEIVRDLNQrEGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDL---AQNEDVKEF 250
Cdd:PRK11264 176 DPELVGEVLNTIRQLAQ-EKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALfadPQQPRTRQF 243
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
13-251 |
3.53e-21 |
|
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: 89.37 E-value: 3.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 13 LLDVNGIEVIYNHVIlVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSnllkgerGDVTKGY---IQYRDERIERLSPA 89
Cdd:COG1119 3 LLELRNVTVRRGGKT-ILDDISWTVKPGEHWAILGPNGAGKSTLLSLIT-------GDLPPTYgndVRLFGERRGGEDVW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 90 ELVKR-GVVQVMEGRHCFAHLTIEENLLTGAY-----TRELSRGDISIA---LERVyqyfpRLKQRRGSQAGYTSGGEQQ 160
Cdd:COG1119 75 ELRKRiGLVSPALQLRFPRDETVLDVVLSGFFdsiglYREPTDEQRERArelLELL-----GLAHLADRPFGTLSQGEQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 161 MTAIGRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLL----AE---QNTNIALryadygyILENGRVM 233
Cdd:COG1119 150 RVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLvthhVEeipPGITHVL-------LLKDGRVV 222
|
250
....*....|....*...
gi 695928685 234 MDGAASDLAQNEDVKEFY 251
Cdd:COG1119 223 AAGPKEEVLTSENLSEAF 240
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
14-209 |
6.28e-21 |
|
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: 88.30 E-value: 6.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 14 LDVNGIEVIY---NHVILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKgergdVTKGYIQYRDERIERLSPAe 90
Cdd:cd03293 1 LEVRNVSKTYgggGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLER-----PTSGEVLVDGEPVTGPGPD- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 91 lvkRGVV-QvmegRHC-FAHLTIEENLLTGAYTRELSRGDisiALERVYQYFPR--LKQRRGSQAGYTSGGEQQMTAIGR 166
Cdd:cd03293 75 ---RGYVfQ----QDAlLPWLTVLDNVALGLELQGVPKAE---ARERAEELLELvgLSGFENAYPHQLSGGMRQRVALAR 144
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 695928685 167 ALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLL 209
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLL 187
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
29-241 |
1.04e-20 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 89.82 E-value: 1.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLlkgERGDvtKGYIQYRDERIE-RLSPAElvkrgvvqvmegRHC-- 105
Cdd:COG1118 17 LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGL---ETPD--SGRIVLNGRDLFtNLPPRE------------RRVgf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 106 -------FAHLTIEENLLTGAYTRELSRGDISialERVYQYF-----PRLKQRRGSQagyTSGGEQQMTAIGRALMASPN 173
Cdd:COG1118 80 vfqhyalFPHMTVAENIAFGLRVRPPSKAEIR---ARVEELLelvqlEGLADRYPSQ---LSGGQRQRVALARALAVEPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 174 MILLDEPsMG-----LAPQIVEEIFEIVRDL---------NQREgvsfllaeqntniALRYADYGYILENGRVMMDGAAS 239
Cdd:COG1118 154 VLLLDEP-FGaldakVRKELRRWLRRLHDELggttvfvthDQEE-------------ALELADRVVVMNQGRIEQVGTPD 219
|
..
gi 695928685 240 DL 241
Cdd:COG1118 220 EV 221
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
29-231 |
1.23e-20 |
|
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: 86.28 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLkgergDVTKGYIQYRDERIERLSPAELVKR-GVV----QVMEGr 103
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLY-----DPTSGEILIDGVDLRDLDLESLRKNiAYVpqdpFLFSG- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 104 hcfahlTIEENLLtgaytrelsrgdisialervyqyfprlkqrrgsqagytSGGEQQMTAIGRALMASPNMILLDEPSMG 183
Cdd:cd03228 91 ------TIRENIL--------------------------------------SGGQRQRIAIARALLRDPPILILDEATSA 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 695928685 184 LAPQIVEEIFEIVRDLnqREGVSFLLaeqntnIA-----LRYADYGYILENGR 231
Cdd:cd03228 127 LDPETEALILEALRAL--AKGKTVIV------IAhrlstIRDADRIIVLDDGR 171
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
29-249 |
1.73e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 87.76 E-value: 1.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTkgyiqYRDERIERLSPAELVKRGVV--QVmegrhcf 106
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVF-----LGDKPISMLSSRQLARRLALlpQH------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 107 aHLTIE----ENLLtgAYTR--------ELSRGD---ISIALERVyqYFPRLKQRRGSQagyTSGGEQQMTAIGRALMAS 171
Cdd:PRK11231 85 -HLTPEgitvRELV--AYGRspwlslwgRLSAEDnarVNQAMEQT--RINHLADRRLTD---LSGGQRQRAFLAMVLAQD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 172 PNMILLDEPS--MGLAPQIveEIFEIVRDLNQrEGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDLAQNEDVKE 249
Cdd:PRK11231 157 TPVVLLDEPTtyLDINHQV--ELMRLMRELNT-QGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRT 233
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-244 |
2.02e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 87.66 E-value: 2.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 14 LDVNGIEVIYNHViLVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTKGYIQYRDERIERLSPAELVK 93
Cdd:PRK14247 4 IEIRDLKVSFGQV-EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVYLDGQDIFKMDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 94 RgVVQVMEGRHCFAHLTIEENLLTGAYTRELSRGD------ISIALERVyQYFPRLKQRRGSQAGYTSGGEQQMTAIGRA 167
Cdd:PRK14247 83 R-VQMVFQIPNPIPNLSIFENVALGLKLNRLVKSKkelqerVRWALEKA-QLWDEVKDRLDAPAGKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695928685 168 LMASPNMILLDEPSMGLAPQIVEEIFEIVRDLnqREGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDLAQN 244
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLEL--KKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTN 235
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
29-241 |
2.88e-20 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 88.62 E-value: 2.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERG-------DVTKGYIQYRDerierlspaelvkrgVVQVME 101
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGqifidgeDVTHRSIQQRD---------------ICMVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 102 GRHCFAHLTIEENLLTGAYTRELSRGDISialERVYQYFpRLKQRRGSQAGYT---SGGEQQMTAIGRALMASPNMILLD 178
Cdd:PRK11432 86 SYALFPHMSLGENVGYGLKMLGVPKEERK---QRVKEAL-ELVDLAGFEDRYVdqiSGGQQQRVALARALILKPKVLLFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695928685 179 EPSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDL 241
Cdd:PRK11432 162 EPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
30-249 |
3.21e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 87.48 E-value: 3.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 30 LKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTKGYIQYRDERIERLSPaelvKRGVV------QVMEGr 103
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRS----KVGLVfqdpddQVFSS- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 104 hcfahlTIEENLLTGAYTRELSRGDIsiaLERVYQYFP--RLKQRRGSQAGYTSGGEQQMTAIGRALMASPNMILLDEPS 181
Cdd:PRK13647 96 ------TVWDDVAFGPVNMGLDKDEV---ERRVEEALKavRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPM 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695928685 182 MGLAPQIVEEIFEIVRDLNQrEGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDLAqNEDVKE 249
Cdd:PRK13647 167 AYLDPRGQETLMEILDRLHN-QGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLT-DEDIVE 232
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
33-246 |
3.81e-20 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 88.62 E-value: 3.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 33 VSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVT-KGYIQYRDERIERLsPAElvKR--GVV-QvmEGRhCFAH 108
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRlGGEVLQDSARGIFL-PPH--RRriGYVfQ--EAR-LFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 109 LTIEENLLTGAytRELSRGDISIALERVYQYF---PRLKQRrgsqAGYTSGGEQQMTAIGRALMASPNMILLDEPSMGLA 185
Cdd:COG4148 92 LSVRGNLLYGR--KRAPRAERRISFDEVVELLgigHLLDRR----PATLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695928685 186 PQIVEEIFEIVRDLNQREG-----VSFLLAEqntniALRYADYGYILENGRVMMDGAASDLAQNED 246
Cdd:COG4148 166 LARKAEILPYLERLRDELDipilyVSHSLDE-----VARLADHVVLLEQGRVVASGPLAEVLSRPD 226
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-245 |
5.42e-20 |
|
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: 89.05 E-value: 5.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 4 ASPTPPSKVLLDVNGIEVIYNHVILVLKGVSLRVPEGKIVALLGANGAGKTTTLravsNLLKGeRGDVTKGYIQYRDERI 83
Cdd:COG4988 327 APLPAAGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLL----NLLLG-FLPPYSGSILINGVDL 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 84 ERLSPAELvkRGVVQVMEGRHCFAHLTIEENLLTGAytRELSRGDISIALERVY--QYFPRLKQ----RRGSQAGYTSGG 157
Cdd:COG4988 402 SDLDPASW--RRQIAWVPQNPYLFAGTIRENLRLGR--PDASDEELEAALEAAGldEFVAALPDgldtPLGEGGRGLSGG 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 158 EQQMTAIGRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDlnqregvsflLAEQNTNI-------ALRYADYGYILENG 230
Cdd:COG4988 478 QAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRR----------LAKGRTVIlithrlaLLAQADRILVLDDG 547
|
250
....*....|....*
gi 695928685 231 RVMMDGAASDLAQNE 245
Cdd:COG4988 548 RIVEQGTHEELLAKN 562
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
14-241 |
5.47e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 88.75 E-value: 5.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 14 LDVNGIEVIYNHVIlVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTKGyiqyrDERIERLSPAELVK 93
Cdd:PRK09536 4 IDVSDLSVEFGDTT-VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVA-----GDDVEALSARAASR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 94 R--------------GVVQVME-GRHcfAHLTiEENLLTGAYTRELSRgdisiALER--VYQYFPRlkqrrgsQAGYTSG 156
Cdd:PRK09536 78 RvasvpqdtslsfefDVRQVVEmGRT--PHRS-RFDTWTETDRAAVER-----AMERtgVAQFADR-------PVTSLSG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 157 GEQQMTAIGRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQrEGVSFLLAEQNTNIALRYADYGYILENGRVMMDG 236
Cdd:PRK09536 143 GERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVD-DGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
....*
gi 695928685 237 AASDL 241
Cdd:PRK09536 222 PPADV 226
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
13-247 |
5.63e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 86.67 E-value: 5.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 13 LLDVNGIEVIYNHVILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDV-TKGY-IQYRDERIERLSPae 90
Cdd:PRK13639 1 ILETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVlIKGEpIKYDKKSLLEVRK-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 91 lvKRGVVQVMEGRHCFAHlTIEENLLTGAYTRELSRGDISialERVYQYFPRLkqrrgSQAGYT-------SGGEQQMTA 163
Cdd:PRK13639 79 --TVGIVFQNPDDQLFAP-TVEEDVAFGPLNLGLSKEEVE---KRVKEALKAV-----GMEGFEnkpphhlSGGQKKRVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 164 IGRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNqREGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDLAQ 243
Cdd:PRK13639 148 IAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLN-KEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFS 226
|
....
gi 695928685 244 NEDV 247
Cdd:PRK13639 227 DIET 230
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
14-180 |
6.97e-20 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 87.82 E-value: 6.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 14 LDVNGIEVIYNHVIlVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLkgergDVTKGYIQYRDERIERLSPAelvK 93
Cdd:COG3839 4 LELENVSKSYGGVE-ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLE-----DPTSGEILIGGRDVTDLPPK---D 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 94 RGVVQVMEGrhcFA---HLTIEENLLTGAYTRELSRGDISialERVyqyfpR----------LKQRRGSQAgytSGGEQQ 160
Cdd:COG3839 75 RNIAMVFQS---YAlypHMTVYENIAFPLKLRKVPKAEID---RRV-----ReaaellgledLLDRKPKQL---SGGQRQ 140
|
170 180
....*....|....*....|
gi 695928685 161 MTAIGRALMASPNMILLDEP 180
Cdd:COG3839 141 RVALGRALVREPKVFLLDEP 160
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
29-244 |
1.17e-19 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 85.79 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGD--VTKGYIQYRDERIERLSPAE-----LVKRGVVQVME 101
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSivVNGQTINLVRDKDGQLKVADknqlrLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 102 GRHCFAHLTIEENLLTG-AYTRELSRGDisiALERVYQYFPRLKQRRGSQAGYT---SGGEQQMTAIGRALMASPNMILL 177
Cdd:PRK10619 100 HFNLWSHMTVLENVMEApIQVLGLSKQE---ARERAVKYLAKVGIDERAQGKYPvhlSGGQQQRVSIARALAMEPEVLLF 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695928685 178 DEPSMGLAPQIVEEIFEIVRDLNQrEGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDLAQN 244
Cdd:PRK10619 177 DEPTSALDPELVGEVLRIMQQLAE-EGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGN 242
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
22-231 |
1.30e-19 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 84.61 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 22 IYNHVILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVtkgyiQYRDERIERLSPAEL--VKRGVVQV 99
Cdd:TIGR02673 10 AYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQV-----RIAGEDVNRLRGRQLplLRRRIGVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 100 MEGRHCFAHLTIEENLLTGAYTRELSRGDISIALERVYQYFPrLKQRRGSQAGYTSGGEQQMTAIGRALMASPNMILLDE 179
Cdd:TIGR02673 85 FQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVG-LEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 695928685 180 PSMGLAPQIVEEIFEIVRDLNQReGVSFLLAEQNTNIALRYADYGYILENGR 231
Cdd:TIGR02673 164 PTGNLDPDLSERILDLLKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-244 |
2.54e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 84.51 E-value: 2.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 24 NHVIlvlKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTKGYIQYRDERI--ERLSPAElVKRGVVQVME 101
Cdd:PRK14267 17 NHVI---KGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNIysPDVDPIE-VRREVGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 102 GRHCFAHLTIEENLLTGAYTRELSRGDISIAlERV------YQYFPRLKQRRGSQAGYTSGGEQQMTAIGRALMASPNMI 175
Cdd:PRK14267 93 YPNPFPHLTIYDNVAIGVKLNGLVKSKKELD-ERVewalkkAALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695928685 176 LLDEPSMGLAPQIVEEIFEIVRDLnqREGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDLAQN 244
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFEN 238
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
23-232 |
2.84e-19 |
|
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: 83.61 E-value: 2.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 23 YNHVILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAvsnLLKGERGdvTKGYIQYRDERIERL--SPAELVKRGVVQVM 100
Cdd:cd03292 10 YPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKL---IYKEELP--TSGTIRVNGQDVSDLrgRAIPYLRRKIGVVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 101 EGRHCFAHLTIEENL-----LTGAYTRELSRgDISIALERVyqyfpRLKQRRGSQAGYTSGGEQQMTAIGRALMASPNMI 175
Cdd:cd03292 85 QDFRLLPDRNVYENVafaleVTGVPPREIRK-RVPAALELV-----GLSHKHRALPAELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 695928685 176 LLDEPSMGLAPQIVEEIFEIVRDLNQReGVSFLLAEQNTNIALRYADYGYILENGRV 232
Cdd:cd03292 159 IADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-205 |
5.15e-19 |
|
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: 86.26 E-value: 5.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 4 ASPTPPSKVLLDVNGIEVIYNHVILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTKGyiqyrDERI 83
Cdd:TIGR02868 325 AGAVGLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLD-----GVPV 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 84 ERLSPAELVKRgVVQVMEGRHCFAhLTIEENLLTGAytRELSRGDISIALERV-----YQYFPR-LKQRRGSQAGYTSGG 157
Cdd:TIGR02868 400 SSLDQDEVRRR-VSVCAQDAHLFD-TTVRENLRLAR--PDATDEELWAALERVgladwLRALPDgLDTVLGEGGARLSGG 475
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 695928685 158 EQQMTAIGRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQREGV 205
Cdd:TIGR02868 476 ERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTV 523
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
13-247 |
7.64e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 83.70 E-value: 7.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 13 LLDVNGIEVIYNHVILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTkgyiqYRDERIERLSPAELV 92
Cdd:PRK13652 3 LIETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVL-----IRGEPITKENIREVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 93 KR-GVVQVMEGRHCFAHlTIEENLLTGAYTRELSRGDISIALERVYQYFPrLKQRRGSQAGYTSGGEQQMTAIGRALMAS 171
Cdd:PRK13652 78 KFvGLVFQNPDDQIFSP-TVEQDIAFGPINLGLDEETVAHRVSSALHMLG-LEELRDRVPHHLSGGEKKRVAIAGVIAME 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695928685 172 PNMILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDLAQNEDV 247
Cdd:PRK13652 156 PQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDL 231
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
28-245 |
1.07e-18 |
|
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: 85.66 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 28 LVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLkgergDVTKGYIQYRDERIERLSPAELVKR-GVV----QVMEG 102
Cdd:COG2274 489 PVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLY-----EPTSGRILIDGIDLRQIDPASLRRQiGVVlqdvFLFSG 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 103 rhcfahlTIEENLLTGAytRELSRGDISIALER--VYQYFPRLKQrrgsqaGY-T---------SGGEQQMTAIGRALMA 170
Cdd:COG2274 564 -------TIRENITLGD--PDATDEEIIEAARLagLHDFIEALPM------GYdTvvgeggsnlSGGQRQRLAIARALLR 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 171 SPNMILLDEPSMGLAPQIVEEIFEIVRDLNQreGVSFLLaeqntnIA-----LRYADYGYILENGRVMMDGAASDLAQNE 245
Cdd:COG2274 629 NPRILILDEATSALDAETEAIILENLRRLLK--GRTVII------IAhrlstIRLADRIIVLDKGRIVEDGTHEELLARK 700
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
5-223 |
1.97e-18 |
|
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: 84.65 E-value: 1.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 5 SPTPPSKVLlDVNGIEVIYNHVILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLkgergDVTKGYIQYRDERIE 84
Cdd:TIGR02857 314 VTAAPASSL-EFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFV-----DPTEGSIAVNGVPLA 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 85 RLSPAELVKRgVVQVMEGRHCFAHlTIEENLLTGayTRELSRGDISIALERVY-----QYFPRLKQRR-GSQAGYTSGGE 158
Cdd:TIGR02857 388 DADADSWRDQ-IAWVPQHPFLFAG-TIAENIRLA--RPDASDAEIREALERAGldefvAALPQGLDTPiGEGGAGLSGGQ 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695928685 159 QQMTAIGRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLnqREGVSFLLAEQNTNIALRyADY 223
Cdd:TIGR02857 464 AQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL--AQGRTVLLVTHRLALAAL-ADR 525
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
18-217 |
2.28e-18 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 81.12 E-value: 2.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 18 GIEVIYNHvILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVtkgYIQYRDERIERLSPAELVKRGVV 97
Cdd:TIGR03608 3 NISKKFGD-KVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQV---YLNGQETPPLNSKKASKFRREKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 98 Q-------VMEgrhcfaHLTIEENLLTGAYTRELSRGD----ISIALERV--YQYfprLKQRRgsqagYT-SGGEQQMTA 163
Cdd:TIGR03608 79 GylfqnfaLIE------NETVEENLDLGLKYKKLSKKEkrekKKEALEKVglNLK---LKQKI-----YElSGGEQQRVA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 695928685 164 IGRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNqREGVSFLLAEQNTNIA 217
Cdd:TIGR03608 145 LARAILKPPPLILADEPTGSLDPKNRDEVLDLLLELN-DEGKTIIIVTHDPEVA 197
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
29-241 |
4.16e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 82.08 E-value: 4.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGergdvTKGYIQYRDERIERLS-------PAElvkRGVVQVMe 101
Cdd:COG4152 16 AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAP-----DSGEVLWDGEPLDPEDrrrigylPEE---RGLYPKM- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 102 grhcfahlTIEENL-----LTGaytreLSRGDisiALERVYQYFPR--LKQRRGSQAGYTSGGEQQMTAIGRALMASPNM 174
Cdd:COG4152 87 --------KVGEQLvylarLKG-----LSKAE---AKRRADEWLERlgLGDRANKKVEELSKGNQQKVQLIAALLHDPEL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695928685 175 ILLDEPSMGLAPQIVEEIFEIVRDLNqREGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDL 241
Cdd:COG4152 151 LILDEPFSGLDPVNVELLKDVIRELA-AKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
14-235 |
5.91e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 80.90 E-value: 5.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 14 LDVNGIEVIYN----HVILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKgergdVTKGYIQYRDERIERLSP- 88
Cdd:COG1101 2 LELKNLSKTFNpgtvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLP-----PDSGSILIDGKDVTKLPEy 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 89 --AELVKRgVVQ-VMEGrhCFAHLTIEENLLTgAYTRELSRGdISIAL--ERVYQYFPRLKQ-------RRGSQAGYTSG 156
Cdd:COG1101 77 krAKYIGR-VFQdPMMG--TAPSMTIEENLAL-AYRRGKRRG-LRRGLtkKRRELFRELLATlglglenRLDTKVGLLSG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695928685 157 GEQQMTAIGRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILENGRVMMD 235
Cdd:COG1101 152 GQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIILD 230
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
14-201 |
6.30e-18 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 82.05 E-value: 6.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 14 LDVNGIEVIYNHViLVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGergdvTKGYIQYRDERIERLSPAElvk 93
Cdd:PRK10851 3 IEIANIKKSFGRT-QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQ-----TSGHIRFHGTDVSRLHARD--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 94 RGVVQVMEGRHCFAHLTIEENL---LTGAYTRElsRGDISIALERVYQY-----FPRLKQRRGSQagyTSGGEQQMTAIG 165
Cdd:PRK10851 74 RKVGFVFQHYALFRHMTVFDNIafgLTVLPRRE--RPNAAAIKAKVTQLlemvqLAHLADRYPAQ---LSGGQKQRVALA 148
|
170 180 190
....*....|....*....|....*....|....*.
gi 695928685 166 RALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQ 201
Cdd:PRK10851 149 RALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHE 184
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
29-251 |
6.37e-18 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 81.03 E-value: 6.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKG---ERGDVTKGYIQYRDERIERLSPAELVKRGVVQVMEGRHC 105
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGggaPRGARVTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 106 FAhLTIEENLLTGAYTR-----ELSRGD---ISIALERVyqyfpRLKQRRGSQAGYTSGGEQQMTAIGRAL--------- 168
Cdd:PRK13547 96 FA-FSAREIVLLGRYPHarragALTHRDgeiAWQALALA-----GATALVGRDVTTLSGGELARVQFARVLaqlwpphda 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 169 MASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDLAQNEDVK 248
Cdd:PRK13547 170 AQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLTPAHIA 249
|
...
gi 695928685 249 EFY 251
Cdd:PRK13547 250 RCY 252
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-209 |
1.04e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 82.37 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 4 ASPTPPSKVLLDVNGIEVIYnhvilVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTKGyiqyrDERI 83
Cdd:COG1129 247 KRAAAPGEVVLEVEGLSVGG-----VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLD-----GKPV 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 84 ERLSPAELVKRGVVQVMEGRH---CFAHLTIEENLLTGAYTRELSRGDISIALER--VYQYFPRLKQRRGS---QAGYTS 155
Cdd:COG1129 317 RIRSPRDAIRAGIAYVPEDRKgegLVLDLSIRENITLASLDRLSRGGLLDRRRERalAEEYIKRLRIKTPSpeqPVGNLS 396
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 695928685 156 GGEQQMTAIGRALMASPNMILLDEPSMGlapqiV-----EEIFEIVRDLNqREGVSFLL 209
Cdd:COG1129 397 GGNQQKVVLAKWLATDPKVLILDEPTRG-----IdvgakAEIYRLIRELA-AEGKAVIV 449
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
34-256 |
1.27e-17 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 79.63 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 34 SLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVtkgYIQYRDERieRLSPAelvKRGVVQVMEGRHCFAHLTIEE 113
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSL---TLNGQDHT--TTPPS---RRPVSMLFQENNLFSHLTVAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 114 NL---------LTGAYTRELSRGDISIALErvyQYFPRLkqrrgsqAGYTSGGEQQMTAIGRALMASPNMILLDEPSMGL 184
Cdd:PRK10771 91 NIglglnpglkLNAAQREKLHAIARQMGIE---DLLARL-------PGQLSGGQRQRVALARCLVREQPILLLDEPFSAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 695928685 185 APQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDLAQNEDVKEFYLGISS 256
Cdd:PRK10771 161 DPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKASASALLGIKS 232
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
10-253 |
1.40e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 81.03 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 10 SKVLLDVNGIEVIYNHVILVlKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTKGYIQYRDErierlspA 89
Cdd:PRK13536 38 STVAIDLAGVSKSYGDKAVV-NGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPAR-------A 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 90 ELVKRGVVQVMEGRHCFAHLTIEENLLT-GAYTRELSRgDISIALERVYQyFPRLKQRRGSQAGYTSGGEQQMTAIGRAL 168
Cdd:PRK13536 110 RLARARIGVVPQFDNLDLEFTVRENLLVfGRYFGMSTR-EIEAVIPSLLE-FARLESKADARVSDLSGGMKRRLTLARAL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 169 MASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQReGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDLAQNE--- 245
Cdd:PRK13536 188 INDPQLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHigc 266
|
....*...
gi 695928685 246 DVKEFYLG 253
Cdd:PRK13536 267 QVIEIYGG 274
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2-205 |
1.59e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 82.02 E-value: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 2 TVASPTPpskvLLDVNGIEVIYNHVIlVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTKGyiqyrDE 81
Cdd:PRK15439 4 SDTTAPP----LLCARSISKQYSGVE-VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIG-----GN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 82 RIERLSPAELVKRGVVQVMEGRHCFAHLTIEENLLTGAYTRELsrgdisiALERVYQyfprLKQRRGSQ------AGYTS 155
Cdd:PRK15439 74 PCARLTPAKAHQLGIYLVPQEPLLFPNLSVKENILFGLPKRQA-------SMQKMKQ----LLAALGCQldldssAGSLE 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 695928685 156 GGEQQMTAIGRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLnQREGV 205
Cdd:PRK15439 143 VADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIREL-LAQGV 191
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
24-236 |
1.92e-17 |
|
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: 78.79 E-value: 1.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 24 NHVILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTKGYIQYRderieRLSPAELvKRGVVQVMEGR 103
Cdd:cd03245 14 NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIR-----QLDPADL-RRNIGYVPQDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 104 HCFAHlTIEENLLTGAytRELSRGDISIALER--VYQYFPRLK---QRRGSQAGYT-SGGEQQMTAIGRALMASPNMILL 177
Cdd:cd03245 88 TLFYG-TLRDNITLGA--PLADDERILRAAELagVTDFVNKHPnglDLQIGERGRGlSGGQRQAVALARALLNDPPILLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 695928685 178 DEPSMGLAPQIVEEIFEIVRDLnqREGVSFLLAEQNTNIaLRYADYGYILENGRVMMDG 236
Cdd:cd03245 165 DEPTSAMDMNSEERLKERLRQL--LGDKTLIIITHRPSL-LDLVDRIIVMDSGRIVADG 220
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
7-239 |
2.00e-17 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 79.01 E-value: 2.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 7 TPPSKVLLDVNGIEVIYN---HVILVLKGVSLRVPEGKIVALLGANGAGKTTTLRavsnLLKG-ERgdVTKGYIQYRDER 82
Cdd:COG4181 2 SSSSAPIIELRGLTKTVGtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLG----LLAGlDR--PTSGTVRLAGQD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 83 IERLSP---AELVKRGVVQVMEGRHCFAHLTIEENLLTGAytrEL-----SRGDISIALERVyqyfpRLKQRRGSQAGYT 154
Cdd:COG4181 76 LFALDEdarARLRARHVGFVFQSFQLLPTLTALENVMLPL---ELagrrdARARARALLERV-----GLGHRLDHYPAQL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 155 SGGEQQMTAIGRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRyADYGYILENGRVMM 234
Cdd:COG4181 148 SGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVE 226
|
....*
gi 695928685 235 DGAAS 239
Cdd:COG4181 227 DTAAT 231
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
29-219 |
2.27e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 78.70 E-value: 2.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTkgyiqYRDERIERLSP---AELVKRGVVQVMEGRHC 105
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVI-----FNGQPMSKLSSaakAELRNQKLGFIYQFHHL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 106 FAHLTIEEN----LLTGAYTRELSRGDISIALERVyqyfpRLKQRRGSQAGYTSGGEQQMTAIGRALMASPNMILLDEPS 181
Cdd:PRK11629 99 LPDFTALENvampLLIGKKKPAEINSRALEMLAAV-----GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPT 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 695928685 182 MGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALR 219
Cdd:PRK11629 174 GNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKR 211
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
30-241 |
2.49e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 79.51 E-value: 2.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 30 LKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTKGYiqyrderierlSPAELVKRGVVQVMEGRHcFAHL 109
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDG-----------KPIDYSRKGLMKLRESVG-MVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 110 TIEENLLTGAYTRELSRGDISIAL------ERVYQYFPR--LKQRRGSQAGYTSGGEQQMTAIGRALMASPNMILLDEPS 181
Cdd:PRK13636 90 DPDNQLFSASVYQDVSFGAVNLKLpedevrKRVDNALKRtgIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 182 MGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDL 241
Cdd:PRK13636 170 AGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
28-202 |
4.18e-17 |
|
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: 78.08 E-value: 4.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 28 LVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLkgERGDVTKGYIQYRDERIERlspaELVKRGVVQVMEGRHCFA 107
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRV--EGGGTTSGQILFNGQPRKP----DQFQKCVAYVRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 108 HLTIEENLLTGAYTRELSRGDISIALERVYQYFPR---LKQRRGSQAGYTSGGEQQMTAIGRALMASPNMILLDEPSMGL 184
Cdd:cd03234 95 GLTVRETLTYTAILRLPRKSSDAIRKKRVEDVLLRdlaLTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170
....*....|....*...
gi 695928685 185 APQIVEEIFEIVRDLNQR 202
Cdd:cd03234 175 DSFTALNLVSTLSQLARR 192
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
29-239 |
4.26e-17 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 78.46 E-value: 4.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTtlraVSNLLKG-ERGDVTKGYIQYRDERIERLSPAELVKRGVVQVMEGRHCFA 107
Cdd:TIGR01978 15 ILKGVNLTVKKGEIHAIMGPNGSGKST----LSKTIAGhPSYEVTSGTILFKGQDLLELEPDERARAGLFLAFQYPEEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 108 HLTIEENLLTGAYTRELSRGDISIALervYQYFPRLKQ------------RRGSQAGYtSGGEQQMTAIGRALMASPNMI 175
Cdd:TIGR01978 91 GVSNLEFLRSALNARRSARGEEPLDL---LDFEKLLKEklalldmdeeflNRSVNEGF-SGGEKKRNEILQMALLEPKLA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695928685 176 LLDEPSMGLAPQIVEEIFEIVRDLNQrEGVSFLLAEQNTNIaLRY--ADYGYILENGRVMMDGAAS 239
Cdd:TIGR01978 167 ILDEIDSGLDIDALKIVAEGINRLRE-PDRSFLIITHYQRL-LNYikPDYVHVLLDGRIVKSGDVE 230
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
26-236 |
4.75e-17 |
|
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: 78.14 E-value: 4.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 26 VILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVT-KGYIQYRDERierlspaELVKR-GVV------ 97
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRvAGLVPWKRRK-------KFLRRiGVVfgqktq 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 98 -----QVMEGRHCFAHLTieeNLLTGAYTRELSRGDISIALERVyqyfprLKQrrgsQAGYTSGGEQQMTAIGRALMASP 172
Cdd:cd03267 106 lwwdlPVIDSFYLLAAIY---DLPPARFKKRLDELSELLDLEEL------LDT----PVRQLSLGQRMRAEIAAALLHEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695928685 173 NMILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILENGRVMMDG 236
Cdd:cd03267 173 EILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
13-233 |
1.21e-16 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 77.54 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 13 LLDVNGIEVIYNHVIL--------VLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGergdvTKGYIQYRDERIE 84
Cdd:TIGR02769 2 LLEVRDVTHTYRTGGLfgakqrapVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKP-----AQGTVSFRGQDLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 85 RLSPAEL--VKRGVVQVMEgrHCF----AHLTIEENLltGAYTRELSRGDISIALERVYQYF------PRLKQRRGSQag 152
Cdd:TIGR02769 77 QLDRKQRraFRRDVQLVFQ--DSPsavnPRMTVRQII--GEPLRHLTSLDESEQKARIAELLdmvglrSEDADKLPRQ-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 153 yTSGGEQQMTAIGRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILENGRV 232
Cdd:TIGR02769 151 -LSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
.
gi 695928685 233 M 233
Cdd:TIGR02769 230 V 230
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
29-241 |
1.38e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 77.44 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNL---LKGER--GDVTKG---YIQYRDerierlspAELVKRGVVQVM 100
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMndkVSGYRysGDVLLGgrsIFNYRD--------VLEFRRRVGMLF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 101 EGRHCFAhLTIEENLLTGAYTRELS-----RGDISIALERVyQYFPRLKQRRGSQAGYTSGGEQQMTAIGRALMASPNMI 175
Cdd:PRK14271 108 QRPNPFP-MSIMDNVLAGVRAHKLVprkefRGVAQARLTEV-GLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVL 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695928685 176 LLDEPSMGLAPQIVEEIFEIVRDLNQRegVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDL 241
Cdd:PRK14271 186 LLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
29-236 |
1.54e-16 |
|
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: 76.03 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAvsnLLKGERGDVTKGYIQYRDERIERLSPAELVKRGVVQVMEGRHCFAH 108
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKT---IMGHPKYEVTEGEILFKGEDITDLPPEERARLGIFLAFQYPPEIPG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 109 LTIEEnlltgaYTRELSRGdisialervyqyFprlkqrrgsqagytSGGEQQMTAIGRALMASPNMILLDEPSMGLAPQI 188
Cdd:cd03217 92 VKNAD------FLRYVNEG------------F--------------SGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 695928685 189 VEEIFEIVRDLNqREGVSFLLAEQNTNIA-LRYADYGYILENGRVMMDG 236
Cdd:cd03217 140 LRLVAEVINKLR-EEGKSVLIITHYQRLLdYIKPDRVHVLYDGRIVKSG 187
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
13-209 |
1.78e-16 |
|
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: 77.79 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 13 LLDVNGIEVIY---NHVILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLkgERGDVTKGYIQYRDERIERLSPA 89
Cdd:COG0444 1 LLEVRNLKVYFptrRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLL--PPPGITSGEILFDGEDLLKLSEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 90 ELVK-RG----VV----------------QVMEG--RHcfahltieeNLLTGAYTRE-----LSRGDISIALERVYQY-- 139
Cdd:COG0444 79 ELRKiRGreiqMIfqdpmtslnpvmtvgdQIAEPlrIH---------GGLSKAEAREraielLERVGLPDPERRLDRYph 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695928685 140 -FprlkqrrgsqagytSGGEQQMTAIGRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLL 209
Cdd:COG0444 150 eL--------------SGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILF 206
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
29-223 |
2.00e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 77.00 E-value: 2.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTKGYIQYRDERI-ERLSPAELVKRGVVQVMEGRHCFA 107
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFFNQNIyERRVNLNRLRRQVSMVHPKPNLFP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 108 hLTIEENLLTG----AYTRELSRGDISIALERVYQYFPRLKQRRGSQAGYTSGGEQQMTAIGRALMASPNMILLDEPSMG 183
Cdd:PRK14258 102 -MSVYDNVAYGvkivGWRPKLEIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 695928685 184 LAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRYADY 223
Cdd:PRK14258 181 LDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDF 220
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-254 |
3.85e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 76.21 E-value: 3.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 13 LLDVNGIEVIY-NHVILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTKGYIQYRDERIERlspael 91
Cdd:PRK13635 5 IIRVEHISFRYpDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWD------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 92 VKRGVVQVMEG-RHCFAHLTIEENLLTGAYTRELSRGD----ISIALERVyqyfpRLKQRRGSQAGYTSGGEQQMTAIGR 166
Cdd:PRK13635 79 VRRQVGMVFQNpDNQFVGATVQDDVAFGLENIGVPREEmverVDQALRQV-----GMEDFLNREPHRLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 167 ALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRyADYGYILENGRVMMDGAASDL-AQNE 245
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIfKSGH 232
|
....*....
gi 695928685 246 DVKEFYLGI 254
Cdd:PRK13635 233 MLQEIGLDV 241
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
29-253 |
6.45e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 75.47 E-value: 6.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDV-TKGYIQYRDERIERLSPAELvKRGVVQVMEGRHCFA 107
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIkVDGKVLYFGKDIFQIDAIKL-RKEVGMVFQQPNPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 108 HLTIEENLLTGAYTRELS-RGDISIALE---RVYQYFPRLKQRRGSQAGYTSGGEQQMTAIGRALMASPNMILLDEPSMG 183
Cdd:PRK14246 104 HLSIYDNIAYPLKSHGIKeKREIKKIVEeclRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695928685 184 LAPQIVEEIFEIVRDLNQRegVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDL---AQNEDVKEFYLG 253
Cdd:PRK14246 184 IDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIftsPKNELTEKYVIG 254
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
4-223 |
1.17e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 74.82 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 4 ASPTPPSKVLLDVNGIEVIY-NHviLVLKGVSLRVPEGKIVALLGANGAGKTTTLRA---VSNLLKGERGDvtkGYIQYR 79
Cdd:PRK14243 1 TSTLNGTETVLRTENLNVYYgSF--LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGFRVE---GKVTFH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 80 DERI--ERLSPAElVKRGVVQVMEGRHCFAHlTIEENLLTGAYTRELsRGDISIALERVYQ---YFPRLKQRRGSQAGYT 154
Cdd:PRK14243 76 GKNLyaPDVDPVE-VRRRIGMVFQKPNPFPK-SIYDNIAYGARINGY-KGDMDELVERSLRqaaLWDEVKDKLKQSGLSL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695928685 155 SGGEQQMTAIGRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQRegVSFLLAEQNTNIALRYADY 223
Cdd:PRK14243 153 SGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSDM 219
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
33-265 |
1.18e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 75.16 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 33 VSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTKGYIQYRDERIERLSPAELVKRGVVQVMEGRHCFAHlTIE 112
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQFPESQLFEE-TVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 113 ENLLTGAYTRELSRGDIS-IALERVyQYFPRLKQRRGSQAGYTSGGEQQMTAIGRALMASPNMILLDEPSMGLAPQIVEE 191
Cdd:PRK13643 104 KDVAFGPQNFGIPKEKAEkIAAEKL-EMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIE 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695928685 192 IFEIVRDLNQrEGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDLAQNED-VKEFYLGISSGERksFRDQ 265
Cdd:PRK13643 183 MMQLFESIHQ-SGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDfLKAHELGVPKATH--FADQ 254
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
14-200 |
1.35e-15 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 73.67 E-value: 1.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 14 LDVNGIEVIYNHVILVlKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLkgERGDVTKGYIQYRDERIERLsPAElvK 93
Cdd:COG4136 2 LSLENLTITLGGRPLL-APLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTL--SPAFSASGEVLLNGRRLTAL-PAE--Q 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 94 RGVVQVMEGRHCFAHLTIEENL---LTGAYTRELSRGDISIALERVyqyfprlkqrrgSQAGYT-------SGGEQQMTA 163
Cdd:COG4136 76 RRIGILFQDDLLFPHLSVGENLafaLPPTIGRAQRRARVEQALEEA------------GLAGFAdrdpatlSGGQRARVA 143
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 695928685 164 IGRALMASPNMILLDEP----SMGLAPQIVEEIFEIVRDLN 200
Cdd:COG4136 144 LLRALLAEPRALLLDEPfsklDAALRAQFREFVFEQIRQRG 184
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-244 |
2.04e-15 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 75.26 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 1 MTVASPTPPSKV------LLDVNGIEVIYNHvILVLKGVSLRVPEGKIVALLGANGAGKTTTLRavsnLLKGERGDvTKG 74
Cdd:PRK11607 1 MNDAIPRPQAKTrkaltpLLEIRNLTKSFDG-QHAVDDVSLTIYKGEIFALLGASGCGKSTLLR----MLAGFEQP-TAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 75 YIQYRDERIERLSPaelVKRGVVQVMEGRHCFAHLTIEENLLTGAYTRELSRGDISIALERVYQ--YFPRLKQRRGSQag 152
Cdd:PRK11607 75 QIMLDGVDLSHVPP---YQRPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGlvHMQEFAKRKPHQ-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 153 yTSGGEQQMTAIGRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILENGRV 232
Cdd:PRK11607 150 -LSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKF 228
|
250
....*....|..
gi 695928685 233 MMDGAASDLAQN 244
Cdd:PRK11607 229 VQIGEPEEIYEH 240
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-184 |
2.27e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 75.45 E-value: 2.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 6 PTPPSKVLLDVNGIEVIYNHVILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKgergdVTKGYIQYRDERIER 85
Cdd:COG3845 250 PAEPGEVVLEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRP-----PASGSIRLDGEDITG 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 86 LSPAELVKRGVVQVMEGRH---CFAHLTIEENLLTGAYTRE-LSRGDIsIALERVYQYFPRLKQR-------RGSQAGYT 154
Cdd:COG3845 325 LSPRERRRLGVAYIPEDRLgrgLVPDMSVAENLILGRYRRPpFSRGGF-LDRKAIRAFAEELIEEfdvrtpgPDTPARSL 403
|
170 180 190
....*....|....*....|....*....|
gi 695928685 155 SGGEQQMTAIGRALMASPNMILLDEPSMGL 184
Cdd:COG3845 404 SGGNQQKVILARELSRDPKLLIAAQPTRGL 433
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
29-210 |
3.41e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 71.88 E-value: 3.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTkgyiqyrdeRIERLSPAELVKRG---------VVQV 99
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR---------RAGGARVAYVPQRSevpdslpltVRDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 100 ME-GRhcFAHLTieenlLTGAYTRElSRGDISIALERVyqyfpRLKQRRGSQAGYTSGGEQQMTAIGRALMASPNMILLD 178
Cdd:NF040873 78 VAmGR--WARRG-----LWRRLTRD-DRAAVDDALERV-----GLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLD 144
|
170 180 190
....*....|....*....|....*....|..
gi 695928685 179 EPSMGLAPQIVEEIFEIVRDLnQREGVSFLLA 210
Cdd:NF040873 145 EPTTGLDAESRERIIALLAEE-HARGATVVVV 175
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
28-236 |
3.68e-15 |
|
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: 71.58 E-value: 3.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 28 LVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTkgyiqyrderierLSPAELvkrgvvqvmegrhcfa 107
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEIT-------------LDGVPV---------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 108 hLTIEENLltgaytrelsRGDISIALERVYQYFPRLKQRRGSQagyTSGGEQQMTAIGRALMASPNMILLDEPSMGLAP- 186
Cdd:cd03247 67 -SDLEKAL----------SSLISVLNQRPYLFDTTLRNNLGRR---FSGGERQRLALARILLQDAPIVLLDEPTVGLDPi 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 695928685 187 ---QIVEEIFEIVRDlnqregvSFLLAEQNTNIALRYADYGYILENGRVMMDG 236
Cdd:cd03247 133 terQLLSLIFEVLKD-------KTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
29-251 |
4.36e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 73.10 E-value: 4.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVtkgyiqYRD-ERIERLSPAELVKRgVVQVMEGRHCFA 107
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHV------WLDgEHIQHYASKEVARR-IGLLAQNATTPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 108 HLTIEENLLTGAYTRE----LSRGDISIALERVYQYfPRLKQRRGSQAGYTSGGEQQMTAIGRALMASPNMILLDEPS-- 181
Cdd:PRK10253 95 DITVQELVARGRYPHQplftRWRKEDEEAVTKAMQA-TGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTtw 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 182 MGLAPQIveEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDLAQNEDVKEFY 251
Cdd:PRK10253 174 LDISHQI--DLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIY 241
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
27-232 |
9.32e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 73.14 E-value: 9.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 27 ILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLlkgerGDVTKGYIQYRDERIERLSPAelvKRGVVQVMEGRHCF 106
Cdd:PRK11000 16 VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGL-----EDITSGDLFIGEKRMNDVPPA---ERGVGMVFQSYALY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 107 AHLTIEENLltgAYTRELSRGDISIALERVYQ-----YFPRLKQRRGSQagyTSGGEQQMTAIGRALMASPNMILLDEPS 181
Cdd:PRK11000 88 PHLSVAENM---SFGLKLAGAKKEEINQRVNQvaevlQLAHLLDRKPKA---LSGGQRQRVAIGRTLVAEPSVFLLDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 695928685 182 MGL-APQIVEEIFEIVRdLNQREGVSFLLAEQNTNIALRYADYGYILENGRV 232
Cdd:PRK11000 162 SNLdAALRVQMRIEISR-LHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
16-246 |
1.03e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 72.43 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 16 VNGIEVIYNH----VILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTKGY----IQYRDERIERLS 87
Cdd:PRK13651 5 VKNIVKIFNKklptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFkdekNKKKTKEKEKVL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 88 PAELVKR----------------GVV------QVMEGrhcfahlTIEENLLTGAYTRELSRGDisiALERVYQYFPRLkq 145
Cdd:PRK13651 85 EKLVIQKtrfkkikkikeirrrvGVVfqfaeyQLFEQ-------TIEKDIIFGPVSMGVSKEE---AKKRAAKYIELV-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 146 rrGSQAGYT-------SGGEQQMTAIGRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQrEGVSFLLAEQNTNIAL 218
Cdd:PRK13651 153 --GLDESYLqrspfelSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNK-QGKTIILVTHDLDNVL 229
|
250 260
....*....|....*....|....*...
gi 695928685 219 RYADYGYILENGRVMMDGAASDLAQNED 246
Cdd:PRK13651 230 EWTKRTIFFKDGKIIKDGDTYDILSDNK 257
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
29-236 |
1.10e-14 |
|
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: 70.66 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERgdvTKGYIQYRDERIERLSPaelvKRGVVQVMEGRHCFAH 108
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLG---VSGEVLINGRPLDKRSF----RKIIGYVPQDDILHPT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 109 LTIEENLLTGAYTRELsrgdisialervyqyfprlkqrrgsqagytSGGEQQMTAIGRALMASPNMILLDEPSMGLAPQI 188
Cdd:cd03213 97 LTVRETLMFAAKLRGL------------------------------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSS 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 695928685 189 VEEIFEIVRDlnqregvsflLAEQNTNI-----ALRYADYG-----YILENGRVMMDG 236
Cdd:cd03213 147 ALQVMSLLRR----------LADTGRTIicsihQPSSEIFElfdklLLLSQGRVIYFG 194
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
14-215 |
1.21e-14 |
|
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: 71.07 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 14 LDVNGIEVIYNHVIlVLKGVSLRVPEGkIVALLGANGAGKTTTLRAVSNLLKGERGDVTkgyiqyRDERIERLSPAELvk 93
Cdd:cd03264 1 LQLENLTKRYGKKR-ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIR------IDGQDVLKQPQKL-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 94 RGVVQVMEGR-HCFAHLTIEENLLTGAYTRELSRGD----ISIALERVyqyfpRLKQRRGSQAGYTSGGEQQMTAIGRAL 168
Cdd:cd03264 71 RRRIGYLPQEfGVYPNFTVREFLDYIAWLKGIPSKEvkarVDEVLELV-----NLGDRAKKKIGSLSGGMRRRVGIAQAL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 695928685 169 MASPNMILLDEPSMGLAPQiveeifeivrdlnQREGVSFLLAEQNTN 215
Cdd:cd03264 146 VGDPSILIVDEPTAGLDPE-------------ERIRFRNLLSELGED 179
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
30-249 |
1.22e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 72.00 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 30 LKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTKGYIQYRDERIerlSPAELVKR-GVV-QVMEgrHCFA 107
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKV---KLSDIRKKvGLVfQYPE--YQLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 108 HLTIEENLLTGAYTRELSRGDISI----ALERVYQYFPRLKQRRGSQagyTSGGEQQMTAIGRALMASPNMILLDEPSMG 183
Cdd:PRK13637 98 EETIEKDIAFGPINLGLSEEEIENrvkrAMNIVGLDYEDYKDKSPFE---LSGGQKRRVAIAGVVAMEPKILILDEPTAG 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695928685 184 LAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDLAQNEDVKE 249
Cdd:PRK13637 175 LDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVETLE 240
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
16-244 |
1.69e-14 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 72.42 E-value: 1.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 16 VNGIEVIYNH---VILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVsNLLkgERgdVTKGYIQYRDERIERLSPAELV 92
Cdd:COG1135 4 LENLSKTFPTkggPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCI-NLL--ER--PTSGSVLVDGVDLTALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 93 KR----GVVqvmegrhcFAHLtieeNLLTgaytrelSR---GDISIALE-----------RVYQYFPR--LKQRRGSqag 152
Cdd:COG1135 79 AArrkiGMI--------FQHF----NLLS-------SRtvaENVALPLEiagvpkaeirkRVAELLELvgLSDKADA--- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 153 YT---SGGEQQMTAIGRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILEN 229
Cdd:COG1135 137 YPsqlSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLEN 216
|
250
....*....|....*
gi 695928685 230 GRVMMDGAASDLAQN 244
Cdd:COG1135 217 GRIVEQGPVLDVFAN 231
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
13-202 |
2.23e-14 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 72.83 E-value: 2.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 13 LLDVNGIEVIY---NHVILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVtkgYIQYRD-ERIERLSP 88
Cdd:PRK10535 4 LLELKDIRRSYpsgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTY---RVAGQDvATLDADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 89 AELVKRGVVQVMEGRHCFAHLTIEENLLTGAYTRELSRGDisiALERVYQYFPRL--KQRRGSQAGYTSGGEQQMTAIGR 166
Cdd:PRK10535 81 AQLRREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQ---RLLRAQELLQRLglEDRVEYQPSQLSGGQQQRVSIAR 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 695928685 167 ALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQR 202
Cdd:PRK10535 158 ALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDR 193
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
13-241 |
3.13e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 72.05 E-value: 3.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 13 LLDVNGIEVIYNH---VILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTKGYIQYRDERIERLSPA 89
Cdd:PRK15134 5 LLAIENLSVAFRQqqtVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVYPSGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 90 ELVK-RGVVQVMEGRHCFAHL----TIEENL-----LTGAYTRELSRGDISIALERVyqyfpRLKQRRGSQAGYT---SG 156
Cdd:PRK15134 85 TLRGvRGNKIAMIFQEPMVSLnplhTLEKQLyevlsLHRGMRREAARGEILNCLDRV-----GIRQAAKRLTDYPhqlSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 157 GEQQMTAIGRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILENGRVMMDG 236
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQN 239
|
....*
gi 695928685 237 AASDL 241
Cdd:PRK15134 240 RAATL 244
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
29-180 |
3.33e-14 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 71.52 E-value: 3.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLlkgerGDVTKGYIQYRDERIERLsPAElvKRGVVQVMEGRHCFAH 108
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGF-----ETPDSGRIMLDGQDITHV-PAE--NRHVNTVFQSYALFPH 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695928685 109 LTIEENLLTGAYTRELSRGDISialERVYQ-----YFPRLKQRRGSQagyTSGGEQQMTAIGRALMASPNMILLDEP 180
Cdd:PRK09452 101 MTVFENVAFGLRMQKTPAAEIT---PRVMEalrmvQLEEFAQRKPHQ---LSGGQQQRVAIARAVVNKPKVLLLDES 171
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
23-236 |
4.52e-14 |
|
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: 69.56 E-value: 4.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 23 YNHVILVLKGVSLRVPEGKIVALLGANGAGKTTtlraVSNLLKGERgDVTKGYIQYRDERIERLSPAELVKR-GVVQvmE 101
Cdd:cd03254 12 YDEKKPVLKDINFSIKPGETVAIVGPTGAGKTT----LINLLMRFY-DPQKGQILIDGIDIRDISRKSLRSMiGVVL--Q 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 102 GRHCFAHlTIEENLLTGayTRELSRGDISIALERV-YQYFPR-----LKQRRGSQAGYTSGGEQQMTAIGRALMASPNMI 175
Cdd:cd03254 85 DTFLFSG-TIMENIRLG--RPNATDEEVIEAAKEAgAHDFIMklpngYDTVLGENGGNLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695928685 176 LLDEPSMGLAPQIVEEIFEIVRDLNQREgVSFLLAEQNTNIalRYADYGYILENGRVMMDG 236
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKLMKGR-TSIIIAHRLSTI--KNADKILVLDDGKIIEEG 219
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-246 |
5.48e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 71.39 E-value: 5.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 5 SPTPPSKVLLDVNGIEVIYNHVIL-VLKGVSLRVPEGKIVALLGANGAGKTTTLravsNLLKGERgDVTKGYIQYRDERI 83
Cdd:PRK11160 330 STAAADQVSLTLNNVSFTYPDQPQpVLKGLSLQIKAGEKVALLGRTGCGKSTLL----QLLTRAW-DPQQGEILLNGQPI 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 84 ERLSPAELvkRGVVQVMEGR-HCFAHlTIEENLLTGAYTreLSRGDISIALERV-----YQYFPRLKQRRGSQAGYTSGG 157
Cdd:PRK11160 405 ADYSEAAL--RQAISVVSQRvHLFSA-TLRDNLLLAAPN--ASDEALIEVLQQVgleklLEDDKGLNAWLGEGGRQLSGG 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 158 EQQMTAIGRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLlaeqnTN--IALRYADYGYILENGRVMMD 235
Cdd:PRK11160 480 EQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMI-----THrlTGLEQFDRICVMDNGQIIEQ 554
|
250
....*....|.
gi 695928685 236 GAASDLAQNED 246
Cdd:PRK11160 555 GTHQELLAQQG 565
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
30-247 |
6.31e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 70.04 E-value: 6.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 30 LKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTKGyiqyrDERIerlsPAELVKRGVVQVMEGRHCFAHL 109
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVG-----DYAI----PANLKKIKEVKRLRKEIGLVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 110 TIEENLLTGAYTRELSRGDISIAL--ERVYQYFPRLKQRRGSQAGYT-------SGGEQQMTAIGRALMASPNMILLDEP 180
Cdd:PRK13645 98 FPEYQLFQETIEKDIAFGPVNLGEnkQEAYKKVPELLKLVQLPEDYVkrspfelSGGQKRRVALAGIIAMDGNTLVLDEP 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695928685 181 SMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDLAQNEDV 247
Cdd:PRK13645 178 TGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQEL 244
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
39-236 |
7.02e-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: 71.58 E-value: 7.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 39 EGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTKGyiqyrDERIErlSPAELVKRGVVQVMEGRHCFAHLTIEENLLTG 118
Cdd:TIGR01257 955 ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVG-----GKDIE--TNLDAVRQSLGMCPQHNILFHHLTVAEHILFY 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 119 AYTRELSRGDISIALERVYQYfPRLKQRRGSQAGYTSGGEQQMTAIGRALMASPNMILLDEPSMGLAPQIVEEIFEIVrd 198
Cdd:TIGR01257 1028 AQLKGRSWEEAQLEMEAMLED-TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL-- 1104
|
170 180 190
....*....|....*....|....*....|....*...
gi 695928685 199 LNQREGVSFLLAEQNTNIALRYADYGYILENGRVMMDG 236
Cdd:TIGR01257 1105 LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
30-248 |
7.78e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 70.97 E-value: 7.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 30 LKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGergdvTKGYIQYRDERIERLSPAELVKRGVVQVMEGRHCFAHL 109
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEP-----TKGTITINNINYNKLDHKLAAQLGIGIIYQELSVIDEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 110 TIEENLLTGAY-TREL----------SRGDISIALERVyqyfpRLKQRRGSQAGYTSGGEQQMTAIGRALMASPNMILLD 178
Cdd:PRK09700 96 TVLENLYIGRHlTKKVcgvniidwreMRVRAAMMLLRV-----GLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMD 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 179 EPSMGLAPQIVEEIFEIVRDLnQREGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDLAQNEDVK 248
Cdd:PRK09700 171 EPTSSLTNKEVDYLFLIMNQL-RKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVR 239
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
10-232 |
8.19e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 70.83 E-value: 8.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 10 SKVLLDVNGIEVIYNHVIlVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDvtkgyIQYRDERIERLSPA 89
Cdd:COG3845 2 MPPALELRGITKRFGGVV-ANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGE-----ILIDGKPVRIRSPR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 90 ELVKRGVVQVmegrhcFAH------LTIEENLLTGAYTRELSRGDISIALERVyqyfprlkQRRGSQAGYT--------- 154
Cdd:COG3845 76 DAIALGIGMV------HQHfmlvpnLTVAENIVLGLEPTKGGRLDRKAARARI--------RELSERYGLDvdpdakved 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 155 -SGGEQQMTAIGRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLnQREGVSFL-----LAEqntniALRYADYGYILE 228
Cdd:COG3845 142 lSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRL-AAEGKSIIfithkLRE-----VMAIADRVTVLR 215
|
....
gi 695928685 229 NGRV 232
Cdd:COG3845 216 RGKV 219
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
28-264 |
1.12e-13 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 70.45 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 28 LVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTKGYIQyrderIERLSPAELV---KRGVVQVMEGRH 104
Cdd:PRK10070 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVD-----IAKISDAELRevrRKKIAMVFQSFA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 105 CFAHLTIEENLltgAYTRELSRgdiSIALERVYQYFPRLKQ--RRGSQAGYT---SGGEQQMTAIGRALMASPNMILLDE 179
Cdd:PRK10070 117 LMPHMTVLDNT---AFGMELAG---INAEERREKALDALRQvgLENYAHSYPdelSGGMRQRVGLARALAINPDILLMDE 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 180 PSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDLAQ---NEDVKEFYLGISS 256
Cdd:PRK10070 191 AFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNnpaNDYVRTFFRGVDI 270
|
....*...
gi 695928685 257 GERKSFRD 264
Cdd:PRK10070 271 SQVFSAKD 278
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
11-199 |
1.35e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 70.42 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 11 KVLLDVNGIEVIYNHViLVLKGVSLRVPEGKIVALLGANGAGKTTtlravsnLLKGERGDVTK--GYIQYRDERIERLSP 88
Cdd:PRK10762 2 QALLQLKGIDKAFPGV-KALSGAALNVYPGRVMALVGENGAGKST-------MMKVLTGIYTRdaGSILYLGKEVTFNGP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 89 AELVKRGVVQVMEGRHCFAHLTIEENLLTGaytRELSRGDISIALERVYQ----YFPRLKQRRGSQ--AGYTSGGEQQMT 162
Cdd:PRK10762 74 KSSQEAGIGIIHQELNLIPQLTIAENIFLG---REFVNRFGRIDWKKMYAeadkLLARLNLRFSSDklVGELSIGEQQMV 150
|
170 180 190
....*....|....*....|....*....|....*..
gi 695928685 163 AIGRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDL 199
Cdd:PRK10762 151 EIAKVLSFESKVIIMDEPTDALTDTETESLFRVIREL 187
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
13-241 |
1.36e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 68.95 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 13 LLDVNGIEVIYNHVIL--------VLKGVSLRVPEGKIVALLGANGAGKTTTLRavsnLLKG-ERGdvTKGYIQYRDERI 83
Cdd:PRK10419 3 LLNVSGLSHHYAHGGLsgkhqhqtVLNNVSLSLKSGETVALLGRSGCGKSTLAR----LLVGlESP--SQGNVSWRGEPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 84 ERLSPAELVK-RGVVQVM--------EGRHCFAHLTIE--ENLLTGAYTRELSRGDisiALERVYQYFPRLKQRRGSQag 152
Cdd:PRK10419 77 AKLNRAQRKAfRRDIQMVfqdsisavNPRKTVREIIREplRHLLSLDKAERLARAS---EMLRAVDLDDSVLDKRPPQ-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 153 yTSGGEQQMTAIGRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILENGRV 232
Cdd:PRK10419 152 -LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
....*....
gi 695928685 233 MMDGAASDL 241
Cdd:PRK10419 231 VETQPVGDK 239
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
30-232 |
1.63e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 67.98 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 30 LKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLlkgERGdvTKGYIQYRDERIERLSPAEL--VKRGVVQVMEGRHCFA 107
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGI---ERP--SAGKIWFSGHDITRLKNREVpfLRRQIGMIFQDHHLLM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 108 HLTIEEN-----LLTGAYTRELSRgDISIALERVyqyfpRLKQRRGSQAGYTSGGEQQMTAIGRALMASPNMILLDEPSM 182
Cdd:PRK10908 93 DRTVYDNvaiplIIAGASGDDIRR-RVSAALDKV-----GLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 695928685 183 GLAPQIVEEIFEIVRDLNqREGVSFLLAEQNTNIALRYADYGYILENGRV 232
Cdd:PRK10908 167 NLDDALSEGILRLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
13-223 |
3.14e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 66.90 E-value: 3.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 13 LLDVNGIEVIYnHVILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDvtkgyIQYRDERIERlspaelv 92
Cdd:PRK13540 1 MLDVIELDFDY-HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGE-----ILFERQSIKK------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 93 KRGVVQvmeGRHCFA--------HLTIEENLLtgaYTRELSRGDISIA-LERVYqyfpRLKQRRGSQAGYTSGGEQQMTA 163
Cdd:PRK13540 68 DLCTYQ---KQLCFVghrsginpYLTLRENCL---YDIHFSPGAVGITeLCRLF----SLEHLIDYPCGLLSSGQKRQVA 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 164 IGRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQntNIALRYADY 223
Cdd:PRK13540 138 LLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ--DLPLNKADY 195
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
28-197 |
3.19e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 66.82 E-value: 3.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 28 LVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTkgyiqYRDERIERLSPAELVkrgvvqvmegrHCFA 107
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIK-----LDGGDIDDPDVAEAC-----------HYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 108 H-------LTIEENLLTGAYTRELSRGDISIALERVyqYFPRLKQRRgsqAGYTSGGEQQMTAIGRALMASPNMILLDEP 180
Cdd:PRK13539 80 HrnamkpaLTVAENLEFWAAFLGGEELDIAAALEAV--GLAPLAHLP---FGYLSAGQKRRVALARLLVSNRPIWILDEP 154
|
170
....*....|....*..
gi 695928685 181 SMGLAPQIVEEIFEIVR 197
Cdd:PRK13539 155 TAALDAAAVALFAELIR 171
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
6-209 |
3.40e-13 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 68.94 E-value: 3.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 6 PTPPSKVLLDVNGIEVIY-----------NHVILVlKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKgergdvTKG 74
Cdd:COG4172 268 VPPDAPPLLEARDLKVWFpikrglfrrtvGHVKAV-DGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP------SEG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 75 YIQYRDERIERLSPAELVK-RGVVQV--------MEGRHCFAHLtIEENLLtgAYTRELSRGD----ISIALERVyQYFP 141
Cdd:COG4172 341 EIRFDGQDLDGLSRRALRPlRRRMQVvfqdpfgsLSPRMTVGQI-IAEGLR--VHGPGLSAAErrarVAEALEEV-GLDP 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695928685 142 RLKQRrgsqagYT---SGGEQQMTAIGRALMASPNMILLDEPS----MGLAPQIVeeifEIVRDLNQREGVSFLL 209
Cdd:COG4172 417 AARHR------YPhefSGGQRQRIAIARALILEPKLLVLDEPTsaldVSVQAQIL----DLLRDLQREHGLAYLF 481
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
27-240 |
3.78e-13 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 68.29 E-value: 3.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 27 ILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVsNLLkgERGdvTKGYIQYRDERIERLSPAELVKR----GVVqvmeg 102
Cdd:PRK11153 18 IHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCI-NLL--ERP--TSGRVLVDGQDLTALSEKELRKArrqiGMI----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 103 rhcFAHLtieeNLLTgaytrelSR---GDISIALE-----------RVYQYFPR--LKQRRGSQAGYTSGGEQQMTAIGR 166
Cdd:PRK11153 88 ---FQHF----NLLS-------SRtvfDNVALPLElagtpkaeikaRVTELLELvgLSDKADRYPAQLSGGQKQRVAIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695928685 167 ALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASD 240
Cdd:PRK11153 154 ALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSE 227
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
27-179 |
4.24e-13 |
|
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: 67.18 E-value: 4.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 27 ILVLKGVSLRVPEGKIVALLGANGAGKTTTLravsNLLkgER-GDVTKGYIQYRDERIERLSPAELVKR-GVV----QVM 100
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVV----SLL--ERfYDPTSGEILLDGVDIRDLNLRWLRSQiGLVsqepVLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 101 EGrhcfahlTIEENLLTGAYTRELSRGDISIALERVYQYFPRLKQR-------RGSQagyTSGGEQQMTAIGRALMASPN 173
Cdd:cd03249 90 DG-------TIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGydtlvgeRGSQ---LSGGQKQRIAIARALLRNPK 159
|
....*.
gi 695928685 174 MILLDE 179
Cdd:cd03249 160 ILLLDE 165
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
16-236 |
4.55e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.60 E-value: 4.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 16 VNGIEVIYNHVILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKgergdVTKGYIQYRDERIERLSPAELVKRg 95
Cdd:PRK15056 9 VNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVR-----LASGKISILGQPTRQALQKNLVAY- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 96 VVQVMEGRHCFAHLtIEENLLTGAY--------TRELSRGDISIALERVyqyfpRLKQRRGSQAGYTSGGEQQMTAIGRA 167
Cdd:PRK15056 83 VPQSEEVDWSFPVL-VEDVVMMGRYghmgwlrrAKKRDRQIVTAALARV-----DMVEFRHRQIGELSGGQKKRVFLARA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695928685 168 LMASPNMILLDEPSMGLAPQIVEEIFEIVRDLnQREGVSFLLAEQNTNIALRYADYGYILEnGRVMMDG 236
Cdd:PRK15056 157 IAQQGQVILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDYTVMVK-GTVLASG 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
16-180 |
7.48e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 68.17 E-value: 7.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 16 VNGIEVIYNHVILvLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTKGyiqyRDERIERLS--PAELVK 93
Cdd:COG0488 1 LENLSKSFGGRPL-LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP----KGLRIGYLPqePPLDDD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 94 RGVVQ-VMEGrhcFAHLTIEENLLTGAYTRELSRGDISIALERVYQYFPRLKqrrgsqaGYT------------------ 154
Cdd:COG0488 76 LTVLDtVLDG---DAELRALEAELEELEAKLAEPDEDLERLAELQEEFEALG-------GWEaearaeeilsglgfpeed 145
|
170 180 190
....*....|....*....|....*....|....
gi 695928685 155 --------SGGEQQMTAIGRALMASPNMILLDEP 180
Cdd:COG0488 146 ldrpvselSGGWRRRVALARALLSEPDLLLLDEP 179
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
9-241 |
8.85e-13 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 67.79 E-value: 8.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 9 PSKVLLDVNGIEVIY---NHVILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLkGERGDVTKGYIQYRDERIER 85
Cdd:COG4172 2 MSMPLLSVEDLSVAFgqgGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLL-PDPAAHPSGSILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 86 LSPAELVK-RG-----VVQ--------VMegrhcfahlTIEENL-----LTGAYTRELSRGDISIALERVyqYFPRLKQR 146
Cdd:COG4172 81 LSERELRRiRGnriamIFQepmtslnpLH---------TIGKQIaevlrLHRGLSGAAARARALELLERV--GIPDPERR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 147 RGSqagYT---SGGEQQ--MTAIgrALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRYA 221
Cdd:COG4172 150 LDA---YPhqlSGGQRQrvMIAM--ALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFA 224
|
250 260
....*....|....*....|
gi 695928685 222 DYGYILENGRVMMDGAASDL 241
Cdd:COG4172 225 DRVAVMRQGEIVEQGPTAEL 244
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
28-254 |
9.95e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 66.58 E-value: 9.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 28 LVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGergdvTKGYIQYRDERIE------RLSPaeLVKR-GVV-QV 99
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQP-----TSGTVTIGERVITagkknkKLKP--LRKKvGIVfQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 100 MEgrHCFAHLTIEENLLTGAYTRELSRGDisiALERVYQYF------PRLKQRRGSQagyTSGGEQQMTAIGRALMASPN 173
Cdd:PRK13634 94 PE--HQLFEETVEKDICFGPMNFGVSEED---AKQKAREMIelvglpEELLARSPFE---LSGGQMRRVAIAGVLAMEPE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 174 MILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDLAQN-EDVKEFYL 252
Cdd:PRK13634 166 VLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADpDELEAIGL 245
|
..
gi 695928685 253 GI 254
Cdd:PRK13634 246 DL 247
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
25-219 |
1.22e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 65.57 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 25 HVILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTK-GYIQYRDERIERlspAELVKRGVVQVMEGR 103
Cdd:PRK10584 21 HELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLvGQPLHQMDEEAR---AKLRAKHVGFVFQSF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 104 HCFAHLTIEEN-----LLTGAYTRElSRGDISIALERVyqyfpRLKQRRGSQAGYTSGGEQQMTAIGRALMASPNMILLD 178
Cdd:PRK10584 98 MLIPTLNALENvelpaLLRGESSRQ-SRNGAKALLEQL-----GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFAD 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 695928685 179 EPSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALR 219
Cdd:PRK10584 172 EPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAAR 212
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
14-199 |
1.51e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 67.24 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 14 LDVNGIEVIYNHViLVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSnllkgerGDV--TKGYIQYRDERIERLSPAEL 91
Cdd:PRK11288 5 LSFDGIGKTFPGV-KALDDISFDCRAGQVHALMGENGAGKSTLLKILS-------GNYqpDAGSILIDGQEMRFASTTAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 92 VKRGVVQVMEGRHCFAHLTIEENLLTGAYTRELSRGDISIALERVYQYFPRLKQRRGSQA--GYTSGGEQQMTAIGRALM 169
Cdd:PRK11288 77 LAAGVAIIYQELHLVPEMTVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTplKYLSIGQRQMVEIAKALA 156
|
170 180 190
....*....|....*....|....*....|
gi 695928685 170 ASPNMILLDEPSMGLAPQIVEEIFEIVRDL 199
Cdd:PRK11288 157 RNARVIAFDEPTSSLSAREIEQLFRVIREL 186
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-191 |
1.56e-12 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 65.83 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 1 MTVASPTPPSKvlLDVNGIEVIYNHViLVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTKGYIQYRD 80
Cdd:COG1117 1 MTAPASTLEPK--IEVRNLNVYYGDK-QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGARVEGEILLDG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 81 ERI--ERLSPAELVKR-GVVqvmegrhcFAH-----LTIEENLLTGA-YTRELSRGDISialERVYQYfprLKQ------ 145
Cdd:COG1117 78 EDIydPDVDVVELRRRvGMV--------FQKpnpfpKSIYDNVAYGLrLHGIKSKSELD---EIVEES---LRKaalwde 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 695928685 146 ---RRGSQAGYTSGGEQQMTAIGRALMASPNMILLDEPSMGLAP---QIVEE 191
Cdd:COG1117 144 vkdRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPistAKIEE 195
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
14-235 |
2.04e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 65.47 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 14 LDVNGIEVIYNHVIlVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTKGYI---QYRDERIERLSPAE 90
Cdd:PRK11247 13 LLLNAVSKRYGERT-VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAplaEAREDTRLMFQDAR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 91 LV--KRGVVQVMEGrhcfahltieenlLTGAYtrelsRGDISIALERVyqyfpRLKQRRGSQAGYTSGGEQQMTAIGRAL 168
Cdd:PRK11247 92 LLpwKKVIDNVGLG-------------LKGQW-----RDAALQALAAV-----GLADRANEWPAALSGGQKQRVALARAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695928685 169 MASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILENGRVMMD 235
Cdd:PRK11247 149 IHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLD 215
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
10-267 |
2.21e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 65.18 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 10 SKVLLDVNGIEVIYNHViLVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLlkgerGDV-----TKGYIQYRDERI- 83
Cdd:PRK14239 2 TEPILQVSDLSVYYNKK-KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRM-----NDLnpevtITGSIVYNGHNIy 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 84 -ERLSPAELVKRgVVQVMEGRHCFAhLTIEENLLTGAYTREL-SRGDISIALERVYQ---YFPRLKQRRGSQAGYTSGGE 158
Cdd:PRK14239 76 sPRTDTVDLRKE-IGMVFQQPNPFP-MSIYENVVYGLRLKGIkDKQVLDEAVEKSLKgasIWDEVKDRLHDSALGLSGGQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 159 QQMTAIGRALMASPNMILLDEPSMGLAPQIVEEIFEIVrdLNQREGVSFLLAEQNTNIALRYADygyileNGRVMMDGaa 238
Cdd:PRK14239 154 QQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETL--LGLKDDYTMLLVTRSMQQASRISD------RTGFFLDG-- 223
|
250 260
....*....|....*....|....*....
gi 695928685 239 sDLAQNEDVKEFYLGISSGERKSFRDQKF 267
Cdd:PRK14239 224 -DLIEYNDTKQMFMNPKHKETEDYISGKF 251
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
29-180 |
2.77e-12 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 66.34 E-value: 2.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLkgergDVTKGYIQYRDERIERLSPAELVKR-GVV--QVmegrHC 105
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFY-----DPTSGRILIDGVDIRDLTLESLRRQiGVVpqDT----FL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 106 FaHLTIEENLLTGAytRELSRGDISIALERVY--QYFPRLKQ-------RRGSQAgytSGGEQQMTAIGRALMASPNMIL 176
Cdd:COG1132 426 F-SGTIRENIRYGR--PDATDEEVEEAAKAAQahEFIEALPDgydtvvgERGVNL---SGGQRQRIAIARALLKDPPILI 499
|
....
gi 695928685 177 LDEP 180
Cdd:COG1132 500 LDEA 503
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
29-217 |
2.78e-12 |
|
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: 64.05 E-value: 2.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVT---KGYIQYRDERIErlspaELVKRGVVQVMEGRhc 105
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLlngGPLDFQRDSIAR-----GLLYLGHAPGIKTT-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 106 fahLTIEENLLTgaYTRELSRGDISIALERV----YQYFPrlkqrrgsqAGYTSGGEQQMTAIGRALMASPNMILLDEPS 181
Cdd:cd03231 88 ---LSVLENLRF--WHADHSDEQVEEALARVglngFEDRP---------VAQLSAGQQRRVALARLLLSGRPLWILDEPT 153
|
170 180 190
....*....|....*....|....*....|....*.
gi 695928685 182 MGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIA 217
Cdd:cd03231 154 TALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLS 189
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
33-254 |
3.11e-12 |
|
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: 64.97 E-value: 3.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 33 VSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVtkgYIQYRDerIERLSPAELV---KRGVVQVMEGRHCFAHL 109
Cdd:cd03294 43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKV---LIDGQD--IAAMSRKELRelrRKKISMVFQSFALLPHR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 110 TIEENLltgAYTRELSRGDISIALERVYQYFPR--LKQRRGSQAGYTSGGEQQMTAIGRALMASPNMILLDEPSMGLAPQ 187
Cdd:cd03294 118 TVLENV---AFGLEVQGVPRAEREERAAEALELvgLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPL 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 188 IVEEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDL---AQNEDVKEFYLGI 254
Cdd:cd03294 195 IRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEIltnPANDYVREFFRGV 264
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-247 |
3.24e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 65.64 E-value: 3.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 3 VASPTPPSK-VLLDVNGIEVIYN----HVILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTKGYIQ 77
Cdd:PRK13631 10 LKVPNPLSDdIILRVKNLYCVFDekqeNELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 78 YRDERIERLSPAELVKRGVVQVMEGRHCFAHL-----------TIEENLLTGAYTRELSRGDisiALERVYQYFPRLkqr 146
Cdd:PRK13631 90 IGDKKNNHELITNPYSKKIKNFKELRRRVSMVfqfpeyqlfkdTIEKDIMFGPVALGVKKSE---AKKLAKFYLNKM--- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 147 rGSQAGYT-------SGGEQQMTAIGRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIaLR 219
Cdd:PRK13631 164 -GLDDSYLerspfglSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHV-LE 241
|
250 260
....*....|....*....|....*...
gi 695928685 220 YADYGYILENGRVMMDGAASDLAQNEDV 247
Cdd:PRK13631 242 VADEVIVMDKGKILKTGTPYEIFTDQHI 269
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
14-209 |
3.50e-12 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 64.88 E-value: 3.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 14 LDVNGIEVIY---NHVILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTKGyiqyrDERIErlSPAe 90
Cdd:COG4525 4 LTVRHVSVRYpggGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLD-----GVPVT--GPG- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 91 lVKRGVVqvmegrhcFAH------LTIEENLLTGAYTRELSRGDIsiaLERVYQYFPRLK-----QRRGSQagyTSGGEQ 159
Cdd:COG4525 76 -ADRGVV--------FQKdallpwLNVLDNVAFGLRLRGVPKAER---RARAEELLALVGladfaRRRIWQ---LSGGMR 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 695928685 160 QMTAIGRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLL 209
Cdd:COG4525 141 QRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFL 190
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
29-217 |
3.55e-12 |
|
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: 63.92 E-value: 3.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVtkgyiqyrderierLSPAELVKRGVVQVMEGRHCFAH 108
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEV--------------RWNGTPLAEQRDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 109 -------LTIEENLltgAYTRELSRG---DISIALERVyqyfpRLKQRRGSQAGYTSGGEQQMTAIGRALMASPNMILLD 178
Cdd:TIGR01189 81 lpglkpeLSALENL---HFWAAIHGGaqrTIEDALAAV-----GLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILD 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 695928685 179 EPSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIA 217
Cdd:TIGR01189 153 EPTTALDKAGVALLAGLLRAHLARGGIVLLTTHQDLGLV 191
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
30-254 |
4.00e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 64.80 E-value: 4.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 30 LKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTKGYI----QYRDERIERLSPaelvKRGVVQVMEGRHC 105
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDItithKTKDKYIRPVRK----RIGMVFQFPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 106 FAHlTIEENLLTGAYTRELsrgDISIALERVYQYFPRLKQRRG--SQAGY-TSGGEQQMTAIGRALMASPNMILLDEPSM 182
Cdd:PRK13646 99 FED-TVEREIIFGPKNFKM---NLDEVKNYAHRLLMDLGFSRDvmSQSPFqMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695928685 183 GLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDL-AQNEDVKEFYLGI 254
Cdd:PRK13646 175 GLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELfKDKKKLADWHIGL 247
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
23-180 |
5.89e-12 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 64.86 E-value: 5.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 23 YNHVILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLlkgERgdVTKGYIQYRDERIERLSPAElvkRGVVQVMEG 102
Cdd:PRK11650 13 YDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGL---ER--ITSGEIWIGGRVVNELEPAD---RDIAMVFQN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 103 RHCFAHLTIEENLLTGAYTRELSRGDISialERVYQYFPRLK-----QRRGSQagyTSGGEQQMTAIGRALMASPNMILL 177
Cdd:PRK11650 85 YALYPHMSVRENMAYGLKIRGMPKAEIE---ERVAEAARILElepllDRKPRE---LSGGQRQRVAMGRAIVREPAVFLF 158
|
...
gi 695928685 178 DEP 180
Cdd:PRK11650 159 DEP 161
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
13-202 |
6.35e-12 |
|
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: 65.23 E-value: 6.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 13 LLDVNGIEVIYNHVIlVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDvtkGYIQYRDERIERLSPAELV 92
Cdd:TIGR02633 1 LLEMKGIVKTFGGVK-ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWD---GEIYWSGSPLKASNIRDTE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 93 KRGVVQVMEGRHCFAHLTIEENLLTG-AYTRELSRGDISIALERVYQYFPRLK------QRRGSQAGytsGGEQQMTAIG 165
Cdd:TIGR02633 77 RAGIVIIHQELTLVPELSVAENIFLGnEITLPGGRMAYNAMYLRAKNLLRELQldadnvTRPVGDYG---GGQQQLVEIA 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 695928685 166 RALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQR 202
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH 190
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-180 |
7.79e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 65.09 E-value: 7.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 1 MTVASPTPPSKVLLDVNGIEVIYNHViLVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTKG------ 74
Cdd:COG0488 303 IRFPPPERLGKKVLELEGLSKSYGDK-TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGetvkig 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 75 -YIQYRDERIERLSPAELVKRG--------VVQVMEgrhCFahltieenLLTGaytrelsrgdisialERVYQYFPRLkq 145
Cdd:COG0488 382 yFDQHQEELDPDKTVLDELRDGapggteqeVRGYLG---RF--------LFSG---------------DDAFKPVGVL-- 433
|
170 180 190
....*....|....*....|....*....|....*
gi 695928685 146 rrgsqagytSGGEQQMTAIGRALMASPNMILLDEP 180
Cdd:COG0488 434 ---------SGGEKARLALAKLLLSPPNVLLLDEP 459
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
29-257 |
8.08e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 63.65 E-value: 8.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRavsnlLKGERGDVTKGYIQYRDERIERLSpAELVKRGVVQVMEGRHCFAH 108
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLK-----MLGRHQPPSEGEILLDAQPLESWS-SKAFARKVAYLPQQLPAAEG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 109 LTIEENLLTGAYTRELSRGDISIA-LERVYQYFPR--LKQRRGSQAGYTSGGEQQMTAIGRALMASPNMILLDEPSMGL- 184
Cdd:PRK10575 100 MTVRELVAIGRYPWHGALGRFGAAdREKVEEAISLvgLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALd 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695928685 185 -APQIveEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDLAQNEDVKEFYlGISSG 257
Cdd:PRK10575 180 iAHQV--DVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIY-GIPMG 250
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
29-250 |
8.23e-12 |
|
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: 64.82 E-value: 8.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLravsNLLKG-ERGDVTKGYIQYRDERIERLSPAElvkrgvVQVMEGRHC-- 105
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLM----HVLRGmDQYEPTSGRIIYHVALCEKCGYVE------RPSKVGEPCpv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 106 ----FAHLTIEENLLTGAYTRELSRgDISIALERVYQYFP---------------------------------RLKQRRG 148
Cdd:TIGR03269 85 cggtLEPEEVDFWNLSDKLRRRIRK-RIAIMLQRTFALYGddtvldnvlealeeigyegkeavgravdliemvQLSHRIT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 149 SQAGYTSGGEQQMTAIGRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILE 228
Cdd:TIGR03269 164 HIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLE 243
|
250 260
....*....|....*....|....
gi 695928685 229 NGRVMMDGAASDLAQN--EDVKEF 250
Cdd:TIGR03269 244 NGEIKEEGTPDEVVAVfmEGVSEV 267
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
7-249 |
9.24e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 63.86 E-value: 9.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 7 TPPSKVLLDVNGIEVIYNH-VILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTKGYIQYRDERIER 85
Cdd:PRK13632 1 IKNKSVMIKVENVSFSYPNsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 86 LSPaelvKRGVV------QvmegrhcFAHLTIEENLLTGAYTRELSRGDISIALERVYQYFPRLKQ-RRGSQagYTSGGE 158
Cdd:PRK13632 81 IRK----KIGIIfqnpdnQ-------FIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYlDKEPQ--NLSGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 159 QQMTAIGRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRyADYGYILENGRVMMDGAA 238
Cdd:PRK13632 148 KQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKP 226
|
250
....*....|.
gi 695928685 239 SDLAQNEDVKE 249
Cdd:PRK13632 227 KEILNNKEILE 237
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
30-252 |
1.51e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 63.31 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 30 LKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVT-KGY---IQYRDERIERLSPaelvKRGVVQVMEGRHC 105
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITiAGYhitPETGNKNLKKLRK----KVSLVFQFPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 106 FAHlTIEENLLTGAYTRELSRGDisiALERVYQYFPR--LKQRRGSQAGYT-SGGEQQMTAIGRALMASPNMILLDEPSM 182
Cdd:PRK13641 99 FEN-TVLKDVEFGPKNFGFSEDE---AKEKALKWLKKvgLSEDLISKSPFElSGGQMRRVAIAGVMAYEPEILCLDEPAA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695928685 183 GLAPQIVEEIFEIVRDLnQREGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDLAQNED-VKEFYL 252
Cdd:PRK13641 175 GLDPEGRKEMMQLFKDY-QKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEwLKKHYL 244
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
30-267 |
1.71e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 63.19 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 30 LKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLkgergDVTKGYIQYRDERIERLSPAELVKRGVVQVMEGRHCFAHL 109
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLF-----EEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPDNQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 110 TIEENLLTGAYTRELSRGDIsiaLERVYQYFPRLKQR--RGSQAGYTSGGEQQMTAIGRALMASPNMILLDEPSMGLAPQ 187
Cdd:PRK13642 98 TVEDDVAFGMENQGIPREEM---IKRVDEALLAVNMLdfKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 188 IVEEIFEIVRDLNQREGVSFLLAEQNTNIALRyADYGYILENGRVMMDGAASDL-AQNEDVKEFYLGI--SSGERKSFRD 264
Cdd:PRK13642 175 GRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELfATSEDMVEIGLDVpfSSNLMKDLRK 253
|
...
gi 695928685 265 QKF 267
Cdd:PRK13642 254 NGF 256
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
30-230 |
1.93e-11 |
|
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: 62.10 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 30 LKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGergdvTKGYIQYRDERIERLSPAELVkrgvvqVMEGRHCFAHL 109
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQP-----TSGGVILEGKQITEPGPDRMV------VFQNYSLLPWL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 110 TIEENlltgaytrelsrgdISIALERVYQYFPRLKQRR---------------GSQAGYTSGGEQQMTAIGRALMASPNM 174
Cdd:TIGR01184 70 TVREN--------------IALAVDRVLPDLSKSERRAiveehialvglteaaDKRPGQLSGGMKQRVAIARALSIRPKV 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 695928685 175 ILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILENG 230
Cdd:TIGR01184 136 LLLDEPFGALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
28-246 |
2.38e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 62.46 E-value: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 28 LVLKGVSLRVPEGKIVALLGANGAGKTTtlraVSNLLKGERgDVTKGYIQYRDERIERLSPAELVKR-GVV-QVMEGRhc 105
Cdd:PRK13648 23 FTLKDVSFNIPKGQWTSIVGHNGSGKST----IAKLMIGIE-KVKSGEIFYNNQAITDDNFEKLRKHiGIVfQNPDNQ-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 106 FAHLTIEENLLTGAYTRELSRGD----ISIALERVYQYfprlkQRRGSQAGYTSGGEQQMTAIGRALMASPNMILLDEPS 181
Cdd:PRK13648 96 FVGSIVKYDVAFGLENHAVPYDEmhrrVSEALKQVDML-----ERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEAT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695928685 182 MGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRyADYGYILENGRVMMDGAASDLAQNED 246
Cdd:PRK13648 171 SMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAE 234
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
29-241 |
2.55e-11 |
|
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: 61.86 E-value: 2.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTtlraVSNLLKgeR-GDVTKGYIQYRDERIERLSPAELvKRGVVQVMEGRHCFa 107
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKST----LVNLIP--RfYDVDSGRILIDGHDVRDYTLASL-RRQIGLVSQDVFLF- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 108 HLTIEENLLTGayTRELSRGDISIALERVY--QYFPRLKQ-------RRGSQagyTSGGEQQMTAIGRALMASPNMILLD 178
Cdd:cd03251 89 NDTVAENIAYG--RPGATREEVEEAARAANahEFIMELPEgydtvigERGVK---LSGGQRQRIAIARALLKDPPILILD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695928685 179 EPSMGLAPQIVEEIFEIVRDLNQREgVSFLLAEQNTNIalRYADYGYILENGRVMMDGAASDL 241
Cdd:cd03251 164 EATSALDTESERLVQAALERLMKNR-TTFVIAHRLSTI--ENADRIVVLEDGKIVERGTHEEL 223
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1-241 |
2.56e-11 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 63.22 E-value: 2.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 1 MTVASPTPPSKVLLDVNGIEVIYNHVILVlKGVSLRVPEGKIVALLGANGAG--KTTTLRAVSNLLKGERGDVTKGYIQY 78
Cdd:NF000106 1 MTRKTISNGARNAVEVRGLVKHFGEVKAV-DGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRPWRF*TWCAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 79 RDERIERLSPAELVKRGVVQVMEGRhcfahltieENLLTGAYTRELSRGDISIALERVYQYFpRLKQRRGSQAGYTSGGE 158
Cdd:NF000106 80 RRALRRTIG*HRPVR*GRRESFSGR---------ENLYMIGR*LDLSRKDARARADELLERF-SLTEAAGRAAAKYSGGM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 159 QQMTAIGRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLnQREGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAA 238
Cdd:NF000106 150 RRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSM-VRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKV 228
|
...
gi 695928685 239 SDL 241
Cdd:NF000106 229 DEL 231
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
33-233 |
2.66e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 62.97 E-value: 2.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 33 VSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVT-KGYIQYRDERIERLSPAelvKRGVVQVMEGRHCFAHLTI 111
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVlNGRVLFDAEKGICLPPE---KRRIGYVFQDARLFPHYKV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 112 EENLLTGAYTRELSRGDISIAL---ERVYQYFPrlkqrrgsqaGYTSGGEQQMTAIGRALMASPNMILLDEPSMGLapqi 188
Cdd:PRK11144 94 RGNLRYGMAKSMVAQFDKIVALlgiEPLLDRYP----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASL---- 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 695928685 189 veeifeivrDL-NQREGVSFL--LAEQ-NTNIA---------LRYADYGYILENGRVM 233
Cdd:PRK11144 160 ---------DLpRKRELLPYLerLAREiNIPILyvshsldeiLRLADRVVVLEQGKVK 208
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
13-206 |
4.45e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 62.64 E-value: 4.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 13 LLDVNGIEVIYNHVIlVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKgeRGDVtKGYIQYRDERIERLSPAELV 92
Cdd:PRK13549 5 LLEMKNITKTFGGVK-ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYP--HGTY-EGEIIFEGEELQASNIRDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 93 KRGVVQVMEGRHCFAHLTIEENLLTGaytRELSRGDIsIALERVYQYFPRLKQRRG------SQAGYTSGGEQQMTAIGR 166
Cdd:PRK13549 81 RAGIAIIHQELALVKELSVLENIFLG---NEITPGGI-MDYDAMYLRAQKLLAQLKldinpaTPVGNLGLGQQQLVEIAK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 695928685 167 ALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLnQREGVS 206
Cdd:PRK13549 157 ALNKQARLLILDEPTASLTESETAVLLDIIRDL-KAHGIA 195
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
29-244 |
5.41e-11 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 62.43 E-value: 5.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTtlraVSNLLKgERGDVTKGYIQYRDERIERLSPAELvKRGVVQVMEGRHCFAH 108
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKST----LVNLIP-RFYEPDSGQILLDGHDLADYTLASL-RRQVALVSQDVVLFND 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 109 lTIEENLLTGAyTRELSRGDISIALERVY-QYF----PR-LKQRRGSQAGYTSGGEQQMTAIGRALMASPNMILLDEPSM 182
Cdd:TIGR02203 421 -TIANNIAYGR-TEQADRAEIERALAAAYaQDFvdklPLgLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATS 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695928685 183 GLAPQiVEEIFEIVRDLNQREGVSFLLAEQNTNIalRYADYGYILENGRVMMDGAASDL-AQN 244
Cdd:TIGR02203 499 ALDNE-SERLVQAALERLMQGRTTLVIAHRLSTI--EKADRIVVMDDGRIVERGTHNELlARN 558
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
28-232 |
1.23e-10 |
|
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: 59.79 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 28 LVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVtkgyiqyrderierlspaeLVKRGVVQVMEgrHCFA 107
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQV-------------------LLDGKPISQYE--HKYL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 108 HLTI-----EENLLTGAYTRELSRGDISIALERV---------YQYFPRLKQ-------RRGSQagyTSGGEQQMTAIGR 166
Cdd:cd03248 87 HSKVslvgqEPVLFARSLQDNIAYGLQSCSFECVkeaaqkahaHSFISELASgydtevgEKGSQ---LSGGQKQRVAIAR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695928685 167 ALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTniaLRYADYGYILENGRV 232
Cdd:cd03248 164 ALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLST---VERADQILVLDGGRI 226
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
14-181 |
1.25e-10 |
|
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: 58.23 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 14 LDVNGIEVIYNHVILvLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTKGyiqyrderierlspaelvk 93
Cdd:cd03221 1 IELENLSKTYGGKLL-LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 94 rgvvqvmegrhcfahltieenlltgaytrelsrGDISIAlervyqYFPRLkqrrgsqagytSGGEQQMTAIGRALMASPN 173
Cdd:cd03221 61 ---------------------------------STVKIG------YFEQL-----------SGGEKMRLALAKLLLENPN 90
|
....*...
gi 695928685 174 MILLDEPS 181
Cdd:cd03221 91 LLLLDEPT 98
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
14-179 |
1.30e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 61.27 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 14 LDVNGIEVIYNHVILVLKGVSLRVPEGKIVALLGANGAGKTTtlraVSNLLKGERgDVTKGYIQYRDERIERLSPAELvK 93
Cdd:PRK10790 341 IDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKST----LASLLMGYY-PLTEGEIRLDGRPLSSLSHSVL-R 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 94 RGVVQVMEGRHCFAHlTIEENLLTGaytRELSRGDISIALERV-----YQYFPR-LKQRRGSQAGYTSGGEQQMTAIGRA 167
Cdd:PRK10790 415 QGVAMVQQDPVVLAD-TFLANVTLG---RDISEEQVWQALETVqlaelARSLPDgLYTPLGEQGNNLSVGQKQLLALARV 490
|
170
....*....|..
gi 695928685 168 LMASPNMILLDE 179
Cdd:PRK10790 491 LVQTPQILILDE 502
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
26-236 |
1.65e-10 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 59.47 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 26 VILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTkgyiqyrderierlspaelVKRGVVQVMEGRHC 105
Cdd:cd03220 34 EFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT-------------------VRGRVSSLLGLGGG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 106 F-AHLTIEENLLTGAYTRELSRGDISIALERVYQyFPRLKQRRGSQAGYTSGGEQQMTAIGRALMASPNMILLDEpsmGL 184
Cdd:cd03220 95 FnPELTGRENIYLNGRLLGLSRKEIDEKIDEIIE-FSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDE---VL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 695928685 185 A---PQIVEEIFEIVRDLNQReGVSFLLAEQNTNIALRYADYGYILENGRVMMDG 236
Cdd:cd03220 171 AvgdAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
29-259 |
1.82e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 59.71 E-value: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTkgyiqyRDERIerLSPAELvkrGVvqvmeGRHcfAH 108
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE------VNGRV--SALLEL---GA-----GFH--PE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 109 LTIEENLLTGAYTRELSRGDI-----SIA----LERvyqYF--PrLKQrrgsqagYTSGgeqqMTA-IGRALMAS--PNM 174
Cdd:COG1134 103 LTGRENIYLNGRLLGLSRKEIdekfdEIVefaeLGD---FIdqP-VKT-------YSSG----MRArLAFAVATAvdPDI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 175 ILLDEpsmGLApqiV----------EEIFEIVrdlnqREGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAAsdlaqn 244
Cdd:COG1134 168 LLVDE---VLA---VgdaafqkkclARIRELR-----ESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDP------ 230
|
250
....*....|....*
gi 695928685 245 EDVKEFYLGISSGER 259
Cdd:COG1134 231 EEVIAAYEALLAGRE 245
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
29-232 |
1.97e-10 |
|
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: 58.38 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKgergdVTKGYIQYRDERIERLSPAELvkrgvvqvmegRHCFAH 108
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLR-----PTSGRVRLDGADISQWDPNEL-----------GDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 109 LTIEENLLTGaytrelsrgdiSIAlERVYqyfprlkqrrgsqagytSGGEQQMTAIGRALMASPNMILLDEPSMGLAPQI 188
Cdd:cd03246 81 LPQDDELFSG-----------SIA-ENIL-----------------SGGQRQRLGLARALYGNPRILVLDEPNSHLDVEG 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 695928685 189 VEEIFEIVRDLNQREGVSFLLAEQNTNIALryADYGYILENGRV 232
Cdd:cd03246 132 ERALNQAIAALKAAGATRIVIAHRPETLAS--ADRILVLEDGRV 173
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
29-241 |
2.12e-10 |
|
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: 59.17 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLkgergDVTKGYIQYRDERIERLSPAELVKR-GVV---QVMegrh 104
Cdd:cd03253 16 VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFY-----DVSSGSILIDGQDIREVTLDSLRRAiGVVpqdTVL---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 105 cFaHLTIEENLltgAYTReLSRGDISI-------ALERVYQYFPR-LKQRRGSQAGYTSGGEQQMTAIGRALMASPNMIL 176
Cdd:cd03253 87 -F-NDTIGYNI---RYGR-PDATDEEVieaakaaQIHDKIMRFPDgYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695928685 177 LDEPSMGLAPQIVEEIFEIVRDLNQREgVSFLLAEQNTNIAlrYADYGYILENGRVMMDGAASDL 241
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGR-TTIVIAHRLSTIV--NADKIIVLKDGRIVERGTHEEL 222
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
30-209 |
2.18e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.79 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 30 LKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTkgyiqYRDERIERLSPAELVKRGVVQVMEGRH---CF 106
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVT-----LDGHEVVTRSPQDGLANGIVYISEDRKrdgLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 107 AHLTIEENL-LTGayTRELSRGDISI-------ALERVYQYFPRLKQRRGSQAGYTSGGEQQMTAIGRALMASPNMILLD 178
Cdd:PRK10762 343 LGMSVKENMsLTA--LRYFSRAGGSLkhadeqqAVSDFIRLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILD 420
|
170 180 190
....*....|....*....|....*....|...
gi 695928685 179 EPSMGLAPQIVEEIFEIVrdlNQ--REGVSFLL 209
Cdd:PRK10762 421 EPTRGVDVGAKKEIYQLI---NQfkAEGLSIIL 450
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
29-241 |
2.30e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 59.64 E-value: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVtkgyiqyrderIERLSPAELVKRGVVQVME------- 101
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAV-----------LWQGKPLDYSKRGLLALRQqvatvfq 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 102 --GRHCFaHLTIEENLltgAYT-RELSRGDISIAlERVYQYFPRLKQRRGSQAGYT--SGGEQQMTAIGRALMASPNMIL 176
Cdd:PRK13638 85 dpEQQIF-YTDIDSDI---AFSlRNLGVPEAEIT-RRVDEALTLVDAQHFRHQPIQclSHGQKKRVAIAGALVLQARYLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695928685 177 LDEPSMGLAPQIVEEIFEIVRDLNQrEGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDL 241
Cdd:PRK13638 160 LDEPTAGLDPAGRTQMIAIIRRIVA-QGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV 223
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
28-236 |
3.56e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 59.33 E-value: 3.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 28 LVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVtkgYIQYRDERIER-----LSPAELVKRG-----VV 97
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKV---YVDGLDTSDEEnlwdiRNKAGMVFQNpdnqiVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 98 QVMEGRHCFAhltiEENLltGAYTRELsRGDISIALERV--YQYfprlkqrRGSQAGYTSGGEQQMTAIGRALMASPNMI 175
Cdd:PRK13633 101 TIVEEDVAFG----PENL--GIPPEEI-RERVDESLKKVgmYEY-------RRHAPHLLSGGQKQRVAIAGILAMRPECI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695928685 176 LLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRyADYGYILENGRVMMDG 236
Cdd:PRK13633 167 IFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEG 226
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
25-244 |
3.67e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 59.33 E-value: 3.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 25 HVILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVT-KGYIQYRDERierlspaELVKR-GVV--Q-- 98
Cdd:COG4586 33 REVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRvLGYVPFKRRK-------EFARRiGVVfgQrs 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 99 -------VMEGRHCFAHL----------TIEE--------NLLTGAyTRELSRGdisialervyqyfprlkQRrgsqagy 153
Cdd:COG4586 106 qlwwdlpAIDSFRLLKAIyripdaeykkRLDElvelldlgELLDTP-VRQLSLG-----------------QR------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 154 tsggeqqMTA-IGRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTN--IALryADYGYILENG 230
Cdd:COG4586 161 -------MRCeLAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDdiEAL--CDRVIVIDHG 231
|
250
....*....|....
gi 695928685 231 RVMMDGAASDLAQN 244
Cdd:COG4586 232 RIIYDGSLEELKER 245
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
29-254 |
4.31e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 59.04 E-value: 4.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTKGYIqyrderierlSPAELVKRGVVQVMEG------ 102
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITV----------DGITLTAKTVWDIREKvgivfq 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 103 --RHCFAHLTIEENLLTGAYTRELSRGDISIALERVYQYFPRLKQRRgSQAGYTSGGEQQMTAIGRALMASPNMILLDEP 180
Cdd:PRK13640 92 npDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYID-SEPANLSGGQKQRVAIAGILAVEPKIIILDES 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695928685 181 SMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIAlRYADYGYILENGRVMMDGAASDLAQNED-VKEFYLGI 254
Cdd:PRK13640 171 TSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVEmLKEIGLDI 244
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
11-247 |
5.99e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 58.95 E-value: 5.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 11 KVLLDVNGIEVIYN------------HVILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGergdvTKGYIQY 78
Cdd:PRK15079 6 KVLLEVADLKVHFDikdgkqwfwqppKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKA-----TDGEVAW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 79 RDERIERLSPAEL-VKRGVVQvMEGRHCFAHLT--------IEENLLTgaYTRELSRGDISialERVYQY------FPRL 143
Cdd:PRK15079 81 LGKDLLGMKDDEWrAVRSDIQ-MIFQDPLASLNprmtigeiIAEPLRT--YHPKLSRQEVK---DRVKAMmlkvglLPNL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 144 KQRrgsqagYT---SGGEQQMTAIGRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLnQRE-GVSFLLaeqntnIALR 219
Cdd:PRK15079 155 INR------YPhefSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQL-QREmGLSLIF------IAHD 221
|
250 260
....*....|....*....|....*...
gi 695928685 220 YADYGYILENGRVMMDGAASDLAQNEDV 247
Cdd:PRK15079 222 LAVVKHISDRVLVMYLGHAVELGTYDEV 249
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
30-255 |
6.81e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 58.46 E-value: 6.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 30 LKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTKGYIQYRDerierLSPAELVKRGVVQVMEGRHC-FAH 108
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGD-----FSKLQGIRKLVGIVFQNPETqFVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 109 LTIEENLLTGAYTRELSRGDISIALERVYQYFpRLKQRRGSQAGYTSGGEQQMTAIGRALMASPNMILLDEPSMGLAPQI 188
Cdd:PRK13644 93 RTVEEDLAFGPENLCLPPIEIRKRVDRALAEI-GLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDS 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695928685 189 VEEIFEIVRDLNqREGVSFLLAEQNTNiALRYADYGYILENGRVMMDGAASDLAQNEDVKefYLGIS 255
Cdd:PRK13644 172 GIAVLERIKKLH-EKGKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLSDVSLQ--TLGLT 234
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
25-197 |
8.13e-10 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 57.27 E-value: 8.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 25 HVILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGE---RGDVTKGYIQYRDErierlspAELVKRGVVQVME 101
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEF-------AEKYPGEIIYVSE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 102 GRHCFAHLTIEENLltgaYTRELSRGDisialervyQYFprlkqrRGsqagyTSGGEQQMTAIGRALMASPNMILLDEPS 181
Cdd:cd03233 91 EDVHFPTLTVRETL----DFALRCKGN---------EFV------RG-----ISGGERKRVSIAEALVSRASVLCWDNST 146
|
170
....*....|....*.
gi 695928685 182 MGLAPQIVEEIFEIVR 197
Cdd:cd03233 147 RGLDSSTALEILKCIR 162
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
29-184 |
8.36e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 57.82 E-value: 8.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGdvtkgyiqyrdeRIERlsPAELVKRGVVQVMegrhcfaH 108
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG------------VIKR--NGKLRIGYVPQKL-------Y 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 109 LTIEENLLTGAYTR---ELSRGDISIALERVyqyfprlkqrrgsQAGY--------TSGGEQQMTAIGRALMASPNMILL 177
Cdd:PRK09544 78 LDTTLPLTVNRFLRlrpGTKKEDILPALKRV-------------QAGHlidapmqkLSGGETQRVLLARALLNRPQLLVL 144
|
....*..
gi 695928685 178 DEPSMGL 184
Cdd:PRK09544 145 DEPTQGV 151
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
155-254 |
8.80e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 58.22 E-value: 8.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 155 SGGEQQMTAIGRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQrEGVSFLLAEQNTNIALRYADYGYILENGRVMM 234
Cdd:PRK13649 147 SGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQ-SGMTIVLVTHLMDDVANYADFVYVLEKGKLVL 225
|
90 100
....*....|....*....|.
gi 695928685 235 DGAASDLAQNED-VKEFYLGI 254
Cdd:PRK13649 226 SGKPKDIFQDVDfLEEKQLGV 246
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
14-244 |
1.70e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 57.02 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 14 LDVNGIeVIYNHVILVlKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLL-KGERgdVTKGYIQYRDERIerlSPAELV 92
Cdd:PRK10418 5 IELRNI-ALQAAQPLV-HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILpAGVR--QTAGRVLLDGKPV---APCALR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 93 KRGVVQVMEG-RHCF------AHLTIEENLLTGaytRELSRGDISIALE--------RVYQYFPRlkqrrgsqagYTSGG 157
Cdd:PRK10418 78 GRKIATIMQNpRSAFnplhtmHTHARETCLALG---KPADDATLTAALEavglenaaRVLKLYPF----------EMSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 158 EQQMTAIGRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILENGRVMMDGA 237
Cdd:PRK10418 145 MLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGD 224
|
....*..
gi 695928685 238 ASDLAQN 244
Cdd:PRK10418 225 VETLFNA 231
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
30-243 |
1.77e-09 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 58.05 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 30 LKGVSLRVPEGKIVALLGANGAGKTTTLravsNLLkgERG-DVTKGYIQYRDERIERLSPAELvKRGVVQVMEGRHCFAH 108
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLI----NLL--QRVfDPQSGRILIDGTDIRTVTRASL-RRNIAVVFQDAGLFNR 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 109 lTIEENLLTG---AYTRELSRG-DISIALERVYQYFPRLKQRRGSQAGYTSGGEQQMTAIGRALMASPNMILLDEPSMGL 184
Cdd:PRK13657 424 -SIEDNIRVGrpdATDEEMRAAaERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSAL 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 185 APQIVEEIFEIVRDLnqREG-VSFLLAEQNTNIalRYADYGYILENGRVMMDGAASDLAQ 243
Cdd:PRK13657 503 DVETEAKVKAALDEL--MKGrTTFIIAHRLSTV--RNADRILVFDNGRVVESGSFDELVA 558
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
26-236 |
1.87e-09 |
|
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: 57.89 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 26 VILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVtkgYIQYRDERIERLSPAELVKRGVVQVMEGRH- 104
Cdd:TIGR03269 296 VVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEV---NVRVGDEWVDMTKPGPDGRGRAKRYIGILHq 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 105 ---CFAHLTIEENLlTGA----YTRELSRGDISIAL-------ERVYQYFPRLKQRrgsqagyTSGGEQQMTAIGRALMA 170
Cdd:TIGR03269 373 eydLYPHRTVLDNL-TEAigleLPDELARMKAVITLkmvgfdeEKAEEILDKYPDE-------LSEGERHRVALAQVLIK 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 171 SPNMILLDEPSMGLAP----QIVEEIFEIVRDLNQregvSFLLAEQNTNIALRYADYGYILENGRVMMDG 236
Cdd:TIGR03269 445 EPRIVILDEPTGTMDPitkvDVTHSILKAREEMEQ----TFIIVSHDMDFVLDVCDRAALMRDGKIVKIG 510
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
30-199 |
2.05e-09 |
|
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: 55.71 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 30 LKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNllKGERGDVTkGYI----QYRDERIERLSpaelvkrGVVQVMEgrhc 105
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAGVIT-GEIlingRPLDKNFQRST-------GYVEQQD---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 106 fAH---LTIEENLLTGAYTRELSrgdisialervyqyfprLKQRRgsqagytsggeqqMTAIGRALMASPNMILLDEPSM 182
Cdd:cd03232 89 -VHspnLTVREALRFSALLRGLS-----------------VEQRK-------------RLTIGVELAAKPSILFLDEPTS 137
|
170
....*....|....*..
gi 695928685 183 GLAPQIVEEIFEIVRDL 199
Cdd:cd03232 138 GLDSQAAYNIVRFLKKL 154
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
32-180 |
2.55e-09 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 57.05 E-value: 2.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 32 GVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLkgergDVTKGYIQYRDERIERLSPAELVK-RGVVQVMegrhcF---- 106
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLE-----EPTSGEILFDGQDITGLSGRELRPlRRRMQMV-----Fqdpy 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 107 AHL--------TIEE-----NLLTGA----YTRELsrgdisiaLERV------YQYFPRLkqrrgsqagyTSGGEQQMTA 163
Cdd:COG4608 106 ASLnprmtvgdIIAEplrihGLASKAerreRVAEL--------LELVglrpehADRYPHE----------FSGGQRQRIG 167
|
170
....*....|....*..
gi 695928685 164 IGRALMASPNMILLDEP 180
Cdd:COG4608 168 IARALALNPKLIVCDEP 184
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
31-247 |
3.19e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.10 E-value: 3.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 31 KGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKgergdVTKGYIQYRDERIERLSPAELVKRGVVQVMEGRH---CFA 107
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDK-----RAGGEIRLNGKDISPRSPLDAVKKGMAYITESRRdngFFP 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 108 HLTIEEN------LLTGAY--------------TRELSRGDISIALERVYQYFPRLkqrrgsqagytSGGEQQMTAIGRA 167
Cdd:PRK09700 355 NFSIAQNmaisrsLKDGGYkgamglfhevdeqrTAENQRELLALKCHSVNQNITEL-----------SGGNQQKVLISKW 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 168 LMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQrEGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDLAQNEDV 247
Cdd:PRK09700 424 LCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAD-DGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMSEEEI 502
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
13-180 |
3.50e-09 |
|
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: 55.52 E-value: 3.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 13 LLDVNGIE---VIYNH---VILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAV--SNLlkgergdVTKGYIQYRDErie 84
Cdd:COG4778 4 LLEVENLSktfTLHLQggkRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIygNYL-------PDSGSILVRHD--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 85 rLSPAELVKRGVVQVMEGR-----HCFAHL----------TIEENLLTGAYTRELSRGDISIALERVyqyfpRLKQRRGS 149
Cdd:COG4778 74 -GGWVDLAQASPREILALRrrtigYVSQFLrviprvsaldVVAEPLLERGVDREEARARARELLARL-----NLPERLWD 147
|
170 180 190
....*....|....*....|....*....|..
gi 695928685 150 QAGYT-SGGEQQMTAIGRALMASPNMILLDEP 180
Cdd:COG4778 148 LPPATfSGGEQQRVNIARGFIADPPLLLLDEP 179
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
33-245 |
3.65e-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: 56.76 E-value: 3.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 33 VSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGErgdvTKGYIQYRDERIERLSPAELVKRGVVQVMEGRH---CFAHL 109
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGK----FEGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKrhgIVPIL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 110 TIEENLLTGAYTRELSRGDISIALER--VYQYFPRLKQRRGS---QAGYTSGGEQQMTAIGRALMASPNMILLDEPSMGL 184
Cdd:TIGR02633 355 GVGKNITLSVLKSFCFKMRIDAAAELqiIGSAIQRLKVKTASpflPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGV 434
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695928685 185 APQIVEEIFEIVRDLNQrEGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDLAQNE 245
Cdd:TIGR02633 435 DVGAKYEIYKLINQLAQ-EGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGDFVNHALTQEQ 494
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
30-258 |
4.20e-09 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 56.98 E-value: 4.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 30 LKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLkgERGDVTKGYIQYRDERIErlspAELVKRGVVQVMEGRHCFAHL 109
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRS--PKGVKGSGSVLLNGMPID----AKEMRAISAYVQQDDLFIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 110 TIEENLLTGAYTRELSRGDISIALERVYQYFPRLKQRR--------GSQAGYTSGGEQQMTAIGRALMASPNMILLDEPS 181
Cdd:TIGR00955 115 TVREHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKcantrigvPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 182 MGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDLAQ-----------NEDVKEF 250
Cdd:TIGR00955 195 SGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAVPffsdlghpcpeNYNPADF 274
|
....*...
gi 695928685 251 YLGISSGE 258
Cdd:TIGR00955 275 YVQVLAVI 282
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
33-208 |
8.60e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.02 E-value: 8.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 33 VSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTkgyiqYRDERIERLSPAEL--VKRGVVQV-------MEGR 103
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEII-----FNGQRIDTLSPGKLqaLRRDIQFIfqdpyasLDPR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 104 HCFAHLTIEENLLTGAYTRELSRGDISIALERVyQYFPRLKQRRGSQagyTSGGEQQMTAIGRALMASPNMILLDEPSMG 183
Cdd:PRK10261 418 QTVGDSIMEPLRVHGLLPGKAAAARVAWLLERV-GLLPEHAWRYPHE---FSGGQRQRICIARALALNPKVIIADEAVSA 493
|
170 180
....*....|....*....|....*
gi 695928685 184 LAPQIVEEIFEIVRDLNQREGVSFL 208
Cdd:PRK10261 494 LDVSIRGQIINLLLDLQRDFGIAYL 518
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
32-180 |
1.01e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 54.04 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 32 GVSLRVPEGKIVALLGANGAGKTTTLRAVSNLlkgerGDVTKGYIQYRDERIERLSPA---EL--------VKRgvvqvm 100
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGL-----ARPDAGEVLWQGEPIRRQRDEyhqDLlylghqpgIKT------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 101 egrhcfaHLTIEENL-----LTGAYTRElsrgDISIALERVyqyfpRLKQRRGSQAGYTSGGEQQMTAIGRALMASPNMI 175
Cdd:PRK13538 88 -------ELTALENLrfyqrLHGPGDDE----ALWEALAQV-----GLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLW 151
|
....*
gi 695928685 176 LLDEP 180
Cdd:PRK13538 152 ILDEP 156
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
34-209 |
1.43e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.02 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 34 SLRVPEGKIVALLGANGAGKTTTLRAVSN---LLKGERgdvtkgyiQYRDERIERLSPAELVKRgVVQVMEGRHCFAHLT 110
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGelpLLSGER--------QSQFSHITRLSFEQLQKL-VSDEWQRNNTDMLSP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 111 IEENllTGAYTRELSRGDIS--IALERVYQYF--PRLKQRRGSqagYTSGGEQQMTAIGRALMASPNMILLDEPSMGLAP 186
Cdd:PRK10938 94 GEDD--TGRTTAEIIQDEVKdpARCEQLAQQFgiTALLDRRFK---YLSTGETRKTLLCQALMSEPDLLILDEPFDGLDV 168
|
170 180
....*....|....*....|...
gi 695928685 187 QIVEEIFEIVRDLNQrEGVSFLL 209
Cdd:PRK10938 169 ASRQQLAELLASLHQ-SGITLVL 190
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
33-184 |
2.00e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 54.85 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 33 VSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKgERGDVTKGYIQYRDerierLSPAELvKRGVVQVMEGRHCFaHLTIE 112
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP-YQGSLKINGIELRE-----LDPESW-RKHLSWVGQNPQLP-HGTLR 440
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695928685 113 ENLLTGAYtrELSRGDISIALERVY--QYFPRLKQ----RRGSQAGYTSGGEQQMTAIGRALMASPNMILLDEPSMGL 184
Cdd:PRK11174 441 DNVLLGNP--DASDEQLQQALENAWvsEFLPLLPQgldtPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASL 516
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
30-244 |
2.20e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 54.64 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 30 LKGVSLRVPEGKIVALLGANGAGKTTtlraVSNLLKgeR-GDVTKGYIQY-----RDERIERLspaelvKRGVVQVMEGR 103
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKST----IANLLT--RfYDIDEGEILLdghdlRDYTLASL------RNQVALVSQNV 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 104 HCFAHlTIEENLltgAYTRE--LSRGDISIALERVY--QYFPRLKQRR----GSQAGYTSGGEQQMTAIGRALMASPNMI 175
Cdd:PRK11176 427 HLFND-TIANNI---AYARTeqYSREQIEEAARMAYamDFINKMDNGLdtviGENGVLLSGGQRQRIAIARALLRDSPIL 502
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 176 LLDEPSMGLAPQiVEEIFEIVRDLNQREGVSFLLAEQNTNIalRYADYGYILENGRVMMDGAASDL-AQN 244
Cdd:PRK11176 503 ILDEATSALDTE-SERAIQAALDELQKNRTSLVIAHRLSTI--EKADEILVVEDGEIVERGTHAELlAQN 569
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
10-243 |
2.54e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 53.49 E-value: 2.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 10 SKVLLDVNGIEVIYNHvILVLKGVSLRVPEGKIVALLGANGAGKTTtlraVSNLLKGERG-DVTKGYIQYRDERIERLSP 88
Cdd:CHL00131 4 NKPILEIKNLHASVNE-NEILKGLNLSINKGEIHAIMGPNGSGKST----LSKVIAGHPAyKILEGDILFKGESILDLEP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 89 AELVKRGVVQVMEgrhcfahLTIE------ENLLTGAY-TRELSRGDISIALERVYQYF-PRLKQ--------RRGSQAG 152
Cdd:CHL00131 79 EERAHLGIFLAFQ-------YPIEipgvsnADFLRLAYnSKRKFQGLPELDPLEFLEIInEKLKLvgmdpsflSRNVNEG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 153 YtSGGEQQMTAIGRALMASPNMILLDEPSMGL---APQIVEEIFEIVRDLNQregvSFLLAEQNTNIaLRY--ADYGYIL 227
Cdd:CHL00131 152 F-SGGEKKRNEILQMALLDSELAILDETDSGLdidALKIIAEGINKLMTSEN----SIILITHYQRL-LDYikPDYVHVM 225
|
250
....*....|....*.
gi 695928685 228 ENGRVMMDGAASdLAQ 243
Cdd:CHL00131 226 QNGKIIKTGDAE-LAK 240
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
30-206 |
4.09e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 53.20 E-value: 4.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 30 LKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVtkgYIQYrderiERLSPAEL--VKRGVVQVMEG-RHCF 106
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQI---IIDG-----DLLTEENVwdIRHKIGMVFQNpDNQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 107 AHLTIEENLLTGAYTRELSRGDIsiaLERVYQYFP-----RLKQRRGSQagyTSGGEQQMTAIGRALMASPNMILLDEPS 181
Cdd:PRK13650 95 VGATVEDDVAFGLENKGIPHEEM---KERVNEALElvgmqDFKEREPAR---LSGGQKQRVAIAGAVAMRPKIIILDEAT 168
|
170 180
....*....|....*....|....*
gi 695928685 182 MGLAPQIVEEIFEIVRDLNQREGVS 206
Cdd:PRK13650 169 SMLDPEGRLELIKTIKGIRDDYQMT 193
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
6-206 |
6.06e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.39 E-value: 6.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 6 PTPPSKVLLDVNGIEVIY--NHVILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGE-RGDVtkgYIQYRDER 82
Cdd:PRK13549 252 PHTIGEVILEVRNLTAWDpvNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRwEGEI---FIDGKPVK 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 83 IErlSPAELVKRGVVQVMEGRHcfAH-----LTIEENLLTGAYTRELSRGDISIALER--VYQYFPRLKQRRGSQA---G 152
Cdd:PRK13549 329 IR--NPQQAIAQGIAMVPEDRK--RDgivpvMGVGKNITLAALDRFTGGSRIDDAAELktILESIQRLKVKTASPElaiA 404
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 695928685 153 YTSGGEQQMTAIGRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQrEGVS 206
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQ-QGVA 457
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
14-184 |
6.44e-08 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 53.20 E-value: 6.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 14 LDVNGIEVIYNHVILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTKGYIQYRDERIERLspaelvK 93
Cdd:TIGR01193 474 IVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTL------R 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 94 RGVVQVMEGRHCFAHlTIEENLLTGAyTRELSRGDISIALERV-----YQYFPRLKQRRGSQAGYT-SGGEQQMTAIGRA 167
Cdd:TIGR01193 548 QFINYLPQEPYIFSG-SILENLLLGA-KENVSQDEIWAACEIAeikddIENMPLGYQTELSEEGSSiSGGQKQRIALARA 625
|
170
....*....|....*..
gi 695928685 168 LMASPNMILLDEPSMGL 184
Cdd:TIGR01193 626 LLTDSKVLILDESTSNL 642
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
29-240 |
8.62e-08 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 52.83 E-value: 8.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVtkgyiqyrdeR-----IERLSPAELvkrgvvqvmeGR 103
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSV----------RldgadLSQWDREEL----------GR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 104 HcFAHL---------TIEENLltgaytrelSR-GDISIalERVY------------QYFPRlkqrrgsqaGY-T------ 154
Cdd:COG4618 407 H-IGYLpqdvelfdgTIAENI---------ARfGDADP--EKVVaaaklagvhemiLRLPD---------GYdTrigegg 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 155 ---SGGEQQMTAIGRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQReGVSFLLAEQNTNIaLRYADYGYILENGR 231
Cdd:COG4618 466 arlSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSL-LAAVDKLLVLRDGR 543
|
....*....
gi 695928685 232 VMMDGAASD 240
Cdd:COG4618 544 VQAFGPRDE 552
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-209 |
8.63e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.79 E-value: 8.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 3 VASPTPPskvLLDVNGIEVIY------------NHVilVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGErgd 70
Cdd:PRK15134 268 LPEPASP---LLDVEQLQVAFpirkgilkrtvdHNV--VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ--- 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 71 vtkGYIQYRDERIERLSPAELVK-RGVVQVM-------------------EGrhcfahLTIEENLLTGAyTRElsrgdis 130
Cdd:PRK15134 340 ---GEIWFDGQPLHNLNRRQLLPvRHRIQVVfqdpnsslnprlnvlqiieEG------LRVHQPTLSAA-QRE------- 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 131 ialERVYQYF------PRLKQRRGSQagyTSGGEQQMTAIGRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQREG 204
Cdd:PRK15134 403 ---QQVIAVMeevgldPETRHRYPAE---FSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQ 476
|
....*
gi 695928685 205 VSFLL 209
Cdd:PRK15134 477 LAYLF 481
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
9-197 |
9.73e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 52.99 E-value: 9.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 9 PSKVLLDVNGIEVIYNHV-ILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGErGDVTKGYIQYRDERIERLS 87
Cdd:TIGR01271 1213 PSGGQMDVQGLTAKYTEAgRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWR 1291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 88 PAELVKRGVVQVMEGrhcfahlTIEENLltGAYTR----ELSRGDISIALERVYQYFPRLKQRRGSQAGYT-SGGEQQMT 162
Cdd:TIGR01271 1292 KAFGVIPQKVFIFSG-------TFRKNL--DPYEQwsdeEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVlSNGHKQLM 1362
|
170 180 190
....*....|....*....|....*....|....*
gi 695928685 163 AIGRALMASPNMILLDEPSMGLAPQiveeIFEIVR 197
Cdd:TIGR01271 1363 CLARSILSKAKILLLDEPSAHLDPV----TLQIIR 1393
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
28-241 |
1.06e-07 |
|
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: 51.33 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 28 LVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDV-TKGYiqyrdeRIERLSPAELVKR-GVVqvmegrhc 105
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVlVDGH------DLALADPAWLRRQvGVV-------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 106 fahltIEENLLTGAYTRE-LSRGDISIALERVyQYFPRL--------------KQRRGSQAGYTSGGEQQMTAIGRALMA 170
Cdd:cd03252 82 -----LQENVLFNRSIRDnIALADPGMSMERV-IEAAKLagahdfiselpegyDTIVGEQGAGLSGGQRQRIAIARALIH 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695928685 171 SPNMILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTniaLRYADYGYILENGRVMMDGAASDL 241
Cdd:cd03252 156 NPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLST---VKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
28-197 |
1.15e-07 |
|
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: 51.34 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 28 LVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLkgergDVTKGYIQYRDERIERLSPAELVKR-GVV----QVMEG 102
Cdd:cd03244 18 PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLV-----ELSSGSILIDGVDISKIGLHDLRSRiSIIpqdpVLFSG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 103 rhcfahlTIEENL-LTGAYTRElsrgDISIALERVyqyfpRLKQRRGSQAGYT-----------SGGEQQMTAIGRALMA 170
Cdd:cd03244 93 -------TIRSNLdPFGEYSDE----ELWQALERV-----GLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALLR 156
|
170 180
....*....|....*....|....*..
gi 695928685 171 SPNMILLDEPSMGLAPQIVEEIFEIVR 197
Cdd:cd03244 157 KSKILVLDEATASVDPETDALIQKTIR 183
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
29-231 |
1.24e-07 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 50.93 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAvsnLLkGErgdvtkgyiqyrderIERLSpaelvkrGVVQVmEGRHCFA- 107
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSA---LL-GE---------------LEKLS-------GSVSV-PGSIAYVs 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 108 ------HLTIEENLLTGAYTRElSRGDISI---ALERVYQYFPRLKQRRGSQAGYT-SGGEQQMTAIGRALMASPNMILL 177
Cdd:cd03250 73 qepwiqNGTIRENILFGKPFDE-ERYEKVIkacALEPDLEILPDGDLTEIGEKGINlSGGQKQRISLARAVYSDADIYLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 695928685 178 DEPSMGLAPQIVEEIFE--IVRDLnqREGVSFLLAEQNTNIaLRYADYGYILENGR 231
Cdd:cd03250 152 DDPLSAVDAHVGRHIFEncILGLL--LNNKTRILVTHQLQL-LPHADQIVVLDNGR 204
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
29-184 |
1.34e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 52.19 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGergDVTKGYIQYRDERierlsPAELVKRGVVQVMEGRHCFAH 108
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQG---NNFTGTILANNRK-----PTKQILKRTGFVTQDDILYPH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 109 LTIEENLLTGAYTR---ELSRGDISIALERVYQYFPrLKQRRGSQAGYT-----SGGEQQMTAIGRALMASPNMILLDEP 180
Cdd:PLN03211 155 LTVRETLVFCSLLRlpkSLTKQEKILVAESVISELG-LTKCENTIIGNSfirgiSGGERKRVSIAHEMLINPSLLILDEP 233
|
....
gi 695928685 181 SMGL 184
Cdd:PLN03211 234 TSGL 237
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
30-202 |
1.70e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.04 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 30 LKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDvtkgyIQYRDERIERLSPAELVKRGVVQVMEGRHCFAHL 109
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGS-----ILFQGKEIDFKSSKEALENGISMVHQELNLVLQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 110 TIEENLLTGAYTRE--------LSRGDISIALERVYQYFPRLKqrrgsqAGYTSGGEQQMTAIGRALMASPNMILLDEPS 181
Cdd:PRK10982 89 SVMDNMWLGRYPTKgmfvdqdkMYRDTKAIFDELDIDIDPRAK------VATLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
170 180
....*....|....*....|.
gi 695928685 182 MGLAPQIVEEIFEIVRDLNQR 202
Cdd:PRK10982 163 SSLTEKEVNHLFTIIRKLKER 183
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
27-198 |
1.75e-07 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 50.79 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 27 ILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVtkgYIQYRDERIERLSPAELVKRGVVQVMEGRHCF 106
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV---HWSNKNESEPSFEATRSRNRYSVAYAAQKPWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 107 AHLTIEENLLTGA-YTRELSRGDI-SIALERVYQYFPRLKQRRGSQAGYT-SGGEQQMTAIGRALMASPNMILLDEP--- 180
Cdd:cd03290 91 LNATVEENITFGSpFNKQRYKAVTdACSLQPDIDLLPFGDQTEIGERGINlSGGQRQRICVARALYQNTNIVFLDDPfsa 170
|
170 180
....*....|....*....|
gi 695928685 181 -SMGLAPQIVEE-IFEIVRD 198
Cdd:cd03290 171 lDIHLSDHLMQEgILKFLQD 190
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
29-199 |
1.99e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.03 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSnllkgERgdVTKGYIQY---------RDERIERLSpaelvkrGVVQv 99
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLA-----ER--VTTGVITGgdrlvngrpLDSSFQRSI-------GYVQ- 842
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 100 MEGRHcFAHLTIEENLLTGAYTRELSRGDISIALERVYQYFPRLKQRRGSQA--GYTSGG---EQQMTA-IGRALMASPN 173
Cdd:TIGR00956 843 QQDLH-LPTSTVRESLRFSAYLRQPKSVSKSEKMEYVEEVIKLLEMESYADAvvGVPGEGlnvEQRKRLtIGVELVAKPK 921
|
170 180
....*....|....*....|....*..
gi 695928685 174 MIL-LDEPSMGLAPQIVEEIFEIVRDL 199
Cdd:TIGR00956 922 LLLfLDEPTSGLDSQTAWSICKLMRKL 948
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
25-269 |
3.51e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 51.45 E-value: 3.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 25 HVILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVT-KGYIQYrderierlSPAelvkrgVVQVMEGr 103
Cdd:TIGR01271 437 YVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKhSGRISF--------SPQ------TSWIMPG- 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 104 hcfahlTIEENLLTGAYTRELSRGDISIA--LERVYQYFPRLKQRRGSQAGYT-SGGEQQMTAIGRALMASPNMILLDEP 180
Cdd:TIGR01271 502 ------TIKDNIIFGLSYDEYRYTSVIKAcqLEEDIALFPEKDKTVLGEGGITlSGGQRARISLARAVYKDADLYLLDSP 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 181 SMGLAPQIVEEIFEivrdlnqrEGVSFLLAEQnTNIA-------LRYADYGYILENGRVMMDGAASDL-AQNEDVKEFYL 252
Cdd:TIGR01271 576 FTHLDVVTEKEIFE--------SCLCKLMSNK-TRILvtsklehLKKADKILLLHEGVCYFYGTFSELqAKRPDFSSLLL 646
|
250 260
....*....|....*....|...
gi 695928685 253 G------ISSGERKSFRDQKFYR 269
Cdd:TIGR01271 647 GleafdnFSAERRNSILTETLRR 669
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
37-213 |
3.92e-07 |
|
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: 51.17 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 37 VPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTKGyiqyrderierlspAELVKRGVVQVMEGRHCFAHLTIEENLL 116
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVA--------------GKSILTNISDVHQNMGYCPQFDAIDDLL 2027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 117 TGA---YTRELSRGDISIALERVYQYFPR---LKQRRGSQAGYTSGGEQQMTAIGRALMASPNMILLDEPSMGLAPQIVE 190
Cdd:TIGR01257 2028 TGRehlYLYARLRGVPAEEIEKVANWSIQslgLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARR 2107
|
170 180
....*....|....*....|...
gi 695928685 191 EIFEIVRDLnQREGVSFLLAEQN 213
Cdd:TIGR01257 2108 MLWNTIVSI-IREGRAVVLTSHS 2129
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
29-210 |
4.28e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 49.57 E-value: 4.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGdvtkgyiqyrderierlspaelvkRGVVQVMEGrHCFAH 108
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPV------------------------AGCVDVPDN-QFGRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 109 LTIEENLltgaytreLSRGDISIALER--------VYQYFPRLKQrrgsqagyTSGGEQQMTAIGRALMASPNMILLDEP 180
Cdd:COG2401 100 ASLIDAI--------GRKGDFKDAVELlnavglsdAVLWLRRFKE--------LSTGQKFRFRLALLLAERPKLLVIDEF 163
|
170 180 190
....*....|....*....|....*....|
gi 695928685 181 SMGLAPQIVEEIFEIVRDLNQREGVSFLLA 210
Cdd:COG2401 164 CSHLDRQTAKRVARNLQKLARRAGITLVVA 193
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
12-181 |
6.93e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 49.93 E-value: 6.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 12 VLLDVNGIEVIYNHVILVlKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTKG---YIQYRDERIERLSP 88
Cdd:TIGR03719 321 KVIEAENLTKAFGDKLLI-DDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGetvKLAYVDQSRDALDP 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 89 aelvKRGVVQVMEGRHcfahltieENLLTGAYTRElSRgdisialervyQYFPRLKQRRGSQ---AGYTSGGEQQMTAIG 165
Cdd:TIGR03719 400 ----NKTVWEEISGGL--------DIIKLGKREIP-SR-----------AYVGRFNFKGSDQqkkVGQLSGGERNRVHLA 455
|
170
....*....|....*.
gi 695928685 166 RALMASPNMILLDEPS 181
Cdd:TIGR03719 456 KTLKSGGNVLLLDEPT 471
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
30-194 |
9.18e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 49.97 E-value: 9.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 30 LKGVSLRVPEGKIVALLGANGAGKTTTLRAvsnlLKGErgdvtkgyiqyrderierLSPAE---LVKRGVVQVMEGRHCF 106
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISA----MLGE------------------LSHAEtssVVIRGSVAYVPQVSWI 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 107 AHLTIEENLLTGA------YTRELsrgDISiALERVYQYFP-RLKQRRGSQAGYTSGGEQQMTAIGRALMASPNMILLDE 179
Cdd:PLN03232 691 FNATVRENILFGSdfeserYWRAI---DVT-ALQHDLDLLPgRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDD 766
|
170
....*....|....*
gi 695928685 180 PSMGLAPQIVEEIFE 194
Cdd:PLN03232 767 PLSALDAHVAHQVFD 781
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
29-223 |
1.30e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 49.34 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTkGYIQYrderiERLSPAELVK--RG-VVQVMEGRHC 105
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGVE-GVITY-----DGITPEEIKKhyRGdVVYNAETDVH 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 106 FAHLTIEENLLTGAYTRE-------LSRGDISIALERVYQYFPRLKQRRGSQAGY-----TSGGEQQMTAIGRALMASPN 173
Cdd:TIGR00956 150 FPHLTVGETLDFAARCKTpqnrpdgVSREEYAKHIADVYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAK 229
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 695928685 174 MILLDEPSMGL----APQIVEEIFEIVRDLNQREGVSFLLAEQNT-----NIALRYADY 223
Cdd:TIGR00956 230 IQCWDNATRGLdsatALEFIRALKTSANILDTTPLVAIYQCSQDAyelfdKVIVLYEGY 288
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
33-222 |
1.42e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 48.89 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 33 VSLRVPEGKIVALLGANGAGKTTtlraVSNLLKGERgDVTKGYIQYRDERIERLSPAELVKRGVVQVMEGRHC---FAHL 109
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTE----LAETLYGLR-PARGGRIMLNGKEINALSTAQRLARGLVYLPEDRQSsglYLDA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 110 TIEENLLTGAYTRE---LSRGDISIALERVYQYFpRLKQRRGSQAGYT-SGGEQQMTAIGRALMASPNMILLDEPSMGLA 185
Cdd:PRK15439 357 PLAWNVCALTHNRRgfwIKPARENAVLERYRRAL-NIKFNHAEQAARTlSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
170 180 190
....*....|....*....|....*....|....*..
gi 695928685 186 PQIVEEIFEIVRDlnqregvsflLAEQNTNIALRYAD 222
Cdd:PRK15439 436 VSARNDIYQLIRS----------IAAQNVAVLFISSD 462
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
155-223 |
1.45e-06 |
|
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: 47.32 E-value: 1.45e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695928685 155 SGGEQQMTAIGRALMASP--NMILLDEPSMGLAPQIVEEIFEIVRDLNQrEGVSFLLAEQNTNIaLRYADY 223
Cdd:cd03238 89 SGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVIKGLID-LGNTVILIEHNLDV-LSSADW 157
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
155-246 |
2.29e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 48.67 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 155 SGGEQQMTAIGRALMA--SPNMILLDEPSMGLAPQIVEEIFEIVRDLnQREGVSFLLAE---QNTNIALRYADYG--YIL 227
Cdd:PRK00635 478 SGGEQERTALAKHLGAelIGITYILDEPSIGLHPQDTHKLINVIKKL-RDQGNTVLLVEhdeQMISLADRIIDIGpgAGI 556
|
90
....*....|....*....
gi 695928685 228 ENGRVMMDGAASDLAQNED 246
Cdd:PRK00635 557 FGGEVLFNGSPREFLAKSD 575
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
9-245 |
2.30e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.57 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 9 PSKVLLDVNGIEVIYNHVIlvlKGVSLRVPEGKIVALLGANGAGKTTTLRAvsnlLKGERgDVTKGYIQYRDERIERLSP 88
Cdd:PRK10982 246 PGEVILEVRNLTSLRQPSI---RDVSFDLHKGEILGIAGLVGAKRTDIVET----LFGIR-EKSAGTITLHGKKINNHNA 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 89 AELVKRGVVQVMEGRHC---FAHLTIEENLL----------TGAYTRELSRGDISIALERVYQYFPRLKQRRGSqagyTS 155
Cdd:PRK10982 318 NEAINHGFALVTEERRStgiYAYLDIGFNSLisnirnyknkVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIGS----LS 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 156 GGEQQMTAIGRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIaLRYADYGYILENGRVMMD 235
Cdd:PRK10982 394 GGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPEL-LGITDRILVMSNGLVAGI 472
|
250
....*....|
gi 695928685 236 GAASDLAQNE 245
Cdd:PRK10982 473 VDTKTTTQNE 482
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
33-210 |
2.33e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 48.37 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 33 VSLRVPEGKIVALLGANGAGKtttlravSNLLKGERGDV--TKGYIQYRDERIERLSPAELVKRGVVQVMEGRH---CFA 107
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGR-------SELMKLLYGATrrTAGQVYLDGKPIDIRSPRDAIRAGIMLCPEDRKaegIIP 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 108 HLTIEENLLTGAyTRELSRGDISI------ALERVYQYFPRLKQRRGSQA-GYTSGGEQQMTAIGRALMASPNMILLDEP 180
Cdd:PRK11288 345 VHSVADNINISA-RRHHLRAGCLInnrweaENADRFIRSLNIKTPSREQLiMNLSGGNQQKAILGRWLSEDMKVILLDEP 423
|
170 180 190
....*....|....*....|....*....|
gi 695928685 181 SMGLAPQIVEEIFEIVRDLNQReGVSFLLA 210
Cdd:PRK11288 424 TRGIDVGAKHEIYNVIYELAAQ-GVAVLFV 452
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
33-241 |
4.43e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 47.10 E-value: 4.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 33 VSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKgERGDVTKGYIQYRDERIERLSPAE---LVKRGVVQVM-EGRHCFAH 108
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGVTK-DNWRVTADRMRFDDIDLLRLSPRErrkLVGHNVSMIFqEPQSCLDP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 109 LTIEENLLTGAYTRELSRGdisialeRVYQYFpRLKQRRGSQAGYTSG-----------------GEQQMTAIGRALMAS 171
Cdd:PRK15093 105 SERVGRQLMQNIPGWTYKG-------RWWQRF-GWRKRRAIELLHRVGikdhkdamrsfpyelteGECQKVMIAIALANQ 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 172 PNMILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASDL 241
Cdd:PRK15093 177 PRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKEL 246
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
29-246 |
6.27e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 46.32 E-value: 6.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTtlraVSNLLKG-ERGDVTKGYIQYRDERIERLSPAELVKRGV-------VQVM 100
Cdd:PRK09580 16 ILRGLNLEVRPGEVHAIMGPNGSGKST----LSATLAGrEDYEVTGGTVEFKGKDLLELSPEDRAGEGIfmafqypVEIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 101 EGRHCFAHLTIEENLLTGAYTRELSRGDISIALERVYQYF--PRLKQRRGSQAGYtSGGEQQMTAIGRALMASPNMILLD 178
Cdd:PRK09580 92 GVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLkmPEDLLTRSVNVGF-SGGEKKRNDILQMAVLEPELCILD 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695928685 179 EPSMGL---APQIVEEIFEIVRDLNQregvSFLLAEQNTNIaLRY--ADYGYILENGRVMMDGAASDLAQNED 246
Cdd:PRK09580 171 ESDSGLdidALKIVADGVNSLRDGKR----SFIIVTHYQRI-LDYikPDYVHVLYQGRIVKSGDFTLVKQLEE 238
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
25-256 |
7.02e-06 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 46.39 E-value: 7.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 25 HVILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVT-KGYIQYRDErierlspaelvkrgVVQVMEGr 103
Cdd:cd03291 48 VGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKhSGRISFSSQ--------------FSWIMPG- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 104 hcfahlTIEENLLTGAYTRELSRGDISIA--LERVYQYFPRLKQRRGSQAGYT-SGGEQQMTAIGRALMASPNMILLDEP 180
Cdd:cd03291 113 ------TIKENIIFGVSYDEYRYKSVVKAcqLEEDITKFPEKDNTVLGEGGITlSGGQRARISLARAVYKDADLYLLDSP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 181 SMGLAPQIVEEIFEivrdlnqrEGVSFLLAEQnTNI-------ALRYADYGYILENGRVMMDGAASDL-AQNEDVKEFYL 252
Cdd:cd03291 187 FGYLDVFTEKEIFE--------SCVCKLMANK-TRIlvtskmeHLKKADKILILHEGSSYFYGTFSELqSLRPDFSSKLM 257
|
....
gi 695928685 253 GISS 256
Cdd:cd03291 258 GYDT 261
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
29-247 |
7.94e-06 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 47.02 E-value: 7.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTkgyiqYRDERIERLSPAELvKRGVVQVMEGRHCFAH 108
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVL-----LDGVPLVQYDHHYL-HRQVALVGQEPVLFSG 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 109 lTIEENLLTGAYTRELSRGDISIALERVYQYFPRLKQRRGSQAGYT----SGGEQQMTAIGRALMASPNMILLDEPSMGL 184
Cdd:TIGR00958 570 -SVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKgsqlSGGQKQRIAIARALVRKPRVLILDEATSAL 648
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695928685 185 APQIVeeifEIVRDLNQREGVSFLLAEQNTNIAlRYADYGYILENGRVMMDGAASDLAQNEDV 247
Cdd:TIGR00958 649 DAECE----QLLQESRSRASRTVLLIAHRLSTV-ERADQILVLKKGSVVEMGTHKQLMEDQGC 706
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
14-198 |
1.21e-05 |
|
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: 45.10 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 14 LDVNGIEVIYN-HVILVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLkgergDVTKGYIQYRDERIERLsPAELV 92
Cdd:cd03369 7 IEVENLSVRYApDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFL-----EAEEGKIEIDGIDISTI-PLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 93 KRGVVQVMEGRHCFAHlTIEENL-LTGAYTRELSRGDISIalervyqyfprlkqrrgSQAGYT-SGGEQQMTAIGRALMA 170
Cdd:cd03369 81 RSSLTIIPQDPTLFSG-TIRSNLdPFDEYSDEEIYGALRV-----------------SEGGLNlSQGQRQLLCLARALLK 142
|
170 180
....*....|....*....|....*...
gi 695928685 171 SPNMILLDEPSMGLAPQIVEEIFEIVRD 198
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIRE 170
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
29-209 |
1.41e-05 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 45.46 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTKGYIQYRDERIERlspaelvkrGVVQVMEGrhCFAH 108
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER---------GVVFQNEG--LLPW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 109 LTIEENLLTGAYTRELSRGD-ISIALERVYQY-FPRLKQRRGSQagyTSGGEQQMTAIGRALMASPNMILLDEPSMGLAP 186
Cdd:PRK11248 85 RNVQDNVAFGLQLAGVEKMQrLEIAHQMLKKVgLEGAEKRYIWQ---LSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
170 180
....*....|....*....|...
gi 695928685 187 QIVEEIFEIVRDLNQREGVSFLL 209
Cdd:PRK11248 162 FTREQMQTLLLKLWQETGKQVLL 184
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
30-208 |
1.58e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 45.34 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 30 LKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGergdvTKGYIQYRDERIERLSPAEL-VKRGVVQvMEGRHCFAH 108
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETP-----TGGELYYQGQDLLKADPEAQkLLRQKIQ-IVFQNPYGS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 109 L--------TIEENL-----LTGAYTRELSRGdisiALERV------YQYFPRLkqrrgsqagyTSGGEQQMTAIGRALM 169
Cdd:PRK11308 105 LnprkkvgqILEEPLlintsLSAAERREKALA----MMAKVglrpehYDRYPHM----------FSGGQRQRIAIARALM 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 695928685 170 ASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFL 208
Cdd:PRK11308 171 LDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYV 209
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
29-186 |
1.98e-05 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 44.85 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKgergdvTKGYIQYrderierlspaELVKRGVVQVMEGRHCFAH 108
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN------TEGDIQI-----------DGVSWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 109 LTIEENLLTGAYTR-----------ELSRGDISIALERVYQYFPRLKQRRGSQAGYT-SGGEQQMTAIGRALMASPNMIL 176
Cdd:cd03289 82 IPQKVFIFSGTFRKnldpygkwsdeEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVlSHGHKQLMCLARSVLSKAKILL 161
|
170
....*....|
gi 695928685 177 LDEPSMGLAP 186
Cdd:cd03289 162 LDEPSAHLDP 171
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
29-243 |
1.98e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 45.93 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAvsnlLKGERgDVTKGYIqyrderierlspaeLVKRGVVQVMEgRHCFAH 108
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQS----LLSQF-EISEGRV--------------WAERSIAYVPQ-QAWIMN 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 109 LTIEENLLtgaYTRELSRGDISIALeRVYQYFPRLKQ-------RRGSQAGYTSGGEQQMTAIGRALMASPNMILLDEPS 181
Cdd:PTZ00243 735 ATVRGNIL---FFDEEDAARLADAV-RVSQLEADLAQlgggletEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPL 810
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695928685 182 MGL----APQIVEEIFeivrdLNQREGVSFLLAEQNTNIALRyADYGYILENGRVMMDGAASDLAQ 243
Cdd:PTZ00243 811 SALdahvGERVVEECF-----LGALAGKTRVLATHQVHVVPR-ADYVVALGDGRVEFSGSSADFMR 870
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
30-244 |
2.03e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.88 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 30 LKGVSLRVPEGKIVALLGANGAGKTTTLRAVSnllkGErgdvtkgyiqyrderIERLSPAELVKRGVVQVMEGRHCFAHL 109
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAML----GE---------------LPPRSDASVVIRGTVAYVPQVSWIFNA 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 110 TIEENLLTGA------YTRELsrgDISiALERVYQYFPRLKQRRGSQAGYT-SGGEQQMTAIGRALMASPNMILLDEPSM 182
Cdd:PLN03130 694 TVRDNILFGSpfdperYERAI---DVT-ALQHDLDLLPGGDLTEIGERGVNiSGGQKQRVSMARAVYSNSDVYIFDDPLS 769
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 695928685 183 GLAPQIVEEIFE--IVRDLNQREGVsfLLAEQNTniALRYADYGYILENGRVMMDGAASDLAQN 244
Cdd:PLN03130 770 ALDAHVGRQVFDkcIKDELRGKTRV--LVTNQLH--FLSQVDRIILVHEGMIKEEGTYEELSNN 829
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
34-181 |
3.52e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.80 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 34 SLRVP-EGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTKGYiqYRDERIERLSPAELvkrgvvqvmegrhcfahltie 112
Cdd:PRK13409 92 GLPIPkEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEP--SWDEVLKRFRGTEL--------------------- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 113 enlltGAYTRELSRGDISIALERVY-QYFPR---------LKQ--RRGS----------------QAGYTSGGEQQMTAI 164
Cdd:PRK13409 149 -----QNYFKKLYNGEIKVVHKPQYvDLIPKvfkgkvrelLKKvdERGKldevverlglenildrDISELSGGELQRVAI 223
|
170
....*....|....*..
gi 695928685 165 GRALMASPNMILLDEPS 181
Cdd:PRK13409 224 AAALLRDADFYFFDEPT 240
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
29-198 |
5.56e-05 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 44.03 E-value: 5.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGdvtkgyiqyrdeRIERLSPAEL--------VKRGvvqvm 100
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSG------------RIARPAGARVlflpqrpyLPLG----- 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 101 egrhcfahlTIEENLLTGAYTRELSRGDISIALERVYqyFPRLKQRRGSQAGYT---SGGEQQMTAIGRALMASPNMILL 177
Cdd:COG4178 441 ---------TLREALLYPATAEAFSDAELREALEAVG--LGHLAERLDEEADWDqvlSLGEQQRLAFARLLLHKPDWLFL 509
|
170 180
....*....|....*....|.
gi 695928685 178 DEPSMGLAPQIVEEIFEIVRD 198
Cdd:COG4178 510 DEATSALDEENEAALYQLLRE 530
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
33-240 |
6.41e-05 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 43.38 E-value: 6.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 33 VSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGErgdvtkGYIQYRDERIERLSPAELVKR--------GVVQVMegrH 104
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGS------GSIQFAGQPLEAWSAAELARHraylsqqqTPPFAM---P 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 105 CFAHLTieenLLTGAYTRElsrGDISIALERVYQYFpRLKQRRGSQAGYTSGGEQQ---MTA----IGRALMASPNMILL 177
Cdd:PRK03695 86 VFQYLT----LHQPDKTRT---EAVASALNEVAEAL-GLDDKLGRSVNQLSGGEWQrvrLAAvvlqVWPDINPAGQLLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695928685 178 DEPSMGL--APQIVeeIFEIVRDLNQrEGVSFLLAEQNTNIALRYADYGYILENGRVMMDGAASD 240
Cdd:PRK03695 158 DEPMNSLdvAQQAA--LDRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
148-229 |
7.94e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.86 E-value: 7.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 148 GSQAGYTSGGEQQMTAIGRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQREG-VSFLLAEQNTNIalRYADYGYI 226
Cdd:PTZ00265 574 GSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENrITIIIAHRLSTI--RYANTIFV 651
|
...
gi 695928685 227 LEN 229
Cdd:PTZ00265 652 LSN 654
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
34-181 |
8.47e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 43.62 E-value: 8.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 34 SLRVP-EGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTKGyiQYRDERIERLSPAELvkrgvvqvmegrhcFAHLT-I 111
Cdd:COG1245 92 GLPVPkKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEE--PSWDEVLKRFRGTEL--------------QDYFKkL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 112 EENLLTGAY---------------TREL-----SRGDISIALERVyqyfpRLKQRRGSQAGYTSGGEQQMTAIGRALMAS 171
Cdd:COG1245 156 ANGEIKVAHkpqyvdlipkvfkgtVRELlekvdERGKLDELAEKL-----GLENILDRDISELSGGELQRVAIAAALLRD 230
|
170
....*....|
gi 695928685 172 PNMILLDEPS 181
Cdd:COG1245 231 ADFYFFDEPS 240
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
29-180 |
2.70e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.19 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDV------TKGYI-------------------QYRDERI 83
Cdd:PRK15064 334 LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwsenaNIGYYaqdhaydfendltlfdwmsQWRQEGD 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 84 ErlspaELVKRGVVqvmeGRHCFahltieenlltgaytrelSRGDIsialervyqyfprlkqrrGSQAGYTSGGEQQMTA 163
Cdd:PRK15064 414 D-----EQAVRGTL----GRLLF------------------SQDDI------------------KKSVKVLSGGEKGRML 448
|
170
....*....|....*..
gi 695928685 164 IGRALMASPNMILLDEP 180
Cdd:PRK15064 449 FGKLMMQKPNVLVMDEP 465
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
35-180 |
3.30e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 41.86 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 35 LRVPEGKIVALLGANGAGKTTTLRAVSnllkgerGDVT--KGYIQY-RDERIERL----------SPAELVKRGVVQV-- 99
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILN-------GEVLldDGRIIYeQDLIVARLqqdpprnvegTVYDFVAEGIEEQae 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 100 -MEGRHCFAHLT----IEENLltgaytRELSRgdISIALE---------RVYQYFPRLKQRRGSQAGYTSGGEQQMTAIG 165
Cdd:PRK11147 97 yLKRYHDISHLVetdpSEKNL------NELAK--LQEQLDhhnlwqlenRINEVLAQLGLDPDAALSSLSGGWLRKAALG 168
|
170
....*....|....*
gi 695928685 166 RALMASPNMILLDEP 180
Cdd:PRK11147 169 RALVSNPDVLLLDEP 183
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
155-231 |
4.08e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 41.27 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 155 SGGEQQMTAIGRALMASPNMILLDEPSMGLAPQIVEEIFEIVRDLNQREGVSFLL--------AEQNTNIALRYAdyGYI 226
Cdd:PRK11022 155 SGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLithdlalvAEAAHKIIVMYA--GQV 232
|
....*
gi 695928685 227 LENGR 231
Cdd:PRK11022 233 VETGK 237
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
28-199 |
8.26e-04 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 39.06 E-value: 8.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 28 LVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLkgergdvtkgyiQYRDERIERLSPAELVkrgvvqvmegrhcFa 107
Cdd:cd03223 15 VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLW------------PWGSGRIGMPEGEDLL-------------F- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 108 hltieenlltgaytrelsrgdisialerVYQ--YFPR--LKQrrgsQAGYT-----SGGEQQMTAIGRALMASPNMILLD 178
Cdd:cd03223 69 ----------------------------LPQrpYLPLgtLRE----QLIYPwddvlSGGEQQRLAFARLLLHKPKFVFLD 116
|
170 180
....*....|....*....|.
gi 695928685 179 EPSMGLAPQIVEEIFEIVRDL 199
Cdd:cd03223 117 EATSALDEESEDRLYQLLKEL 137
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
29-180 |
1.19e-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: 39.92 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLR-VPEGKIvALLGANGAGKTTTLRAVSNLLK---GE---RGDVTKGYIQYRDErierLSPAELVkRGVVqvME 101
Cdd:TIGR03719 20 ILKDISLSfFPGAKI-GVLGLNGAGKSTLLRIMAGVDKdfnGEarpQPGIKVGYLPQEPQ----LDPTKTV-RENV--EE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 102 GRHCFAHLTIEENLLTGAYTRELSRGDISIALErvyqyfPRLKQRRGSQAGYT------------------------SGG 157
Cdd:TIGR03719 92 GVAEIKDALDRFNEISAKYAEPDADFDKLAAEQ------AELQEIIDAADAWDldsqleiamdalrcppwdadvtklSGG 165
|
170 180
....*....|....*....|...
gi 695928685 158 EQQMTAIGRALMASPNMILLDEP 180
Cdd:TIGR03719 166 ERRRVALCRLLLSKPDMLLLDEP 188
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
8-184 |
1.23e-03 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 39.52 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 8 PPSKVLLDVNGIEVIYNHVIlVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTkgYIQyRDER---IE 84
Cdd:PRK11701 1 MMDQPLLSVRGLTKLYGPRK-GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVH--YRM-RDGQlrdLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 85 RLSPAE--LVKR---GVVQ--VMEG--RHCFAHLTIEENLL-TGA--YtrelsrGDI-SIA---LERVYQYFPRLKQRRG 148
Cdd:PRK11701 77 ALSEAErrRLLRtewGFVHqhPRDGlrMQVSAGGNIGERLMaVGArhY------GDIrATAgdwLERVEIDAARIDDLPT 150
|
170 180 190
....*....|....*....|....*....|....*.
gi 695928685 149 SqagyTSGGEQQMTAIGRALMASPNMILLDEPSMGL 184
Cdd:PRK11701 151 T----FSGGMQQRLQIARNLVTHPRLVFMDEPTGGL 182
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
40-71 |
1.58e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 38.12 E-value: 1.58e-03
10 20 30
....*....|....*....|....*....|..
gi 695928685 40 GKIVALLGANGAGKTTTLRAVSNLLKGERGDV 71
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGV 33
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
151-260 |
1.66e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.61 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 151 AGYTSGGEQQ----MTAIGRALMASpnMILLDEPSMGLAPQIVEEIFEIVRDLnQREGVSFLLAEQNTNiALRYADY--- 223
Cdd:TIGR00630 486 AGTLSGGEAQrirlATQIGSGLTGV--LYVLDEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEHDED-TIRAADYvid 561
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 695928685 224 ---GYILENGRVMMDGAASDLAQNED-VKEFYLgisSGERK 260
Cdd:TIGR00630 562 igpGAGEHGGEVVASGTPEEILANPDsLTGQYL---SGRKK 599
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
29-257 |
1.76e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 39.96 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 29 VLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTkgyiqYRDERIERLSPAELvkRGVVQVMEGRHCFAH 108
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIM-----IDDCDVAKFGLTDL--RRVLSIIPQSPVLFS 1323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 109 LTIEENLLTGAytrELSRGDISIALERVYQYFPRLKQRRGSQAGYTSGGE------QQMTAIGRALMASPNMILLDEPSM 182
Cdd:PLN03232 1324 GTVRFNIDPFS---EHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGEnfsvgqRQLLSLARALLRRSKILVLDEATA 1400
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695928685 183 GLAPQIVEEIFEIVRDlnQREGVSFLLAEQNTNIALRyADYGYILENGRVMMDGAASDLAQNEDVKEFYLGISSG 257
Cdd:PLN03232 1401 SVDVRTDSLIQRTIRE--EFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHSTG 1472
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
28-80 |
1.99e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 39.33 E-value: 1.99e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 695928685 28 LVLKGVSLRVPEGKIVALLGANGAGKTTTLRAVSNLLKGERGDVTKG------YI-QYRD 80
Cdd:PRK11819 338 LLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGetvklaYVdQSRD 397
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
30-66 |
2.77e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 39.10 E-value: 2.77e-03
10 20 30
....*....|....*....|....*....|....*..
gi 695928685 30 LKGVSLRVPEGKIVALLGANGAGKTTtlraVSNLLKG 66
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKST----LSNLIAG 72
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
33-64 |
4.93e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 38.18 E-value: 4.93e-03
10 20 30
....*....|....*....|....*....|..
gi 695928685 33 VSLRVPEGKIVALLGANGAGKTTTLRAVSNLL 64
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLL 316
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
30-55 |
5.53e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 37.85 E-value: 5.53e-03
10 20
....*....|....*....|....*.
gi 695928685 30 LKGVSLRVPEGKIVALLGANGAGKTT 55
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKST 42
|
|
| |
