|
Name |
Accession |
Description |
Interval |
E-value |
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
6-240 |
1.71e-135 |
|
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: 380.48 E-value: 1.71e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 6 EILLKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQGL 85
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 86 VMVPEGRGTFTRMTITENLLMGAYIRDDKAQIEADIERIFGIFPRLKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLL 165
Cdd:COG0410 81 GYVPEGRRIFPSLTVEENLLLGAYARRDRAEVRADLERVYELFPRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032805432 166 DEPSMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLNDPKVRAAYLG 240
Cdd:COG0410 161 DEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEVREAYLG 235
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
9-231 |
3.53e-114 |
|
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: 325.93 E-value: 3.53e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQGLVMV 88
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 89 PEGRGTFTRMTITENLLMGAYIRDDKAqIEADIERIFGIFPRLKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLLDEP 168
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRRAK-RKARLERVYELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032805432 169 SMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLND 231
Cdd:cd03224 160 SEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
7-240 |
2.18e-81 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 243.63 E-value: 2.18e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 7 ILLKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQGLV 86
Cdd:PRK11614 4 VMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 87 MVPEGRGTFTRMTITENLLMGAYIRDdKAQIEADIERIFGIFPRLKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLLD 166
Cdd:PRK11614 84 IVPEGRRVFSRMTVEENLAMGGFFAE-RDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032805432 167 EPSMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLNDPKVRAAYLG 240
Cdd:PRK11614 163 EPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAYLG 236
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
6-241 |
2.16e-62 |
|
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: 195.64 E-value: 2.16e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 6 EILLKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQGL 85
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 86 vmvpeGR-----GTFTRMTITENLLMGAYI----------------RDDKAQIEADIERIFGIFpRLKERRNQLAGTMSG 144
Cdd:COG0411 82 -----ARtfqnpRLFPELTVLENVLVAAHArlgrgllaallrlpraRREEREARERAEELLERV-GLADRADEPAGNLSY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 145 GEQQMLAMGRALMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIH-SQGVTVLLVEQNASRALQLASRGYVMESGLITMTG 223
Cdd:COG0411 156 GQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRdERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEG 235
|
250
....*....|....*...
gi 2032805432 224 EGKTLLNDPKVRAAYLGE 241
Cdd:COG0411 236 TPAEVRADPRVIEAYLGE 253
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
9-234 |
1.37e-58 |
|
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: 185.33 E-value: 1.37e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQGLVM- 87
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 88 --VPEgrgTFTRMTITENLLMGAYIR-----------DDKAQIEADIERIFGIFpRLKERRNQLAGTMSGGEQQMLAMGR 154
Cdd:cd03219 81 fqIPR---LFPELTVLENVMVAAQARtgsglllararREEREARERAEELLERV-GLADLADRPAGELSYGQQRRLEIAR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 155 ALMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLNDPKV 234
Cdd:cd03219 157 ALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPRV 236
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
9-217 |
2.30e-52 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 169.47 E-value: 2.30e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAwdLVKQGLVMV 88
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPA--EVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 89 PEGRGTFTRMTITENL-LMGAYIRDDKAQIEADIERIFGIFpRLKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLLDE 167
Cdd:COG1131 79 PQEPALYPDLTVRENLrFFARLYGLPRKEARERIDELLELF-GLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2032805432 168 PSMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESG 217
Cdd:COG1131 158 PTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKG 207
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
9-240 |
1.11e-46 |
|
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: 154.62 E-value: 1.11e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQGLVMV 88
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 89 PEGRGTFTRMTITENLLMGAYIR-DDKAQIEADIERIFGIFpRLKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLLDE 167
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRgLSKKEREEKLEELLEEF-HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032805432 168 PSMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLNDPKVRAAYLG 240
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKVYLG 232
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
8-241 |
3.61e-46 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 153.99 E-value: 3.61e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 8 LLKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQGLVM 87
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 88 VPEGRGTFTRMTITENLLMG-----------------AYIRDDKAQIEAD---IERIfgifpRLKERRNQLAGTMSGGEQ 147
Cdd:PRK11300 85 TFQHVRLFREMTVIENLLVAqhqqlktglfsgllktpAFRRAESEALDRAatwLERV-----GLLEHANRQAGNLAYGQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 148 QMLAMGRALMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQ-GVTVLLVEQNASRALQLASRGYVMESGLITMTGEGK 226
Cdd:PRK11300 160 RRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPE 239
|
250
....*....|....*
gi 2032805432 227 TLLNDPKVRAAYLGE 241
Cdd:PRK11300 240 EIRNNPDVIKAYLGE 254
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
9-241 |
7.66e-46 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 152.88 E-value: 7.66e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQGLVMV 88
Cdd:COG1137 4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 89 PEGRGTFTRMTITENLLMGAYIRD-DKAQIEADIERIFGIFpRLKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLLDE 167
Cdd:COG1137 84 PQEASIFRKLTVEDNILAVLELRKlSKKEREERLEELLEEF-GITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032805432 168 PSMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLNDPKVRAAYLGE 241
Cdd:COG1137 163 PFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPLVRKVYLGE 236
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
9-241 |
3.56e-45 |
|
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: 150.89 E-value: 3.56e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQGLVMV 88
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLGIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 89 PEGRGTFTRMTITENLLMGAYIRDD--KAQIEADIERIFGIFpRLKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLLD 166
Cdd:TIGR04406 82 PQEASIFRKLTVEENIMAVLEIRKDldRAEREERLEALLEEF-QISHLRDNKAMSLSGGERRRVEIARALATNPKFILLD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032805432 167 EPSMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLNDPKVRAAYLGE 241
Cdd:TIGR04406 161 EPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVRRVYLGE 235
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
8-217 |
8.55e-42 |
|
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: 142.30 E-value: 8.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 8 LLKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQgaWDLVKQGLVM 87
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKE--PREARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 88 VPEGRGTFTRMTITENLLMGAYIRD-DKAQIEADIERIFGIFpRLKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLLD 166
Cdd:COG4555 79 LPDERGLYDRLTVRENIRYFAELYGlFDEELKKRIEELIELL-GLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2032805432 167 EPSMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESG 217
Cdd:COG4555 158 EPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKG 208
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-238 |
1.68e-41 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 141.77 E-value: 1.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 4 SKEILLKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQG------- 76
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARrrigyvp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 77 ------------AWDLVKQGLVmvpEGRGTFTRMTitenllmgayiRDDKAQIEADIERIfgifpRLKERRNQLAGTMSG 144
Cdd:COG1121 82 qraevdwdfpitVRDVVLMGRY---GRRGLFRRPS-----------RADREAVDEALERV-----GLEDLADRPIGELSG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 145 GEQQ--MLAmgRALMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESGLITMt 222
Cdd:COG1121 143 GQQQrvLLA--RALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAH- 219
|
250
....*....|....*.
gi 2032805432 223 GEGKTLLNDPKVRAAY 238
Cdd:COG1121 220 GPPEEVLTPENLSRAY 235
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
9-219 |
1.01e-40 |
|
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: 137.53 E-value: 1.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAwdLVKQGLVMV 88
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPE--EVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 89 PEGRGTFTRMTITENLlmgayirddkaqieadierifgifprlkerrnqlagTMSGGEQQMLAMGRALMTRPKVLLLDEP 168
Cdd:cd03230 79 PEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEP 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2032805432 169 SMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESGLI 219
Cdd:cd03230 123 TSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
9-223 |
2.94e-40 |
|
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: 137.65 E-value: 2.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWdlvKQGLVMV 88
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE---RRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 89 PEGRGTFTRMTITENLLMGAYIR-DDKAQIEADIERI---FGIFPRLKERRNQLagtmSGGEQQMLAMGRALMTRPKVLL 164
Cdd:cd03259 78 FQDYALFPHLTVAENIAFGLKLRgVPKAEIRARVRELlelVGLEGLLNRYPHEL----SGGQQQRVALARALAREPSLLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 165 LDEPSMGLSPIMVDKIFEVVNDIH-SQGVTVLLVEQNASRALQLASRGYVMESGLITMTG 223
Cdd:cd03259 154 LDEPLSALDAKLREELREELKELQrELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
9-219 |
2.51e-39 |
|
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: 135.35 E-value: 2.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQG-AWDLVKQGLVM 87
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKkNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 88 VPEGRGTFTRMTITENLLMGAYIRDDKAQIEADiERIFGIFPR--LKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLL 165
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVKGMSKAEAE-ERALELLEKvgLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2032805432 166 DEPSMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESGLI 219
Cdd:cd03262 160 DEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
9-233 |
6.29e-39 |
|
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: 134.77 E-value: 6.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAY-GGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQ-GLV 86
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKvGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 87 mvpegrgtFT-------RMTITENLLMG-AYIRDDKAQIEADIERIFGIFpRLKERRNQLAGTMSGGEQQMLAMGRALMT 158
Cdd:COG1122 81 --------FQnpddqlfAPTVEEDVAFGpENLGLPREEIRERVEEALELV-GLEHLADRPPHELSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032805432 159 RPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLNDPK 233
Cdd:COG1122 152 EPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
8-233 |
2.10e-38 |
|
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: 133.78 E-value: 2.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 8 LLKVSGLKVAYG----GIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGqgAWDLVKQ 83
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTR--RRRKAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 84 GLV-MVP-EGRGTFT-RMTITENL---LMGAYIRDDKAQIEADIERIfGIFPRLKERR-NQLagtmSGGEQQMLAMGRAL 156
Cdd:COG1124 79 RRVqMVFqDPYASLHpRHTVDRILaepLRIHGLPDREERIAELLEQV-GLPPSFLDRYpHQL----SGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2032805432 157 MTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQ-GVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLNDPK 233
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPK 231
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
24-168 |
2.82e-38 |
|
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: 130.46 E-value: 2.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 24 VKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGaWDLVKQGLVMVPEGRGTFTRMTITEN 103
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDE-RKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 104 LLMGAYI-----RDDKAQIEADIERiFGIFPRLKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLLDEP 168
Cdd:pfam00005 80 LRLGLLLkglskREKDARAEEALEK-LGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
10-217 |
5.08e-38 |
|
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: 131.82 E-value: 5.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 10 KVSGLKVAYGG--IQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQ-GLV 86
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKvGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 87 MV-PEGRgtFTRMTITENLLMGAYIR-DDKAQIEADIERIFGIFpRLKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLL 164
Cdd:cd03225 81 FQnPDDQ--FFGPTVEEEVAFGLENLgLPEEEIEERVEEALELV-GLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2032805432 165 LDEPSMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESG 217
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
8-238 |
5.31e-38 |
|
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: 132.86 E-value: 5.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 8 LLKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQgLVM 87
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARR-IAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 88 VPEGRGTFTRMTITENLLMGAYI---------RDDKAQIEADIERiFGIFPrLKERRnqlAGTMSGGEQQMLAMGRALMT 158
Cdd:COG1120 80 VPQEPPAPFGLTVRELVALGRYPhlglfgrpsAEDREAVEEALER-TGLEH-LADRP---VDELSGGERQRVLIARALAQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 159 RPKVLLLDEPSMGLspimvD-----KIFEVVNDI-HSQGVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLNDP 232
Cdd:COG1120 155 EPPLLLLDEPTSHL-----DlahqlEVLELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPE 229
|
....*.
gi 2032805432 233 KVRAAY 238
Cdd:COG1120 230 LLEEVY 235
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-241 |
6.09e-38 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 132.55 E-value: 6.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 1 MADSKEILLKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDL 80
Cdd:COG4674 3 LDTMHGPILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 81 VKQGLvmvpeGR-----GTFTRMTITENLLMgAYIRD--------------DKAQIEADIERIfgifpRLKERRNQLAGT 141
Cdd:COG4674 83 ARLGI-----GRkfqkpTVFEELTVFENLEL-ALKGDrgvfaslfarltaeERDRIEEVLETI-----GLTDKADRLAGL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 142 MSGGEQQMLAMGRALMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIhSQGVTVLLVEQNASRALQLASRGYVMESGLITM 221
Cdd:COG4674 152 LSHGQKQWLEIGMLLAQDPKLLLLDEPVAGMTDAETERTAELLKSL-AGKHSVVVVEHDMEFVRQIARKVTVLHQGSVLA 230
|
250 260
....*....|....*....|
gi 2032805432 222 TGEGKTLLNDPKVRAAYLGE 241
Cdd:COG4674 231 EGSLDEVQADPRVIEVYLGR 250
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
6-197 |
3.85e-37 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 135.92 E-value: 3.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 6 EILLKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQGL 85
Cdd:COG1129 2 EPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 86 VMVPEGRGTFTRMTITENLLMGAYIRD----DKAQIEADIERIFGifpRLKERRN--QLAGTMSGGEQQMLAMGRALMTR 159
Cdd:COG1129 82 AIIHQELNLVPNLSVAENIFLGREPRRggliDWRAMRRRARELLA---RLGLDIDpdTPVGDLSVAQQQLVEIARALSRD 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 2032805432 160 PKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQGVTVLLV 197
Cdd:COG1129 159 ARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYI 196
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
9-240 |
1.52e-36 |
|
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: 128.51 E-value: 1.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWdlvKQGLVMV 88
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH---KRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 89 PEGRGTFTRMTITENLLMGAYIRD-DKAQIEADIERIFGIFpRLKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLLDE 167
Cdd:cd03300 78 FQNYALFPHLTVFENIAFGLRLKKlPKAEIKERVAEALDLV-QLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2032805432 168 PSMGLSPIMVDKIFEVVNDIHSQ-GVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLNDPKVR--AAYLG 240
Cdd:cd03300 157 PLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRfvADFIG 232
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
10-217 |
7.01e-36 |
|
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: 124.66 E-value: 7.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 10 KVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLkGQGAWDLVKQGLVMVP 89
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDI-AKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 90 egrgtftrmtitenllmgayirddkaqieadierifgifprlkerrnQLagtmSGGEQQMLAMGRALMTRPKVLLLDEPS 169
Cdd:cd00267 80 -----------------------------------------------QL----SGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2032805432 170 MGLSPIMVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESG 217
Cdd:cd00267 109 SGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-233 |
1.04e-35 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 132.33 E-value: 1.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 1 MADSKEILLKVSGLKVAY-----GGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQ 75
Cdd:COG1123 253 AAAAAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 76 GAWDLVKQG--LVMV---PEGrGTFTRMTITENLLMGAYIRD--DKAQIEADIERI---FGIFPRLKERRnqlAGTMSGG 145
Cdd:COG1123 333 SRRSLRELRrrVQMVfqdPYS-SLNPRMTVGDIIAEPLRLHGllSRAERRERVAELlerVGLPPDLADRY---PHELSGG 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 146 EQQMLAMGRALMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQ-GVTVLLVEQNASRALQLASRGYVMESGLITMTGE 224
Cdd:COG1123 409 QRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGP 488
|
....*....
gi 2032805432 225 GKTLLNDPK 233
Cdd:COG1123 489 TEEVFANPQ 497
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
8-241 |
1.19e-35 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 126.55 E-value: 1.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 8 LLKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQGLVM 87
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 88 VPEGRGTFTRMTITENLLMGAYIRDD--KAQIEADIERIFGIFpRLKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLL 165
Cdd:PRK10895 83 LPQEASIFRRLSVYDNLMAVLQIRDDlsAEQREDRANELMEEF-HIEHLRDSMGQSLSGGERRRVEIARALAANPKFILL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2032805432 166 DEPSMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLNDPKVRAAYLGE 241
Cdd:PRK10895 162 DEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYLGE 237
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
9-222 |
1.71e-35 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 123.69 E-value: 1.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQGLVMV 88
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 89 PegrgtftrmtitenllmgayirddkaqieadierifgifprlkerrnQLagtmSGGEQQMLAMGRALMTRPKVLLLDEP 168
Cdd:cd03216 81 Y-----------------------------------------------QL----SVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2032805432 169 SMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESGLITMT 222
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
9-219 |
2.70e-35 |
|
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: 124.91 E-value: 2.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGG----IQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVK-- 82
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAfr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 83 --------QGLVMVPegrgtftRMTITENLLMGAYIR-DDKAQIEADIERIFGIFpRLKERRNQLAGTMSGGEQQMLAMG 153
Cdd:cd03255 81 rrhigfvfQSFNLLP-------DLTALENVELPLLLAgVPKKERRERAEELLERV-GLGDRLNHYPSELSGGQQQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032805432 154 RALMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQ-GVTVLLVEQNAsRALQLASRGYVMESGLI 219
Cdd:cd03255 153 RALANDPKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
9-217 |
2.86e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 124.54 E-value: 2.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQgLVMV 88
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQ-VAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 89 PEgRGTFTRMTITENLLMGAYIRD---DKAQIEADIERiFGIFPRLKERRnqlAGTMSGGEQQMLAMGRALMTRPKVLLL 165
Cdd:COG4619 80 PQ-EPALWGGTVRDNLPFPFQLRErkfDRERALELLER-LGLPPDILDKP---VERLSGGERQRLALIRALLLQPDVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2032805432 166 DEPSMGLSPIMVDKIFEVVND-IHSQGVTVLLVEQNASRALQLASRGYVMESG 217
Cdd:COG4619 155 DEPTSALDPENTRRVEELLREyLAEEGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
10-197 |
5.89e-35 |
|
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: 123.80 E-value: 5.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 10 KVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWdlvkqgLVMVP 89
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR------IGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 90 EgRGTFTR---MTITENLLMGAYI---------RDDKAQIEADIERIfgifpRLKERRNQLAGTMSGGEQQMLAMGRALM 157
Cdd:cd03235 75 Q-RRSIDRdfpISVRDVVLMGLYGhkglfrrlsKADKAKVDEALERV-----GLSELADRQIGELSGGQQQRVLLARALV 148
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2032805432 158 TRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQGVTVLLV 197
Cdd:cd03235 149 QDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVV 188
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
11-223 |
1.15e-34 |
|
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: 123.25 E-value: 1.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 11 VSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGawDLVKQGLVMVPE 90
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP--REVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 91 GRGTFTRMTITENLLMGAYIRDDKAQIEAdiERIFGI--FPRLKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLLDEP 168
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAERR--ERIDELldFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2032805432 169 SMGLSPIMVDKIFEVVNDIH-SQGVTVLLVEQNASRALQLASRGYVMESGLITMTG 223
Cdd:cd03265 159 TIGLDPQTRAHVWEYIEKLKeEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
9-217 |
1.91e-34 |
|
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: 121.53 E-value: 1.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQGLV-M 87
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRIgM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 88 VPEGRGTFTRMTITENLLMGayirddkaqieadierifgifprlkerrnqlagtMSGGEQQMLAMGRALMTRPKVLLLDE 167
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2032805432 168 PSMGLSPIMVDKIFEVVNDIHSQ-GVTVLLVEQNASRALQLASRGYVMESG 217
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
9-197 |
2.25e-34 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 122.39 E-value: 2.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKgqgawDLVKQGLVMV 88
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD-----IAARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 89 PEGRGTFTRMTITENL-----LMGAYIRDDKAQIEADIERiFGIFPRLKERRNQLagtmSGGEQQMLAMGRALMTRPKVL 163
Cdd:cd03269 76 PEERGLYPKMKVIDQLvylaqLKGLKKEEARRRIDEWLER-LELSEYANKRVEEL----SKGNQQKVQFIAAVIHDPELL 150
|
170 180 190
....*....|....*....|....*....|....
gi 2032805432 164 LLDEPSMGLSPIMVDKIFEVVNDIHSQGVTVLLV 197
Cdd:cd03269 151 ILDEPFSGLDPVNVELLKDVIRELARAGKTVILS 184
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
6-220 |
3.19e-34 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 127.83 E-value: 3.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 6 EILLKVSGLKVAyggiQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQGL 85
Cdd:COG1129 254 EVVLEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAGI 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 86 VMVPEGR---GTFTRMTITENLLMGAYIRD------DKAQIEADIERI---FGIFPRlkeRRNQLAGTMSGGEQQMLAMG 153
Cdd:COG1129 330 AYVPEDRkgeGLVLDLSIRENITLASLDRLsrggllDRRRERALAEEYikrLRIKTP---SPEQPVGNLSGGNQQKVVLA 406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032805432 154 RALMTRPKVLLLDEPSMGlspimVD---K--IFEVVNDIHSQGVTVLLV-----EqnasrALQLASRGYVMESGLIT 220
Cdd:COG1129 407 KWLATDPKVLILDEPTRG-----IDvgaKaeIYRLIRELAAEGKAVIVIsselpE-----LLGLSDRILVMREGRIV 473
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
9-216 |
1.46e-33 |
|
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: 120.65 E-value: 1.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGG----IQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAwdlvkqG 84
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP------D 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 85 LVMVPEGRGTFTRMTITENLLMGAYIRD-DKAQIEADIERIFGIFpRLKERRNQLAGTMSGGEQQMLAMGRALMTRPKVL 163
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALGLELQGvPKAEARERAEELLELV-GLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2032805432 164 LLDEPSMGLSPIMVDKIFEVVNDI-HSQGVTVLLVEQNASRALQLASRGYVMES 216
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFLADRVVVLSA 207
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
9-228 |
2.05e-33 |
|
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: 119.92 E-value: 2.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGGIQ--AVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGawDLVKQGLV 86
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDR--KAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 87 MVPEGRGTFTRMTITENLLMGAYIRD-DKAQIEADIERIFGIFpRLKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLL 165
Cdd:cd03263 79 YCPQFDALFDELTVREHLRFYARLKGlPKSEIKEEVELLLRVL-GLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032805432 166 DEPSMGLSPIMVDKIFEVVNDIhSQGVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTL 228
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
8-219 |
2.76e-33 |
|
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: 119.92 E-value: 2.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 8 LLKVSGLKVAY----GGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGK-TLKGQGAWDLVK 82
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 83 QGLV-MVP-EGRGTFT-RMTITENL---LMGAYIRDDKAQIEADIERIFGIFPRLKERRNQLAGTMSGGEQQMLAMGRAL 156
Cdd:cd03257 81 RKEIqMVFqDPMSSLNpRMTIGEQIaepLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032805432 157 MTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQ-GVTVLLVEQNASRALQLASRGYVMESGLI 219
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
9-196 |
3.66e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 121.37 E-value: 3.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLkgqGAWDLVKQGLvmV 88
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL---DPEDRRRIGY--L 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 89 PEGRGTFTRMTITENL-----LMGAYIRDDKAQIEADIERiFGIfprlKERRNQLAGTMSGGEQQMLAMGRALMTRPKVL 163
Cdd:COG4152 77 PEERGLYPKMKVGEQLvylarLKGLSKAEAKRRADEWLER-LGL----GDRANKKVEELSKGNQQKVQLIAALLHDPELL 151
|
170 180 190
....*....|....*....|....*....|...
gi 2032805432 164 LLDEPSMGLSPIMVDKIFEVVNDIHSQGVTVLL 196
Cdd:COG4152 152 ILDEPFSGLDPVNVELLKDVIRELAAKGTTVIF 184
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-237 |
4.61e-33 |
|
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: 125.02 E-value: 4.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 6 EILLKVSGLKVAY--GGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAA---GEIEFMGKTLKGQGAWDL 80
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 81 VKQgLVMVP-EGRGTFTRMTITENLLMGAYIRD-DKAQIEADIERIFGIFpRLKERRNQLAGTMSGGEQQMLAMGRALMT 158
Cdd:COG1123 82 GRR-IGMVFqDPMTQLNPVTVGDQIAEALENLGlSRAEARARVLELLEAV-GLERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 159 RPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQ-GVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLNDPKVRAA 237
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQALAA 239
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-217 |
1.02e-32 |
|
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: 117.15 E-value: 1.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 6 EILLKVSGLKVAYggiqAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQGL 85
Cdd:cd03215 2 EPVLEVRGLSVKG----AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 86 VMVPEGR---GTFTRMTITENLLMGAYirddkaqieadierifgifprlkerrnqlagtMSGGEQQMLAMGRALMTRPKV 162
Cdd:cd03215 78 AYVPEDRkreGLVLDLSVAENIALSSL--------------------------------LSGGNQQKVVLARWLARDPRV 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2032805432 163 LLLDEPSMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESG 217
Cdd:cd03215 126 LILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
8-208 |
1.37e-32 |
|
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: 117.58 E-value: 1.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 8 LLKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGawDLVKQGLVM 87
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR--EDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 88 VPEGRGTFTRMTITENLLMGAYI---RDDKAQIEADIERiFGifprLKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLL 164
Cdd:COG4133 80 LGHADGLKPELTVRENLRFWAALyglRADREAIDEALEA-VG----LAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2032805432 165 LDEPSMGLSPIMVDKIFEVVNDIHSQGVTVLL-----VEQNASRALQLA 208
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAHLARGGAVLLtthqpLELAAARVLDLG 203
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-217 |
1.79e-32 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 118.65 E-value: 1.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 1 MADSkEILLKVSGLKVAY----GGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQG 76
Cdd:COG1116 1 MSAA-APALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 77 AwdlvkqGLVMVPEGRGTFTRMTITENLLMGAYIRD-DKAQIEADIERIFGIFpRLKERRNQLAGTMSGGEQQMLAMGRA 155
Cdd:COG1116 80 P------DRGVVFQEPALLPWLTVLDNVALGLELRGvPKAERRERARELLELV-GLAGFEDAYPHQLSGGMRQRVAIARA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032805432 156 LMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQ-GVTVLLVEQNASRALQLASRGYVMESG 217
Cdd:COG1116 153 LANDPEVLLMDEPFGALDALTRERLQDELLRLWQEtGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
9-238 |
2.27e-32 |
|
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: 118.05 E-value: 2.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYG-GIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDL--VKQGL 85
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 86 VMVPEGRGTFTRMTITENLLMGAYIRDDKAQI------EADIERIFGIFPR--LKERRNQLAGTMSGGEQQMLAMGRALM 157
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRLGRRSTWRSlfglfpKEEKQRALAALERvgLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 158 TRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQ-GVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTlLNDPKVRA 236
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAE-LTDEVLDE 239
|
..
gi 2032805432 237 AY 238
Cdd:cd03256 240 IY 241
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
8-233 |
3.16e-32 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 117.40 E-value: 3.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 8 LLKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGA-WDLVKQGLV 86
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKdINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 87 MVPEGRGTFTRMTITENLLMGAYI--RDDKAQIEAD----IERIfgifpRLKERRNQLAGTMSGGEQQMLAMGRALMTRP 160
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPIKvkKMSKAEAEERamelLERV-----GLADKADAYPAQLSGGQQQRVAIARALAMEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032805432 161 KVLLLDEPSMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLNDPK 233
Cdd:COG1126 156 KVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQ 228
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
9-230 |
3.73e-32 |
|
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: 116.55 E-value: 3.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKtlKGQGAWDLVKQGLVMV 88
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK--SYQKNIEALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 89 pEGRGTFTRMTITENLLMGAYIRDDKaqiEADIERIFGIFpRLKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLLDEP 168
Cdd:cd03268 79 -EAPGFYPNLTARENLRLLARLLGIR---KKRIDEVLDVV-GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032805432 169 SMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRgyvmesglITMTGEGKTLLN 230
Cdd:cd03268 154 TNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADR--------IGIINKGKLIEE 207
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
8-233 |
6.86e-32 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 119.43 E-value: 6.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 8 LLKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGqgawdlvkqglvM 87
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTG------------L 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 88 VPEGRGT---------FTRMTITENLLMGAYIRD-DKAQIEADIERIFGIFpRLKERRNQLAGTMSGGEQQMLAMGRALM 157
Cdd:COG3842 73 PPEKRNVgmvfqdyalFPHLTVAENVAFGLRMRGvPKAEIRARVAELLELV-GLEGLADRYPHQLSGGQQQRVALARALA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 158 TRPKVLLLDEPsmgLSPImvDK------IFEVVnDIHSQ-GVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLN 230
Cdd:COG3842 152 PEPRVLLLDEP---LSAL--DAklreemREELR-RLQRElGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYE 225
|
...
gi 2032805432 231 DPK 233
Cdd:COG3842 226 RPA 228
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
9-217 |
1.83e-31 |
|
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: 115.36 E-value: 1.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGL---QPVA--AGEIEFMGKTLKGQGAWDLV-- 81
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlIPGApdEGEVLLDGKDIYDLDVDVLElr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 82 -KQGLVMvpeGRGTFTRMTITENLLMGAYIRD--DKAQIEADIE---RIFGIFPRLKerRNQLAGTMSGGEQQMLAMGRA 155
Cdd:cd03260 81 rRVGMVF---QKPNPFPGSIYDNVAYGLRLHGikLKEELDERVEealRKAALWDEVK--DRLHALGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032805432 156 LMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQgVTVLLVEQNASRALQLASRGYVMESG 217
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNG 216
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
19-217 |
2.02e-31 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 115.15 E-value: 2.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 19 GGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDL--VKQGLVMVPEGRGTFT 96
Cdd:COG2884 13 GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIpyLRRRIGVVFQDFRLLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 97 RMTITENLLMGAYIRD-DKAQIEADIERIFGIFpRLKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLLDEPSMGLSPI 175
Cdd:COG2884 93 DRTVYENVALPLRVTGkSRKEIRRRVREVLDLV-GLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2032805432 176 MVDKIFEVVNDIHSQGVTVL-------LVEQNASRALQLaSRGYVMESG 217
Cdd:COG2884 172 TSWEIMELLEEINRRGTTVLiathdleLVDRMPKRVLEL-EDGRLVRDE 219
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
6-220 |
4.34e-31 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 114.37 E-value: 4.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 6 EILLKVSGLKVAYG----GIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLV 81
Cdd:COG1136 2 SPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 82 K----------QGLVMVPEgrgtftrMTITENLLMGAYI-----RDDKAQIEADIERiFGifprLKERRNQLAGTMSGGE 146
Cdd:COG1136 82 RlrrrhigfvfQFFNLLPE-------LTALENVALPLLLagvsrKERRERARELLER-VG----LGDRLDHRPSQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032805432 147 QQMLAMGRALMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIH-SQGVTVLLVEQNAsRALQLASRGYVMESGLIT 220
Cdd:COG1136 150 QQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNrELGTTIVMVTHDP-ELAARADRVIRLRDGRIV 223
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
9-233 |
7.87e-31 |
|
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: 113.97 E-value: 7.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGGIQaVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAwdlVKQGLVMV 88
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPP---EKRDISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 89 PEGRGTFTRMTITENLLMGAYIR-DDKAQIEA---DIERIFGIFPRLkerrNQLAGTMSGGEQQMLAMGRALMTRPKVLL 164
Cdd:cd03299 77 PQNYALFPHMTVYKNIAYGLKKRkVDKKEIERkvlEIAEMLGIDHLL----NRKPETLSGGEQQRVAIARALVVNPKILL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 165 LDEPSMGLSPIMVDKIFEVVNDIHSQ-GVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLNDPK 233
Cdd:cd03299 153 LDEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPK 222
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
11-235 |
1.63e-30 |
|
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: 112.98 E-value: 1.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 11 VSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDL--VKQGLVMV 88
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrLRRRMGML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 89 PEGRGTFTRMTITENllMGAYIRDDKAQIEADIERI-------FGifprLKERRNQLAGTMSGGEQQMLAMGRALMTRPK 161
Cdd:cd03261 83 FQSGALFDSLTVFEN--VAFPLREHTRLSEEEIREIvlekleaVG----LRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032805432 162 VLLLDEPSMGLSPIMVDKIFEVVNDIH-SQGVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLN--DPKVR 235
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSLKkELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRAsdDPLVR 233
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-236 |
1.72e-30 |
|
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: 113.15 E-value: 1.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 4 SKEILLKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLkgqgaWDLVKQ 83
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDI-----TGLSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 84 GLVMVPEGRGT-------FTRMTITENLLMGAYIRDDKAqiEADIERI-------FGifprLKERRNQLAGTMSGGEQQM 149
Cdd:COG1127 76 ELYELRRRIGMlfqggalFDSLTVFENVAFPLREHTDLS--EAEIRELvleklelVG----LPGAADKMPSELSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 150 LAMGRALMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQ-GVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTL 228
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL 229
|
250
....*....|
gi 2032805432 229 LN--DPKVRA 236
Cdd:COG1127 230 LAsdDPWVRQ 239
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
19-223 |
2.19e-30 |
|
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: 112.08 E-value: 2.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 19 GGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMG-KTLKGQGAwdlVKQGLVMVPEGRGTFTR 97
Cdd:cd03266 16 KTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfDVVKEPAE---ARRRLGFVSDSTGLYDR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 98 MTITENLLMGAYIRDDK-AQIEADIERIFGIFpRLKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLLDEPSMGLSPIM 176
Cdd:cd03266 93 LTARENLEYFAGLYGLKgDELTARLEELADRL-GMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2032805432 177 VDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESGLITMTG 223
Cdd:cd03266 172 TRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
8-241 |
1.35e-29 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 115.53 E-value: 1.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 8 LLKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQGLVM 87
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 88 VPEGRGTFTRMTITENLLMG-AYIRDDKAQIEAdierifgifpRLKERRNQL-----AGTMSGGEQQMLAMGRALMTRPK 161
Cdd:PRK15439 91 VPQEPLLFPNLSVKENILFGlPKRQASMQKMKQ----------LLAALGCQLdldssAGSLEVADRQIVEILRGLMRDSR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 162 VLLLDEPSMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLND-------PKV 234
Cdd:PRK15439 161 ILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDdiiqaitPAA 240
|
....*..
gi 2032805432 235 RAAYLGE 241
Cdd:PRK15439 241 REKSLSA 247
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
10-223 |
1.61e-29 |
|
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: 108.68 E-value: 1.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 10 KVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQgLVMVP 89
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARK-IAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 90 egrgtftrmtitenllmgayirddkaQIeadIERiFGIFPrLKERRnqlAGTMSGGEQQMLAMGRALMTRPKVLLLDEPS 169
Cdd:cd03214 80 --------------------------QA---LEL-LGLAH-LADRP---FNELSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2032805432 170 MGLSPIMVDKIFEVVNDI-HSQGVTVLLVEQNASRALQLASRGYVMESGLITMTG 223
Cdd:cd03214 126 SHLDIAHQIELLELLRRLaRERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-233 |
2.51e-29 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 112.47 E-value: 2.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 1 MADskeilLKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDl 80
Cdd:COG3839 1 MAS-----LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 81 vkQGLVMVPEGRGTFTRMTITENLLMGAYIRD-DKAQIEADIE---RIFGIFPRLkERRnqlAGTMSGGEQQMLAMGRAL 156
Cdd:COG3839 75 --RNIAMVFQSYALYPHMTVYENIAFPLKLRKvPKAEIDRRVReaaELLGLEDLL-DRK---PKQLSGGQRQRVALGRAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 157 MTRPKVLLLDEPsmgLSPI-------MVDKIFEvvndIHSQ-GVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTL 228
Cdd:COG3839 149 VREPKVFLLDEP---LSNLdaklrveMRAEIKR----LHRRlGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
....*
gi 2032805432 229 LNDPK 233
Cdd:COG3839 222 YDRPA 226
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
18-232 |
2.77e-29 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 109.80 E-value: 2.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 18 YGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWD-LVKQGLVMVPEGRGTFT 96
Cdd:PRK09493 11 FGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErLIRQEAGMVFQQFYLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 97 RMTITENLLMGA-YIRD-DKAQIEADIERIFGIFPrLKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLLDEPSMGLSP 174
Cdd:PRK09493 91 HLTALENVMFGPlRVRGaSKEEAEKQARELLAKVG-LAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2032805432 175 IMVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLNDP 232
Cdd:PRK09493 170 ELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNP 227
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-217 |
6.87e-29 |
|
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: 108.15 E-value: 6.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 27 VDFEVRrGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTlkgqgaWDLVKQGLVMVPEGRGT---------FTR 97
Cdd:cd03297 17 IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTV------LFDSRKKINLPPQQRKIglvfqqyalFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 98 MTITENLLMGAYI---RDDKAQIEADIERiFGIFPRLKERRNQLagtmSGGEQQMLAMGRALMTRPKVLLLDEPSMGLSP 174
Cdd:cd03297 90 LNVRENLAFGLKRkrnREDRISVDELLDL-LGLDHLLNRYPAQL----SGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2032805432 175 IMVDKIFEVVNDIHSQ-GVTVLLVEQNASRALQLASRGYVMESG 217
Cdd:cd03297 165 ALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDG 208
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
9-233 |
1.08e-28 |
|
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: 108.20 E-value: 1.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDlvkQGLVMV 88
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE---RNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 89 PEGRGTFTRMTITENLLMGAYI-----RDDKAQIEADIERIFGiFPRLKERRNQLAGTMSGGEQQMLAMGRALMTRPKVL 163
Cdd:cd03296 80 FQHYALFRHMTVFDNVAFGLRVkprseRPPEAEIRAKVHELLK-LVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032805432 164 LLDEPSMGLSPIMVDKIFEVVNDIHSQ-GVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLNDPK 233
Cdd:cd03296 159 LLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPA 229
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
6-197 |
1.81e-28 |
|
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: 107.86 E-value: 1.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 6 EILLKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTG-LQPVAAGEIEFMGKTLKGQGAWDLVKQ- 83
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRLFGERRGGEDVWELRKRi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 84 GLVMvPEGRGTFTRMTITENLL-------MGAYIRDDKAQIEAdIERIFGIFpRLKERRNQLAGTMSGGEQQMLAMGRAL 156
Cdd:COG1119 81 GLVS-PALQLRFPRDETVLDVVlsgffdsIGLYREPTDEQRER-ARELLELL-GLAHLADRPFGTLSQGEQRRVLIARAL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2032805432 157 MTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQG-VTVLLV 197
Cdd:COG1119 158 VKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLV 199
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
7-217 |
2.80e-28 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 109.54 E-value: 2.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 7 ILLKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAwdLVKQGLV 86
Cdd:PRK13536 40 VAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARAR--LARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 87 MVPEGRGTFTRMTITENLLM-GAYIRDDKAQIEADIERIFGiFPRLKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLL 165
Cdd:PRK13536 118 VVPQFDNLDLEFTVRENLLVfGRYFGMSTREIEAVIPSLLE-FARLESKADARVSDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2032805432 166 DEPSMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESG 217
Cdd:PRK13536 197 DEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAG 248
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-220 |
3.75e-28 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 111.27 E-value: 3.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 2 ADSKEILLKVSGLKVA-YGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDL 80
Cdd:COG3845 251 AEPGEVVLEVENLSVRdDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRER 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 81 VKQGLVMVPE---GRGTFTRMTITENLLMGAYIRD--------DKAQIEADIERI---FGIFPRlkeRRNQLAGTMSGGE 146
Cdd:COG3845 331 RRLGVAYIPEdrlGRGLVPDMSVAENLILGRYRRPpfsrggflDRKAIRAFAEELieeFDVRTP---GPDTPARSLSGGN 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 147 QQMLAMGRALMTRPKVLLLDEPSMGLspimvDkiFEVVNDIHSQ-------GVTVLLVEQNASRALQLASRGYVMESGLI 219
Cdd:COG3845 408 QQKVILARELSRDPKLLIAAQPTRGL-----D--VGAIEFIHQRllelrdaGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
.
gi 2032805432 220 T 220
Cdd:COG3845 481 V 481
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
18-220 |
7.01e-28 |
|
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: 105.42 E-value: 7.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 18 YGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKgqgAWDLVKQ-GLVMVPEGRGTFT 96
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK---AKERRKSiGYVMQDVDYQLFT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 97 RmTITENLLMGAYIRDDKAQIEADIERIFGIFpRLKERRNQlagTMSGGEQQMLAMGRALMTRPKVLLLDEPSMGLSPIM 176
Cdd:cd03226 87 D-SVREELLLGLKELDAGNEQAETVLKDLDLY-ALKERHPL---SLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKN 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2032805432 177 VDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESGLIT 220
Cdd:cd03226 162 MERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
9-217 |
8.24e-28 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 107.58 E-value: 8.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAwdLVKQGLVMV 88
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRAR--HARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 89 PEGRGTFTRMTITENLLM-GAYIRDDKAQIEADIERIFGiFPRLKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLLDE 167
Cdd:PRK13537 86 PQFDNLDPDFTVRENLLVfGRYFGLSAAAARALVPPLLE-FAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2032805432 168 PSMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESG 217
Cdd:PRK13537 165 PTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
9-241 |
1.17e-27 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 107.93 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQgawdlvkqglvMV 88
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTN-----------LP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 89 PEGRGT---------FTRMTITENLLMGAYIRD-DKAQIEADIERIFGIF--PRLKERR-NQLagtmSGGEQQMLAMGRA 155
Cdd:COG1118 72 PRERRVgfvfqhyalFPHMTVAENIAFGLRVRPpSKAEIRARVEELLELVqlEGLADRYpSQL----SGGQRQRVALARA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 156 LMTRPKVLLLDEPsMG-----LSPIMVDKIFEVVNDIHsqgVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLN 230
Cdd:COG1118 148 LAVEPEVLLLDEP-FGaldakVRKELRRWLRRLHDELG---GTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYD 223
|
250
....*....|...
gi 2032805432 231 DPKVRAAY--LGE 241
Cdd:COG1118 224 RPATPFVArfLGC 236
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
19-233 |
2.84e-27 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 104.59 E-value: 2.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 19 GGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVK--QGLVMVPEGRGTFT 96
Cdd:cd03258 16 GKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKarRRIGMIFQHFNLLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 97 RMTITENLlmgAY----IRDDKAQIEADIERIFGiFPRLKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLLDEPSMGL 172
Cdd:cd03258 96 SRTVFENV---ALpleiAGVPKAEIEERVLELLE-LVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSAL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032805432 173 SPIMVDKIFEVVNDIHSQ-GVTVLLV--EQNASRalQLASRGYVMESGLITMTGEGKTLLNDPK 233
Cdd:cd03258 172 DPETTQSILALLRDINRElGLTIVLIthEMEVVK--RICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
8-240 |
3.54e-27 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 107.23 E-value: 3.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 8 LLKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWdlvKQGLVM 87
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPY---QRPINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 88 VPEGRGTFTRMTITENLLMGayIRDDK---AQIEADIERIFGIFpRLKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLL 164
Cdd:PRK11607 96 MFQSYALFPHMTVEQNIAFG--LKQDKlpkAEIASRVNEMLGLV-HMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032805432 165 LDEPSMGLSPIMVDKI-FEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLNDPKVR--AAYLG 240
Cdd:PRK11607 173 LDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRysAEFIG 251
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
9-223 |
2.06e-26 |
|
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: 101.56 E-value: 2.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDlvkQGLVMV 88
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD---RDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 89 PEGRGTFTRMTITENLLMGAYIRD-DKAQIEADIERIFGIFpRLKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLLDE 167
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLKLRKvPKDEIDERVREVAELL-QIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2032805432 168 PSMGL-SPIMVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESGLITMTG 223
Cdd:cd03301 157 PLSNLdAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
23-219 |
2.43e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 102.86 E-value: 2.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 23 AVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKtlkgqgawDLVKQglvmvPE-------GR--- 92
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGK--------DVTKL-----PEykrakyiGRvfq 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 93 ----GTFTRMTITENLLMgAYIRD---------DKAQIEADIERI--FGIfpRLKERRNQLAGTMSGGEQQMLAMGRALM 157
Cdd:COG1101 88 dpmmGTAPSMTIEENLAL-AYRRGkrrglrrglTKKRRELFRELLatLGL--GLENRLDTKVGLLSGGQRQALSLLMATL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032805432 158 TRPKVLLLDEPSMGLSPIMVDKIFEVVNDI-HSQGVTVLLVEQNASRALQLASRGYVMESGLI 219
Cdd:COG1101 165 TKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
19-207 |
4.39e-26 |
|
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: 100.79 E-value: 4.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 19 GGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGK---TLKGQgAWDLVKQGLVMVPEGRGTF 95
Cdd:TIGR02673 13 GGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEdvnRLRGR-QLPLLRRRIGVVFQDFRLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 96 TRMTITENLLMGAYIRDDKAQieaDIERIFGIFPR---LKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLLDEPSMGL 172
Cdd:TIGR02673 92 PDRTVYENVALPLEVRGKKER---EIQRRVGAALRqvgLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2032805432 173 SPIMVDKIFEVVNDIHSQGVTVL-------LVEQNASRALQL 207
Cdd:TIGR02673 169 DPDLSERILDLLKRLNKRGTTVIvathdlsLVDRVAHRVIIL 210
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
18-232 |
5.52e-26 |
|
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: 101.22 E-value: 5.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 18 YGGIQ-AVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKgqgAWDLVK--QGLVMVPEGRGT 94
Cdd:cd03295 10 YGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIR---EQDPVElrRKIGYVIQQIGL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 95 FTRMTITENL-LMGAYIRDDKAQIEADIE---RIFGIFPrlKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLLDEPSM 170
Cdd:cd03295 87 FPHMTVEENIaLVPKLLKWPKEKIRERADellALVGLDP--AEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFG 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032805432 171 GLSPIMVDKIFEVVNDIHSQ-GVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLNDP 232
Cdd:cd03295 165 ALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSP 227
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-197 |
6.77e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 105.11 E-value: 6.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 4 SKEILLKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQ 83
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 84 GLVMVPEgrgTFT---RMTITENLLMGA----YIRDDKAQIEADIERI-----FGIFPrlkerrNQLAGTMSGGEQQMLA 151
Cdd:COG3845 81 GIGMVHQ---HFMlvpNLTVAENIVLGLeptkGGRLDRKAARARIRELserygLDVDP------DAKVEDLSVGEQQRVE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2032805432 152 MGRALMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQGVTVLLV 197
Cdd:COG3845 152 ILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFI 197
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
5-233 |
1.34e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 100.62 E-value: 1.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 5 KEILLKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVT---GLQP--VAAGEIEFMGKTLKGQGAwD 79
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmnDLNPevTITGSIVYNGHNIYSPRT-D 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 80 LV--KQGLVMVPEGRGTFTrMTITENLLMGAYIR--DDKAQIEADIERIF---GIFPRLKERRNQLAGTMSGGEQQMLAM 152
Cdd:PRK14239 81 TVdlRKEIGMVFQQPNPFP-MSIYENVVYGLRLKgiKDKQVLDEAVEKSLkgaSIWDEVKDRLHDSALGLSGGQQQRVCI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 153 GRALMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQgVTVLLVeqnaSRALQLASR-----GYVMESGLITMtGEGKT 227
Cdd:PRK14239 160 ARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLV----TRSMQQASRisdrtGFFLDGDLIEY-NDTKQ 233
|
....*.
gi 2032805432 228 LLNDPK 233
Cdd:PRK14239 234 MFMNPK 239
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
9-217 |
7.07e-25 |
|
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: 96.30 E-value: 7.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGG--IQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQgLV 86
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN-IA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 87 MVPEGRGTFTrMTITENLLmgayirddkaqieadierifgifprlkerrnqlagtmSGGEQQMLAMGRALMTRPKVLLLD 166
Cdd:cd03228 80 YVPQDPFLFS-GTIRENIL-------------------------------------SGGQRQRIAIARALLRDPPILILD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2032805432 167 EPSMGLSPIMVDKIFEVVNDIhSQGVTVLLVEQNASrALQLASRGYVMESG 217
Cdd:cd03228 122 EATSALDPETEALILEALRAL-AKGKTVIVIAHRLS-TIRDADRIIVLDDG 170
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
11-233 |
7.15e-25 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 98.67 E-value: 7.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 11 VSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGL-QP----VAAGEIEF-MGKTLKGQ-GAWDLVKQ 83
Cdd:PRK11264 6 VKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLeQPeagtIRVGDITIdTARSLSQQkGLIRQLRQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 84 GLVMVPEGRGTFTRMTITENLLMGAYIRDDKAQIEAdIERIFGIFPR--LKERRNQLAGTMSGGEQQMLAMGRALMTRPK 161
Cdd:PRK11264 86 HVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEA-TARARELLAKvgLAGKETSYPRRLSGGQQQRVAIARALAMRPE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032805432 162 VLLLDEPSMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLNDPK 233
Cdd:PRK11264 165 VILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQ 236
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
8-238 |
1.31e-24 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 97.88 E-value: 1.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 8 LLKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQGLVM 87
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 88 VPEGRGTFTrMTITENLLMGAY-----IRDDKAQIEADIERiFGIfPRLKERRNQlagTMSGGEQQMLAMGRAL------ 156
Cdd:COG4559 81 PQHSSLAFP-FTVEEVVALGRAphgssAAQDRQIVREALAL-VGL-AHLAGRSYQ---TLSGGEQQRVQLARVLaqlwep 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 157 -MTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLNDPKVR 235
Cdd:COG4559 155 vDGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELLE 234
|
...
gi 2032805432 236 AAY 238
Cdd:COG4559 235 RVY 237
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-217 |
1.46e-24 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 97.80 E-value: 1.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 2 ADSKEILLKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAV---TGLQPVAA--GEIEFMGKTLKGQG 76
Cdd:COG1117 5 ASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmNDLIPGARveGEILLDGEDIYDPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 77 aWDLV----KQGLVmvpegrgtFTR-----MTITENLLMGAYIR--DDKAQIEADIE---RIFGIFPRLKERRNQLAGTM 142
Cdd:COG1117 85 -VDVVelrrRVGMV--------FQKpnpfpKSIYDNVAYGLRLHgiKSKSELDEIVEeslRKAALWDEVKDRLKKSALGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 143 SGGEQQMLAMGRALMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQgVTVLLVEQNasraLQLASR----------GY 212
Cdd:COG1117 156 SGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHN----MQQAARvsdytaffylGE 230
|
....*
gi 2032805432 213 VMESG 217
Cdd:COG1117 231 LVEFG 235
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
6-220 |
1.76e-24 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 100.85 E-value: 1.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 6 EILLKVSGLKVAyggiqAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQGL 85
Cdd:PRK10762 255 EVRLKVDNLSGP-----GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGI 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 86 VMVPEGR---GTFTRMTITENLLMGA--YIRDDKAQIEADIERI-FGIFPRL----KERRNQLAGTMSGGEQQMLAMGRA 155
Cdd:PRK10762 330 VYISEDRkrdGLVLGMSVKENMSLTAlrYFSRAGGSLKHADEQQaVSDFIRLfnikTPSMEQAIGLLSGGNQQKVAIARG 409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032805432 156 LMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESGLIT 220
Cdd:PRK10762 410 LMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRIS 474
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
23-230 |
6.51e-24 |
|
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: 99.91 E-value: 6.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 23 AVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQ-GLVMvPEGRgTFTRmTIT 101
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQiGVVL-QDVF-LFSG-TIR 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 102 ENLLMGAYIRDDK--------AQIEADIERifgiFP-----RLKERRNQLagtmSGGEQQMLAMGRALMTRPKVLLLDEP 168
Cdd:COG2274 567 ENITLGDPDATDEeiieaarlAGLHDFIEA----LPmgydtVVGEGGSNL----SGGQRQRLAIARALLRNPRILILDEA 638
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032805432 169 SMGLSPIMVDKIFEVVNDIhSQGVTVLLVEQNASrALQLASRGYVMESGLITMTGEGKTLLN 230
Cdd:COG2274 639 TSALDAETEAIILENLRRL-LKGRTVIIIAHRLS-TIRLADRIIVLDKGRIVEDGTHEELLA 698
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
6-193 |
1.07e-23 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 98.85 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 6 EILLKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAA--GEIEFMGKTLKGQGAWD---- 79
Cdd:PRK13549 3 EYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQASNIRDtera 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 80 ---LVKQGLVMVPEgrgtftrMTITENLLMGA------YIRDDKAQIEAD--IERI-FGIFPRLKerrnqlAGTMSGGEQ 147
Cdd:PRK13549 83 giaIIHQELALVKE-------LSVLENIFLGNeitpggIMDYDAMYLRAQklLAQLkLDINPATP------VGNLGLGQQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2032805432 148 QMLAMGRALMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQGVT 193
Cdd:PRK13549 150 QLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIA 195
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
9-229 |
1.28e-23 |
|
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: 98.68 E-value: 1.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAY-GGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQgLVM 87
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQ-IAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 88 VPEgRGTFTRMTITENLLMGAYIRDD--------KAQIEADIERIF-GIFPRLKERrnqlAGTMSGGEQQMLAMGRALMT 158
Cdd:COG4988 416 VPQ-NPYLFAGTIRENLRLGRPDASDeeleaaleAAGLDEFVAALPdGLDTPLGEG----GRGLSGGQAQRLALARALLR 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032805432 159 RPKVLLLDEPSMGLSPIMVDKIFEVVNDIhSQGVTVLLVeqnASR--ALQLASRGYVMESGLITMTGEGKTLL 229
Cdd:COG4988 491 DAPLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILI---THRlaLLAQADRILVLDDGRIVEQGTHEELL 559
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
28-241 |
1.63e-23 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 94.44 E-value: 1.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 28 DFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKtlkgqgawDLVKQGlvmvPEGRGT---------FTRM 98
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQ--------DLTALP----PAERPVsmlfqennlFPHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 99 TITENLLMG-----AYIRDDKAQIEADIERIfGIFPrLKERrnqLAGTMSGGEQQMLAMGRALMTRPKVLLLDEPSMGLS 173
Cdd:COG3840 87 TVAQNIGLGlrpglKLTAEQRAQVEQALERV-GLAG-LLDR---LPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032805432 174 PIMVDKIFEVVNDIH-SQGVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLL--NDPKVRAAYLGE 241
Cdd:COG3840 162 PALRQEMLDLVDELCrERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLdgEPPPALAAYLGI 232
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
27-232 |
1.89e-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: 96.72 E-value: 1.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 27 VDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGawdlvkQGLVMVPEGRGT---------FTR 97
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSR------KGIFLPPEKRRIgyvfqearlFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 98 MTITENLLMGaYIRDDKAQIEADIERI---FGIFPRLKerrnQLAGTMSGGEQQMLAMGRALMTRPKVLLLDEPSMGLSP 174
Cdd:TIGR02142 90 LSVRGNLRYG-MKRARPSERRISFERVielLGIGHLLG----RLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2032805432 175 IMVDKIFEVVNDIHSQ-GVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLNDP 232
Cdd:TIGR02142 165 PRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
7-168 |
2.28e-23 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 94.84 E-value: 2.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 7 ILLKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQGLV 86
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 87 MVPEGRGTFTrMTITENLLMGAYI-----RDDKAQIEADIERIfGIFPrLKERRNQlagTMSGGEQQMLAMGRALM---- 157
Cdd:PRK13548 81 LPQHSSLSFP-FTVEEVVAMGRAPhglsrAEDDALVAAALAQV-DLAH-LAGRDYP---QLSGGEQQRVQLARVLAqlwe 154
|
170
....*....|...
gi 2032805432 158 --TRPKVLLLDEP 168
Cdd:PRK13548 155 pdGPPRWLLLDEP 167
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
9-241 |
2.30e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 97.22 E-value: 2.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQgLVMV 88
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR-VASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 89 PEGRG---TFTRMTITEnllMG---------AYIRDDKAQIEADIERIfgifpRLKERRNQLAGTMSGGEQQMLAMGRAL 156
Cdd:PRK09536 83 PQDTSlsfEFDVRQVVE---MGrtphrsrfdTWTETDRAAVERAMERT-----GVAQFADRPVTSLSGGERQRVLLARAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 157 MTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQGVTVLLveqnASRALQLASRgY-----VMESGLITMTGEGKTLLND 231
Cdd:PRK09536 155 AQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVA----AIHDLDLAAR-YcdelvLLADGRVRAAGPPADVLTA 229
|
250
....*....|
gi 2032805432 232 PKVRAAYLGE 241
Cdd:PRK09536 230 DTLRAAFDAR 239
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
27-220 |
2.40e-23 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 97.81 E-value: 2.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 27 VDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQGLVMVPEGR---GTFTRMTITEN 103
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVYLPEDRqssGLYLDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 104 L------LMGAYIRD--DKAQIEAdIERIFGIfpRLKErRNQLAGTMSGGEQQMLAMGRALMTRPKVLLLDEPSMGLSPI 175
Cdd:PRK15439 362 VcalthnRRGFWIKParENAVLER-YRRALNI--KFNH-AEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVS 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2032805432 176 MVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESGLIT 220
Cdd:PRK15439 438 ARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEIS 482
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
8-233 |
2.47e-23 |
|
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: 95.89 E-value: 2.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 8 LLKVSGLKVAY----GGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQP---VAAGEIEFMGKTLKGQGAWDL 80
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 81 VK---QGLVMV---------PegrgtftRMTI----TENLLmgAYIRDDKAQIEADIERIF---GIfPRLKERRNQLAGT 141
Cdd:COG0444 81 RKirgREIQMIfqdpmtslnP-------VMTVgdqiAEPLR--IHGGLSKAEARERAIELLervGL-PDPERRLDRYPHE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 142 MSGGEQQ--MLAMgrALMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQ-GVTVLLVEQNASRALQLASRGYVMESGL 218
Cdd:COG0444 151 LSGGMRQrvMIAR--ALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGR 228
|
250
....*....|....*
gi 2032805432 219 ITMTGEGKTLLNDPK 233
Cdd:COG0444 229 IVEEGPVEELFENPR 243
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
9-239 |
2.70e-23 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 94.31 E-value: 2.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLK-----GQGAWDLVKQ 83
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqkpSEKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 84 GLVMVPEGRGTFTRMTITENLLmGAYIRDDKAQIEADIERIFGIFPRLK--ERRNQLAGTMSGGEQQMLAMGRALMTRPK 161
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENLI-EAPCKVLGLSKEQAREKAMKLLARLRltDKADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 162 VLLLDEPSMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESGLITMTGeGKTLLNDPKVR--AAYL 239
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG-DASHFTQPQTEafAHYL 240
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
9-239 |
2.76e-23 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 94.31 E-value: 2.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIE-------FMGKTLKGQGAwdLV 81
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNiagnhfdFSKTPSDKAIR--EL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 82 KQGLVMVPEGRGTFTRMTITENLLMgAYIR-----DDKAQIEAD--IERIfgifpRLKERRNQLAGTMSGGEQQMLAMGR 154
Cdd:PRK11124 81 RRNVGMVFQQYNLWPHLTVQQNLIE-APCRvlglsKDQALARAEklLERL-----RLKPYADRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 155 ALMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESGLITMTGEgKTLLNDPKV 234
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD-ASCFTQPQT 233
|
....*..
gi 2032805432 235 R--AAYL 239
Cdd:PRK11124 234 EafKNYL 240
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
6-231 |
4.74e-23 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 93.92 E-value: 4.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 6 EILLKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGL---QPVAAGEIEFMGKTLKGQG--AWDL 80
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGrlARDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 81 VKQ----GLVMvpEGRGTFTRMTITENLLMGA-------------YIRDDKAQIEADIERIfgifpRLKERRNQLAGTMS 143
Cdd:PRK09984 82 RKSrantGYIF--QQFNLVNRLSVLENVLIGAlgstpfwrtcfswFTREQKQRALQALTRV-----GMVHFAHQRVSTLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 144 GGEQQMLAMGRALMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIH-SQGVTVLLVEQNASRALQLASRGYVMESGLITMT 222
Cdd:PRK09984 155 GGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINqNDGITVVVTLHQVDYALRYCERIVALRQGHVFYD 234
|
....*....
gi 2032805432 223 GEGKTLLND 231
Cdd:PRK09984 235 GSSQQFDNE 243
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
9-232 |
4.81e-23 |
|
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: 97.14 E-value: 4.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAY--GGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKgqgAWDL--VKQG 84
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLR---DLDEddLRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 85 LVMVPEgRGTFTRMTITENLLMGAYIRDDkAQIEADIERIfGIFPRLKERRNQL-------AGTMSGGEQQMLAMGRALM 157
Cdd:COG4987 411 IAVVPQ-RPHLFDTTLRENLRLARPDATD-EELWAALERV-GLGDWLAALPDGLdtwlgegGRRLSGGERRRLALARALL 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032805432 158 TRPKVLLLDEPSMGLSPIMVDKIFEVVNDiHSQGVTVLLVEQNASrALQLASRGYVMESGLITMTGEGKTLLNDP 232
Cdd:COG4987 488 RDAPILLLDEPTEGLDAATEQALLADLLE-ALAGRTVLLITHRLA-GLERMDRILVLEDGRIVEQGTHEELLAQN 560
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
9-174 |
1.33e-22 |
|
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: 91.49 E-value: 1.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGGIQAVKGVDFEVRRGeLVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGawDLVKQGLVMV 88
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP--QKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 89 PEGRGTFTRMTITENL-----LMGAYIRDDKAQIEADIERIfgifpRLKERRNQLAGTMSGGEQQMLAMGRALMTRPKVL 163
Cdd:cd03264 78 PQEFGVYPNFTVREFLdyiawLKGIPSKEVKARVDEVLELV-----NLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSIL 152
|
170
....*....|.
gi 2032805432 164 LLDEPSMGLSP 174
Cdd:cd03264 153 IVDEPTAGLDP 163
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
9-168 |
2.13e-22 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 93.75 E-value: 2.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAY-GGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKtlkgqgawdLVKQ---- 83
Cdd:PRK11650 4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGR---------VVNElepa 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 84 --GLVMVPEGRGTFTRMTITENLLMGAYIRD-DKAQIEADIE---RIFGIFPRLKERRNQLagtmSGGEQQMLAMGRALM 157
Cdd:PRK11650 75 drDIAMVFQNYALYPHMSVRENMAYGLKIRGmPKAEIEERVAeaaRILELEPLLDRKPREL----SGGQRQRVAMGRAIV 150
|
170
....*....|.
gi 2032805432 158 TRPKVLLLDEP 168
Cdd:PRK11650 151 REPAVFLFDEP 161
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
6-220 |
2.15e-22 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 94.98 E-value: 2.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 6 EILLKVSGLKvaygGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQGL 85
Cdd:PRK11288 255 EVRLRLDGLK----GPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGI 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 86 VMVPEGR---GTFTRMTITENL--------LMGAYIRDDKAQIE-AD--IERIfgifpRLKER-RNQLAGTMSGGEQQML 150
Cdd:PRK11288 331 MLCPEDRkaeGIIPVHSVADNInisarrhhLRAGCLINNRWEAEnADrfIRSL-----NIKTPsREQLIMNLSGGNQQKA 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 151 AMGRALMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESGLIT 220
Cdd:PRK11288 406 ILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
9-197 |
3.74e-22 |
|
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: 94.28 E-value: 3.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGG-IQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQgLVM 87
Cdd:TIGR02857 322 LEFSGVSVAYPGrRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQ-IAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 88 VPEgRGTFTRMTITENLLMGAYIRDDkAQIEADIERIfGIFPRLKERRNQLA------GTM-SGGEQQMLAMGRALMTRP 160
Cdd:TIGR02857 401 VPQ-HPFLFAGTIAENIRLARPDASD-AEIREALERA-GLDEFVAALPQGLDtpigegGAGlSGGQAQRLALARAFLRDA 477
|
170 180 190
....*....|....*....|....*....|....*..
gi 2032805432 161 KVLLLDEPSMGLSPIMVDKIFEVVNDIhSQGVTVLLV 197
Cdd:TIGR02857 478 PLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLV 513
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
19-219 |
3.92e-22 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 90.54 E-value: 3.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 19 GGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKG--QGAWDLVKQGLVMVPEGRGTFT 96
Cdd:cd03292 12 NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlrGRAIPYLRRKIGVVFQDFRLLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 97 RMTITENLLMGAYIRDDKAQIEAdiERIFGIFPR--LKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLLDEPSMGLSP 174
Cdd:cd03292 92 DRNVYENVAFALEVTGVPPREIR--KRVPAALELvgLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2032805432 175 IMVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESGLI 219
Cdd:cd03292 170 DTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
28-223 |
4.05e-22 |
|
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: 90.24 E-value: 4.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 28 DFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIefmgkTLKGQ--GAWDLVKQGLVMVPEGRGTFTRMTITENLL 105
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRV-----LINGVdvTAAPPADRPVSMLFQENNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 106 MGayiRDDKAQI-EADIERIFGIFPR--LKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLLDEPSMGLSPIMVDKIFE 182
Cdd:cd03298 93 LG---LSPGLKLtAEDRQAIEVALARvgLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2032805432 183 VVNDIHSQ-GVTVLLVEQNASRALQLASRGYVMESGLITMTG 223
Cdd:cd03298 170 LVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-220 |
5.43e-22 |
|
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: 90.57 E-value: 5.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 1 MADSKEILLKVSGLKVAYGG----IQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLkgqG 76
Cdd:COG4181 1 MSSSSAPIIELRGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDL---F 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 77 AWDlvkqglvmvPEGRGTFTR---------------MTITENLLM-----GAyiRDDKAQIEADIERIfGifprLKERRN 136
Cdd:COG4181 78 ALD---------EDARARLRArhvgfvfqsfqllptLTALENVMLplelaGR--RDARARARALLERV-G----LGHRLD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 137 QLAGTMSGGEQQMLAMGRALMTRPKVLLLDEPSMGL----SPIMVDKIFEVVNDihsQGVTVLLV---EQNASRalqlAS 209
Cdd:COG4181 142 HYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLdaatGEQIIDLLFELNRE---RGTTLVLVthdPALAAR----CD 214
|
250
....*....|.
gi 2032805432 210 RGYVMESGLIT 220
Cdd:COG4181 215 RVLRLRAGRLV 225
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
20-220 |
5.90e-22 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 93.84 E-value: 5.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 20 GIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVA-AGEIEFMGKTLKGQGAWDLVKQGLVMVPEGR---GTF 95
Cdd:PRK13549 274 HIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRwEGEIFIDGKPVKIRNPQQAIAQGIAMVPEDRkrdGIV 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 96 TRMTITENLLMGAYIR-------DDKAQ---IEADIERIfgifpRLKERRNQLA-GTMSGGEQQMLAMGRALMTRPKVLL 164
Cdd:PRK13549 354 PVMGVGKNITLAALDRftggsriDDAAElktILESIQRL-----KVKTASPELAiARLSGGNQQKAVLAKCLLLNPKILI 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032805432 165 LDEPSMGlspimVD-----KIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESGLIT 220
Cdd:PRK13549 429 LDEPTRG-----IDvgakyEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLK 484
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
8-192 |
6.01e-22 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 93.74 E-value: 6.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 8 LLKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAA--GEIEFMGKTLKGQGAWDLVKQGL 85
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 86 VMVPEGRGTFTRMTITENLLMGAYIrDDKAQIEADIERIFGIFPRLKERR------NQLAGTMSGGEQQMLAMGRALMTR 159
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNEI-TLPGGRMAYNAMYLRAKNLLRELQldadnvTRPVGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190
....*....|....*....|....*....|...
gi 2032805432 160 PKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQGV 192
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILLDIIRDLKAHGV 192
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
6-241 |
7.65e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 91.00 E-value: 7.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 6 EILLKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPV-----AAGEIEFMGKTLKGQGAWDL 80
Cdd:PRK14243 8 ETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLYAPDVDPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 81 -VKQGLVMVPEGRGTFTRmTITENLLMGAYIRDDKAQIEADIERIF---GIFPRLKERRNQLAGTMSGGEQQMLAMGRAL 156
Cdd:PRK14243 88 eVRRRIGMVFQKPNPFPK-SIYDNIAYGARINGYKGDMDELVERSLrqaALWDEVKDKLKQSGLSLSGGQQQRLCIARAI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 157 MTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQgVTVLLVEQNasraLQLASRgyvmesgLITMTGEGKTLLNDPKVRA 236
Cdd:PRK14243 167 AVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHN----MQQAAR-------VSDMTAFFNVELTEGGGRY 234
|
....*
gi 2032805432 237 AYLGE 241
Cdd:PRK14243 235 GYLVE 239
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-233 |
9.13e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 90.36 E-value: 9.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGL-----QPVAAGEIEFMGKTLKGQGAWDLVKQ 83
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 84 gLVMVPEGRGTFTRMTITENLLMGAYIR---DDKAQIEADIERIF---GIFPRLKERRNQLAGTMSGGEQQMLAMGRALM 157
Cdd:PRK14247 84 -VQMVFQIPNPIPNLSIFENVALGLKLNrlvKSKKELQERVRWALekaQLWDEVKDRLDAPAGKLSGGQQQRLCIARALA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2032805432 158 TRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQgVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLNDPK 233
Cdd:PRK14247 163 FQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPR 237
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-233 |
9.36e-22 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 90.41 E-value: 9.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 1 MADSKeilLKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLK------G 74
Cdd:PRK10619 1 MSENK---LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 75 Q------GAWDLVKQGLVMVPEGRGTFTRMTITENLL------MGAYIRDDKAQIEADIERIfGIFPRlkeRRNQLAGTM 142
Cdd:PRK10619 78 QlkvadkNQLRLLRTRLTMVFQHFNLWSHMTVLENVMeapiqvLGLSKQEARERAVKYLAKV-GIDER---AQGKYPVHL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 143 SGGEQQMLAMGRALMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESGLITMT 222
Cdd:PRK10619 154 SGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEE 233
|
250
....*....|.
gi 2032805432 223 GEGKTLLNDPK 233
Cdd:PRK10619 234 GAPEQLFGNPQ 244
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
8-235 |
1.01e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 93.31 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 8 LLKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQGLVM 87
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 88 VPEGRGTFTRMTITENL---------LMGAYIRD-DKAQIEADIerifgIFPRLKERR--NQLAGTMSGGEQQMLAMGRA 155
Cdd:PRK09700 85 IYQELSVIDELTVLENLyigrhltkkVCGVNIIDwREMRVRAAM-----MLLRVGLKVdlDEKVANLSISHKQMLEIAKT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 156 LMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLNDPKVR 235
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVR 239
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
15-196 |
1.94e-21 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 88.78 E-value: 1.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 15 KVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMG---KTLKGQGAWDLVKQgLVMVPEG 91
Cdd:PRK10908 9 KAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhdiTRLKNREVPFLRRQ-IGMIFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 92 RGTFTRMTITENLLM-----GAYIRDDKAQIEADIERIfGIFPRLKERRNQLagtmSGGEQQMLAMGRALMTRPKVLLLD 166
Cdd:PRK10908 88 HHLLMDRTVYDNVAIpliiaGASGDDIRRRVSAALDKV-GLLDKAKNFPIQL----SGGEQQRVGIARAVVNKPAVLLAD 162
|
170 180 190
....*....|....*....|....*....|
gi 2032805432 167 EPSMGLSPIMVDKIFEVVNDIHSQGVTVLL 196
Cdd:PRK10908 163 EPTGNLDDALSEGILRLFEEFNRVGVTVLM 192
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
21-217 |
2.35e-21 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 92.20 E-value: 2.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 21 IQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVA-AGEIEFMGKTLKGQGAWDLVKQGLVMVPEGR---GTFT 96
Cdd:TIGR02633 273 RKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQAIRAGIAMVPEDRkrhGIVP 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 97 RMTITENLLMGAYIR-------DDKAQ---IEADIERIfgifpRLKERRNQLA-GTMSGGEQQMLAMGRALMTRPKVLLL 165
Cdd:TIGR02633 353 ILGVGKNITLSVLKSfcfkmriDAAAElqiIGSAIQRL-----KVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLIL 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2032805432 166 DEPSMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESG 217
Cdd:TIGR02633 428 DEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
6-191 |
2.47e-21 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 91.99 E-value: 2.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 6 EILLKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWD------ 79
Cdd:PRK10762 2 QALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSsqeagi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 80 -LVKQGLVMVPEgrgtftrMTITENLLMG-------AYIRDDKAQIEADierifGIFPRLKERRN--QLAGTMSGGEQQM 149
Cdd:PRK10762 82 gIIHQELNLIPQ-------LTIAENIFLGrefvnrfGRIDWKKMYAEAD-----KLLARLNLRFSsdKLVGELSIGEQQM 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2032805432 150 LAMGRALMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQG 191
Cdd:PRK10762 150 VEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQG 191
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
17-197 |
8.45e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 86.13 E-value: 8.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 17 AYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGqgawdLVKQ------------- 83
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVA-----YVPQrsevpdslpltvr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 84 GLVMVpegrGTFTRMTitenlLMGAYIRDDKAQIEADIERIfGIfPRLKERRnqlAGTMSGGEQQMLAMGRALMTRPKVL 163
Cdd:NF040873 76 DLVAM----GRWARRG-----LWRRLTRDDRAAVDDALERV-GL-ADLAGRQ---LGELSGGQRQRALLAQGLAQEADLL 141
|
170 180 190
....*....|....*....|....*....|....
gi 2032805432 164 LLDEPSMGLSPIMVDKIFEVVNDIHSQGVTVLLV 197
Cdd:NF040873 142 LLDEPTTGLDAESRERIIALLAEEHARGATVVVV 175
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
20-223 |
1.18e-20 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 90.46 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 20 GIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLkgQGAWDLVKQGLVMVPEGRGTFTRMT 99
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI--ETNLDAVRQSLGMCPQHNILFHHLT 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 100 ITENLLMGAYIRD---DKAQIE--ADIERIfgifpRLKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLLDEPSMGLSP 174
Cdd:TIGR01257 1020 VAEHILFYAQLKGrswEEAQLEmeAMLEDT-----GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDP 1094
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2032805432 175 IMVDKIFEVVNDIHSqGVTVLLVEQNASRALQLASRGYVMESGLITMTG 223
Cdd:TIGR01257 1095 YSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
24-224 |
1.39e-20 |
|
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: 86.75 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 24 VKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVkqglvmVPEGRGTFTRMTITEN 103
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV------VFQNYSLLPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 104 --LLMGAYIRD-DKAQIEADIERIFGIFpRLKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLLDEPSMGLSPI----M 176
Cdd:TIGR01184 75 iaLAVDRVLPDlSKSERRAIVEEHIALV-GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALtrgnL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2032805432 177 VDKIFEVVNDihsQGVTVLLVEQNASRALQLASRGYVMESGLITMTGE 224
Cdd:TIGR01184 154 QEELMQIWEE---HRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQ 198
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
13-223 |
1.41e-20 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 86.43 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 13 GLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTlkgqgAWdLVKQGLVMVPEgr 92
Cdd:cd03220 27 GRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV-----SS-LLGLGGGFNPE-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 93 gtftrMTITENL-LMGAYIRDDKAQIEADIERIFGiFPRLKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLLDEpsmg 171
Cdd:cd03220 99 -----LTGRENIyLNGRLLGLSRKEIDEKIDEIIE-FSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDE---- 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2032805432 172 lsPIMV------DKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESGLITMTG 223
Cdd:cd03220 169 --VLAVgdaafqEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
9-197 |
1.79e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 89.59 E-value: 1.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQG---- 84
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGvaii 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 85 ---LVMVPEgrgtftrMTITENLLMGAY--------IRDDKAQIEADIERI-FGIFPRLKERRnqlagtMSGGEQQMLAM 152
Cdd:PRK11288 85 yqeLHLVPE-------MTVAENLYLGQLphkggivnRRLLNYEAREQLEHLgVDIDPDTPLKY------LSIGQRQMVEI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2032805432 153 GRALMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQGVTVLLV 197
Cdd:PRK11288 152 AKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYV 196
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
27-241 |
1.99e-20 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 88.24 E-value: 1.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 27 VDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKtlkgqgawDLVKQG-----LVMVPEGRGTFTRMTIT 101
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGE--------DVTHRSiqqrdICMVFQSYALFPHMSLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 102 EN----LLMGAYIRDDKAQieadierifgifpRLKERRN--QLAG-------TMSGGEQQMLAMGRALMTRPKVLLLDEP 168
Cdd:PRK11432 97 ENvgygLKMLGVPKEERKQ-------------RVKEALElvDLAGfedryvdQISGGQQQRVALARALILKPKVLLFDEP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 169 smgLSPI-------MVDKIFEVVNDIhsqGVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLNDPKVR--AAYL 239
Cdd:PRK11432 164 ---LSNLdanlrrsMREKIRELQQQF---NITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRfmASFM 237
|
..
gi 2032805432 240 GE 241
Cdd:PRK11432 238 GD 239
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-168 |
2.34e-20 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 87.86 E-value: 2.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 2 ADSKEILLKVSGLKVAY---GGI--------QAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGK 70
Cdd:COG4608 1 AAMAEPLLEVRDLKKHFpvrGGLfgrtvgvvKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 71 TLKGQGAWDLVK--QGLVMVpegrgtF--------TRMTItenllmgayirddkAQIEADIERIFGIFPRlKERRNQLAG 140
Cdd:COG4608 81 DITGLSGRELRPlrRRMQMV------FqdpyaslnPRMTV--------------GDIIAEPLRIHGLASK-AERRERVAE 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2032805432 141 TM-----------------SGGEQQMLAMGRALMTRPKVLLLDEP 168
Cdd:COG4608 140 LLelvglrpehadryphefSGGQRQRIGIARALALNPKLIVCDEP 184
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
11-200 |
3.36e-20 |
|
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: 84.97 E-value: 3.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 11 VSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGK---TLKGQGAWDLVKQGLVM 87
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQetpPLNSKKASKFRREKLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 88 VPEGRGTFTRMTITENLLMG-AYIRDDKAQIEADIERI---FGIFPRLKERRNQLagtmSGGEQQMLAMGRALMTRPKVL 163
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGlKYKKLSKKEKREKKKEAlekVGLNLKLKQKIYEL----SGGEQQRVALARAILKPPPLI 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 2032805432 164 LLDEPSMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQN 200
Cdd:TIGR03608 157 LADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHD 193
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
9-195 |
3.51e-20 |
|
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: 84.72 E-value: 3.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGawDLVKQGLVMV 88
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQR--DEPHENILYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 89 PEGRGTFTRMTITENL-LMGAYIRDDKAQIEADIERIfgifpRLKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLLDE 167
Cdd:TIGR01189 79 GHLPGLKPELSALENLhFWAAIHGGAQRTIEDALAAV-----GLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDE 153
|
170 180
....*....|....*....|....*....
gi 2032805432 168 PSMGLSPIMVDKIFEVVND-IHSQGVTVL 195
Cdd:TIGR01189 154 PTTALDKAGVALLAGLLRAhLARGGIVLL 182
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
18-223 |
4.81e-20 |
|
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: 85.46 E-value: 4.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 18 YGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGktlkgqgawdlvkqglvMVP-EGRGTFT 96
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-----------------LVPwKRRKKFL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 97 RMTiteNLLMGayirdDKAQIEADI---------ERIFGIFP-RLKERRNQLAGTMSGGE------------QQMLA-MG 153
Cdd:cd03267 94 RRI---GVVFG-----QKTQLWWDLpvidsfyllAAIYDLPPaRFKKRLDELSELLDLEElldtpvrqlslgQRMRAeIA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032805432 154 RALMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQ-GVTVLLVEQNASRALQLASRGYVMESGLITMTG 223
Cdd:cd03267 166 AALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
21-233 |
6.09e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 86.29 E-value: 6.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 21 IQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQGLVMVPEGRGTFTRMTI 100
Cdd:PRK13651 20 LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEKVLEKLVIQKTRFKKIKK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 101 TENL-------LMGAYIRDDKAQIEADIerIFGifPRL----KERRNQLAGTM------------------SGGEQQMLA 151
Cdd:PRK13651 100 IKEIrrrvgvvFQFAEYQLFEQTIEKDI--IFG--PVSmgvsKEEAKKRAAKYielvgldesylqrspfelSGGQKRRVA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 152 MGRALMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLND 231
Cdd:PRK13651 176 LAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDILSD 255
|
..
gi 2032805432 232 PK 233
Cdd:PRK13651 256 NK 257
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
3-232 |
6.87e-20 |
|
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: 85.77 E-value: 6.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 3 DSKEILLKVSGLKVAyggiqaVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLV- 81
Cdd:cd03294 25 KSKEEILKKTGQTVG------VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRe 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 82 --KQGLVMVPEGRGTFTRMTITENLLMGAYIRDDKAQIEAD-----IERIfgifpRLKERRNQLAGTMSGGEQQMLAMGR 154
Cdd:cd03294 99 lrRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREEraaeaLELV-----GLEGWEHKYPDELSGGMQQRVGLAR 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032805432 155 ALMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHS-QGVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLNDP 232
Cdd:cd03294 174 ALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAeLQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNP 252
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
24-220 |
7.10e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 87.92 E-value: 7.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 24 VKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQGLVMVPEGR---GTFTRMTI 100
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYITESRrdnGFFPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 101 TENLLMGAYIRDDKaqieadIERIFGIFPRLKERR----------------NQLAGTMSGGEQQMLAMGRALMTRPKVLL 164
Cdd:PRK09700 359 AQNMAISRSLKDGG------YKGAMGLFHEVDEQRtaenqrellalkchsvNQNITELSGGNQQKVLISKWLCCCPEVII 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2032805432 165 LDEPSMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESGLIT 220
Cdd:PRK09700 433 FDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLT 488
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-196 |
1.15e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 85.91 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 21 IQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTG-LQPvAAGEIEFMGKTlkgqgAW----DLVKQ-GLVMvpegrGT 94
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGiLVP-TSGEVRVLGYV-----PFkrrkEFARRiGVVF-----GQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 95 FTR----MTITENLLMgayirddkaqieadIERIFGIFP-RLKERRNQLAGTMSGGE------------QQM---LAMgr 154
Cdd:COG4586 104 RSQlwwdLPAIDSFRL--------------LKAIYRIPDaEYKKRLDELVELLDLGElldtpvrqlslgQRMrceLAA-- 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2032805432 155 ALMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIH-SQGVTVLL 196
Cdd:COG4586 168 ALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNrERGTTILL 210
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
5-223 |
1.37e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 85.07 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 5 KEILLKVSGLKVAYGGIQ--AVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVK 82
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 83 Q-GLVmvpegrgtFTRmtiTENLLMGAYIRDDKA------QIEAD--IERIFGIFPR--LKERRNQLAGTMSGGEQQMLA 151
Cdd:PRK13635 82 QvGMV--------FQN---PDNQFVGATVQDDVAfgleniGVPREemVERVDQALRQvgMEDFLNREPHRLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032805432 152 MGRALMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQ-GVTVLLVEQNASRALQlASRGYVMESGLITMTG 223
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQkGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEG 222
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-231 |
1.56e-19 |
|
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: 86.78 E-value: 1.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 5 KEILLKVSGLKVAY-----GGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEI------EFMGKTLK 73
Cdd:TIGR03269 276 GEPIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdEWVDMTKP 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 74 GQGAWDLVKQGLVMVPEGRGTFTRMTITENLL--MGAYIRDDKAQIEADIERIFGIFPRLKERR--NQLAGTMSGGEQQM 149
Cdd:TIGR03269 356 GPDGRGRAKRYIGILHQEYDLYPHRTVLDNLTeaIGLELPDELARMKAVITLKMVGFDEEKAEEilDKYPDELSEGERHR 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 150 LAMGRALMTRPKVLLLDEPSMGLSPI-MVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTL 228
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPItKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
...
gi 2032805432 229 LND 231
Cdd:TIGR03269 516 VEE 518
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-168 |
1.85e-19 |
|
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: 86.66 E-value: 1.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 2 ADSKEILLKVSGLKVAY-----------GGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPvAAGEIEFMGK 70
Cdd:COG4172 269 PPDAPPLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 71 TLKGQGAWDL--VKQGLVMV---------PegrgtftRMTItenllmgayirddkAQIEADIERIFGIFPRLKERRNQLA 139
Cdd:COG4172 348 DLDGLSRRALrpLRRRMQVVfqdpfgslsP-------RMTV--------------GQIIAEGLRVHGPGLSAAERRARVA 406
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2032805432 140 GTM-----------------SGGEQQMLAMGRALMTRPKVLLLDEP 168
Cdd:COG4172 407 EALeevgldpaarhryphefSGGQRQRIAIARALILEPKLLVLDEP 452
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-233 |
1.88e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 84.12 E-value: 1.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 14 LKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKA---VTGLQPVA--AGEIEFMGKTLKGQGAWDL-VKQGLVM 87
Cdd:PRK14267 10 LRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrLLELNEEArvEGEVRLFGRNIYSPDVDPIeVRREVGM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 88 VPEGRGTFTRMTITENLLMGAYIRD-DKAQIEADiERI------FGIFPRLKERRNQLAGTMSGGEQQMLAMGRALMTRP 160
Cdd:PRK14267 90 VFQYPNPFPHLTIYDNVAIGVKLNGlVKSKKELD-ERVewalkkAALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKP 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032805432 161 KVLLLDEPSMGLSPIMVDKIFEVVNDIHSQgVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLNDPK 233
Cdd:PRK14267 169 KILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPE 240
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-208 |
2.03e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 84.32 E-value: 2.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAA-----GEIEFMGKTL-KGQGAWDLVK 82
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyERRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 83 QGLVMVPEGRGTFTrMTITENLLMGAYIRDDKAQIEAD--IERIFG---IFPRLKERRNQLAGTMSGGEQQMLAMGRALM 157
Cdd:PRK14258 88 RQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKLEIDdiVESALKdadLWDEIKHKIHKSALDLSGGQQQRLCIARALA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2032805432 158 TRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQG-VTVLLVEQNASRALQLA 208
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSeLTMVIVSHNLHQVSRLS 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-168 |
2.18e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 86.27 E-value: 2.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 7 ILLKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFmGKTLKgqgawdlvkqgLV 86
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK-----------IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 87 MVPEGRGTF-TRMTITENLlmgAYIRDDKAQIEA-DIERIFGiFPRlkERRNQLAGTMSGGEQQMLAMGRALMTRPKVLL 164
Cdd:COG0488 382 YFDQHQEELdPDKTVLDEL---RDGAPGGTEQEVrGYLGRFL-FSG--DDAFKPVGVLSGGEKARLALAKLLLSPPNVLL 455
|
....
gi 2032805432 165 LDEP 168
Cdd:COG0488 456 LDEP 459
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
9-241 |
2.57e-19 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 85.14 E-value: 2.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLvKQGLVMv 88
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDR-KVGFVF- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 89 pEGRGTFTRMTITENLLMGAYI-----RDDKAQIEADIERIFGI--FPRLKERR-NQLagtmSGGEQQMLAMGRALMTRP 160
Cdd:PRK10851 81 -QHYALFRHMTVFDNIAFGLTVlprreRPNAAAIKAKVTQLLEMvqLAHLADRYpAQL----SGGQKQRVALARALAVEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 161 KVLLLDEPSMGLSPIMVDKIFEVVNDIHSQ-GVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLNDPKVR--AA 237
Cdd:PRK10851 156 QILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRfvLE 235
|
....
gi 2032805432 238 YLGE 241
Cdd:PRK10851 236 FMGE 239
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
8-239 |
2.76e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 83.97 E-value: 2.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 8 LLKVSGLKVAY-GGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKgqgaWDlvKQGLV 86
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK----YD--KKSLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 87 MVPEGRGTFTRMTitENLLMGAYIRDDKA-------QIEADIERifgifpRLKE--RRNQLAGT-------MSGGEQQML 150
Cdd:PRK13639 75 EVRKTVGIVFQNP--DDQLFAPTVEEDVAfgplnlgLSKEEVEK------RVKEalKAVGMEGFenkpphhLSGGQKKRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 151 AMGRALMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLN 230
Cdd:PRK13639 147 AIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFS 226
|
250
....*....|
gi 2032805432 231 DPK-VRAAYL 239
Cdd:PRK13639 227 DIEtIRKANL 236
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
28-240 |
2.92e-19 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 83.09 E-value: 2.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 28 DFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIefmgkTLKGQG--AWDLVKQGLVMVPEGRGTFTRMTITENLL 105
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSL-----TLNGQDhtTTPPSRRPVSMLFQENNLFSHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 106 MGAY--IRDDKAQIE--ADIERIFGIFPRLkerrNQLAGTMSGGEQQMLAMGRALMTRPKVLLLDEPSMGLSPIMVDKIF 181
Cdd:PRK10771 94 LGLNpgLKLNAAQREklHAIARQMGIEDLL----ARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEML 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 182 EVVNDI-HSQGVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLNDPKVRAAYLG 240
Cdd:PRK10771 170 TLVSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKASASALLG 229
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
9-208 |
4.83e-19 |
|
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: 81.77 E-value: 4.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGawDLVKQGLVMV 88
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQR--DSIARGLLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 89 PEGRGTFTRMTITENLLMGAYIRDDkAQIEADIERIfgifpRLKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLLDEP 168
Cdd:cd03231 79 GHAPGIKTTLSVLENLRFWHADHSD-EQVEEALARV-----GLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2032805432 169 SMGLSPIMVDKIFEVVNDIHSQGVTVLL-------VEQNASRALQLA 208
Cdd:cd03231 153 TTALDKAGVARFAEAMAGHCARGGMVVLtthqdlgLSEAGARELDLG 199
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
5-224 |
6.22e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 82.44 E-value: 6.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 5 KEILLKVSGLKvaYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEfmgktLKGQGAWdLVKQG 84
Cdd:COG1134 25 KELLLRRRRTR--REEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE-----VNGRVSA-LLELG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 85 LVMVPE--GRgtftrmtitENLLMGAYI----RDDKAQIEADIERifgiFPRLKERRNQLAGTMSGGEQQMLAMGRALMT 158
Cdd:COG1134 97 AGFHPEltGR---------ENIYLNGRLlglsRKEIDEKFDEIVE----FAELGDFIDQPVKTYSSGMRARLAFAVATAV 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032805432 159 RPKVLLLDEpsmGLSpimV------DKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESGLITMTGE 224
Cdd:COG1134 164 DPDILLVDE---VLA---VgdaafqKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGD 229
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
20-237 |
8.26e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 82.86 E-value: 8.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 20 GIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGA-WDLVKQGLVMVPEGRGTFTrM 98
Cdd:PRK13647 17 GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEkWVRSKVGLVFQDPDDQVFS-S 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 99 TITENLLMGAY-IRDDKAQIEADIERIFGIFpRLKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLLDEPSMGLSPIMV 177
Cdd:PRK13647 96 TVWDDVAFGPVnMGLDKDEVERRVEEALKAV-RMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQ 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 178 DKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESGLITMTGeGKTLLNDPKVRAA 237
Cdd:PRK13647 175 ETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG-DKSLLTDEDIVEQ 233
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
27-168 |
1.03e-18 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 83.61 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 27 VDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLkgQGAwdlvKQGLVMVPEGRGT---------FTR 97
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL--QDS----ARGIFLPPHRRRIgyvfqearlFPH 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032805432 98 MTITENLLMGaYIRDDKAQIEADIERI---FGIFPRLkERRnqlAGTMSGGEQQMLAMGRALMTRPKVLLLDEP 168
Cdd:COG4148 92 LSVRGNLLYG-RKRAPRAERRISFDEVvelLGIGHLL-DRR---PATLSGGERQRVAIGRALLSSPRLLLMDEP 160
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-223 |
1.11e-18 |
|
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: 84.68 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 4 SKEILLKVSGLKVAYGGIQ--AVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAwdLV 81
Cdd:TIGR01257 1933 NKTDILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNIS--DV 2010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 82 KQGLVMVPEGRGTFTRMTITENLLMGAYIRDDKAQieaDIERI--FGIFPR-LKERRNQLAGTMSGGEQQMLAMGRALMT 158
Cdd:TIGR01257 2011 HQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAE---EIEKVanWSIQSLgLSLYADRLAGTYSGGNKRKLSTAIALIG 2087
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032805432 159 RPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESGLITMTG 223
Cdd:TIGR01257 2088 CPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLG 2152
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
15-240 |
1.25e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 82.34 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 15 KVAYG---GIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTL----KGQGAWDLVkqGLVM 87
Cdd:PRK13644 6 NVSYSypdGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdfsKLQGIRKLV--GIVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 88 V-PEGRgtFTRMTITENLLMGAY--------IRD--DKAQIEADIERIfgifprlkerRNQLAGTMSGGEQQMLAMGRAL 156
Cdd:PRK13644 84 QnPETQ--FVGRTVEEDLAFGPEnlclppieIRKrvDRALAEIGLEKY----------RHRSPKTLSGGQGQCVALAGIL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 157 MTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQNASRaLQLASRGYVMESGLITMTGEGKTLLNDPKVRa 236
Cdd:PRK13644 152 TMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSLQ- 229
|
....
gi 2032805432 237 aYLG 240
Cdd:PRK13644 230 -TLG 232
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
5-220 |
2.14e-18 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 83.63 E-value: 2.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 5 KEILLKVSGLKVAYGgiQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQG 84
Cdd:PRK10982 247 GEVILEVRNLTSLRQ--PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHG 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 85 LVMVPEGR---GTFTRMTITENLL---MGAYIRD----DKAQIEADIERIFGIFpRLKERRNQLA-GTMSGGEQQMLAMG 153
Cdd:PRK10982 325 FALVTEERrstGIYAYLDIGFNSLisnIRNYKNKvgllDNSRMKSDTQWVIDSM-RVKTPGHRTQiGSLSGGNQQKVIIG 403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032805432 154 RALMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESGLIT 220
Cdd:PRK10982 404 RWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVA 470
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
9-217 |
2.24e-18 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 81.45 E-value: 2.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGG----IQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAwdlvKQG 84
Cdd:COG4525 4 LTVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGA----DRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 85 LVMVPEGrgTFTRMTITENLLMGAYIRD-DKAQIEADIERIFGIFpRLKERRNQLAGTMSGGEQQMLAMGRALMTRPKVL 163
Cdd:COG4525 80 VVFQKDA--LLPWLNVLDNVAFGLRLRGvPKAERRARAEELLALV-GLADFARRRIWQLSGGMRQRVGIARALAADPRFL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2032805432 164 LLDEPSMGLSPIMVDKIFEVVNDI-HSQGVTVLLVEQNASRALQLASRGYVMESG 217
Cdd:COG4525 157 LMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITHSVEEALFLATRLVVMSPG 211
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
11-168 |
2.87e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 83.19 E-value: 2.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 11 VSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIeFMGKTLK------------GQGAW 78
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV-SIPKGLRigylpqepplddDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 79 DLVKQGLV----MVPEGRGTFTRMTITENLL------------MGAYirddkaQIEADIERI---FGIFPrlkERRNQLA 139
Cdd:COG0488 80 DTVLDGDAelraLEAELEELEAKLAEPDEDLerlaelqeefeaLGGW------EAEARAEEIlsgLGFPE---EDLDRPV 150
|
170 180
....*....|....*....|....*....
gi 2032805432 140 GTMSGGEQQMLAMGRALMTRPKVLLLDEP 168
Cdd:COG0488 151 SELSGGWRRRVALARALLSEPDLLLLDEP 179
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-197 |
2.87e-18 |
|
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: 83.18 E-value: 2.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 4 SKEILLKVSGLKVAYGGIQAV-KGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIefmgkTLKGQGAW---- 78
Cdd:TIGR02868 330 LGKPTLELRDLSAGYPGAPPVlDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEV-----TLDGVPVSsldq 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 79 DLVKQGLVMVPEGRGTFTrMTITENLLMGAYIRDDkAQIEADIERIfGIFPRLKERRNQL-------AGTMSGGEQQMLA 151
Cdd:TIGR02868 405 DEVRRRVSVCAQDAHLFD-TTVRENLRLARPDATD-EELWAALERV-GLADWLRALPDGLdtvlgegGARLSGGERQRLA 481
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2032805432 152 MGRALMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIhSQGVTVLLV 197
Cdd:TIGR02868 482 LARALLADAPILLLDEPTEHLDAETADELLEDLLAA-LSGRTVVLI 526
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
19-233 |
2.91e-18 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 82.05 E-value: 2.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 19 GGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVK--QGLVMVPEGRGTFT 96
Cdd:COG1135 16 GPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAarRKIGMIFQHFNLLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 97 RMTITENL-----LMGAyirdDKAQIEADIERIF---GifprLKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLLDEP 168
Cdd:COG1135 96 SRTVAENValpleIAGV----PKAEIRKRVAELLelvG----LSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2032805432 169 SMGLSPIMVDKIFEVVNDIHSQ-GVTVLLV--EQNASRalQLASRGYVMESGLITMTGEGKTLLNDPK 233
Cdd:COG1135 168 TSALDPETTRSILDLLKDINRElGLTIVLIthEMDVVR--RICDRVAVLENGRIVEQGPVLDVFANPQ 233
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-241 |
3.15e-18 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 82.30 E-value: 3.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 4 SKEILLKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIefmgkTLKGQGAWDLvkq 83
Cdd:PRK09452 10 SLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRI-----MLDGQDITHV--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 84 glvmVPEGR---------GTFTRMTITENLLMGayIRDDKAQiEADIErifgifPRLKE--RRNQLAGT-------MSGG 145
Cdd:PRK09452 82 ----PAENRhvntvfqsyALFPHMTVFENVAFG--LRMQKTP-AAEIT------PRVMEalRMVQLEEFaqrkphqLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 146 EQQMLAMGRALMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQ-GVTVLLVEQNASRALQLASRGYVMESGLITMTGE 224
Cdd:PRK09452 149 QQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
250
....*....|....*....
gi 2032805432 225 GKTLLNDPKVR--AAYLGE 241
Cdd:PRK09452 229 PREIYEEPKNLfvARFIGE 247
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
21-195 |
6.66e-18 |
|
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: 79.40 E-value: 6.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 21 IQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFmgktlKGQGAW-DLVK----------------- 82
Cdd:COG4778 24 LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILV-----RHDGGWvDLAQaspreilalrrrtigyv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 83 -QGLVMVPegRGTfTRMTITENLL-MGayIRDDKAQIEAdiERIFGIFpRLKERRNQLA-GTMSGGEQQMLAMGRALMTR 159
Cdd:COG4778 99 sQFLRVIP--RVS-ALDVVAEPLLeRG--VDREEARARA--RELLARL-NLPERLWDLPpATFSGGEQQRVNIARGFIAD 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 2032805432 160 PKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQGVTVL 195
Cdd:COG4778 171 PPLLLLDEPTASLDAANRAVVVELIEEAKARGTAII 206
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
9-197 |
7.68e-18 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 78.68 E-value: 7.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTG-LQPV--AAGEIEFMGKTLKGqgawdlvkqgl 85
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAfsASGEVLLNGRRLTA----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 86 vMVPEGRGT---------FTRMTITENLLMG--AYI--RDDKAQIEADIERIfgifpRLKERRNQLAGTMSGGEQQMLAM 152
Cdd:COG4136 71 -LPAEQRRIgilfqddllFPHLSVGENLAFAlpPTIgrAQRRARVEQALEEA-----GLAGFADRDPATLSGGQRARVAL 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2032805432 153 GRALMTRPKVLLLDEPSMGLSPIMVDKIFE-VVNDIHSQGVTVLLV 197
Cdd:COG4136 145 LRALLAEPRALLLDEPFSKLDAALRAQFREfVFEQIRQRGIPALLV 190
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
8-232 |
1.09e-17 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 79.58 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 8 LLKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKT---------------L 72
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrdlyalseaerrR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 73 KGQGAWDLVKQ----GLvmvpegrgtftRMTITE--NL---LMGA----Y--IRDDKAQ----IEADIERIfgifprlke 133
Cdd:PRK11701 86 LLRTEWGFVHQhprdGL-----------RMQVSAggNIgerLMAVgarhYgdIRATAGDwlerVEIDAARI--------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 134 rrNQLAGTMSGGEQQMLAMGRALMTRPKVLLLDEPSMGL----SPIMVDKIFEVVNDIhsqGVTVLLVEQNASRALQLAS 209
Cdd:PRK11701 146 --DDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLdvsvQARLLDLLRGLVREL---GLAVVIVTHDLAVARLLAH 220
|
250 260
....*....|....*....|...
gi 2032805432 210 RGYVMESGLITMTGEGKTLLNDP 232
Cdd:PRK11701 221 RLLVMKQGRVVESGLTDQVLDDP 243
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
8-196 |
1.21e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 78.07 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 8 LLKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAwdLVKQGLVM 87
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLC--TYQKQLCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 88 VPEGRGTFTRMTITENLLMGAYIRDDKAQIEaDIERIFgifpRLKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLLDE 167
Cdd:PRK13540 79 VGHRSGINPYLTLRENCLYDIHFSPGAVGIT-ELCRLF----SLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDE 153
|
170 180
....*....|....*....|....*....
gi 2032805432 168 PSMGLSPIMVDKIFEVVNDIHSQGVTVLL 196
Cdd:PRK13540 154 PLVALDELSLLTIITKIQEHRAKGGAVLL 182
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
21-210 |
1.31e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 78.67 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 21 IQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTL-----KGQGAW-----DLVKQGLVMVPE 90
Cdd:PRK10584 23 LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhqmdeEARAKLrakhvGFVFQSFMLIPT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 91 grgtftrMTITEN-----LLMGAYIRDDKAQIEADIERIfgifpRLKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLL 165
Cdd:PRK10584 103 -------LNALENvelpaLLRGESSRQSRNGAKALLEQL-----GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2032805432 166 DEPSMGLSPIMVDKIFEVVNDI-HSQGVTVLLVEQNAsralQLASR 210
Cdd:PRK10584 171 DEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDL----QLAAR 212
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
9-217 |
2.72e-17 |
|
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: 76.49 E-value: 2.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGGIQA--VKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKgQGAWDLVKQGLV 86
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADIS-QWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 87 MVPEGRGTFTRmTITENLLmgayirddkaqieadierifgifprlkerrnqlagtmSGGEQQMLAMGRALMTRPKVLLLD 166
Cdd:cd03246 80 YLPQDDELFSG-SIAENIL-------------------------------------SGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2032805432 167 EPSMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQNASrALQLASRGYVMESG 217
Cdd:cd03246 122 EPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPE-TLASADRILVLEDG 171
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
24-210 |
3.02e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 77.93 E-value: 3.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 24 VKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGA---WDLVKQGLVMVPEGRGTFTRMTI 100
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakAELRNQKLGFIYQFHHLLPDFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 101 TEN----LLMGAYIRDDKAQIEADIERIFGIFPRLKERRNQLagtmSGGEQQMLAMGRALMTRPKVLLLDEPSMGLSPIM 176
Cdd:PRK11629 105 LENvampLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSEL----SGGERQRVAIARALVNNPRLVLADEPTGNLDARN 180
|
170 180 190
....*....|....*....|....*....|....
gi 2032805432 177 VDKIFEVVNDIHSQGVTVLLVeqnASRALQLASR 210
Cdd:PRK11629 181 ADSIFQLLGELNRLQGTAFLV---VTHDLQLAKR 211
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
17-240 |
3.41e-17 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 79.30 E-value: 3.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 17 AYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIeFMGktlkGQGAWDL--VKQGLVMVPEGRGT 94
Cdd:PRK11000 12 AYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDL-FIG----EKRMNDVppAERGVGMVFQSYAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 95 FTRMTITENLLMGAYI-RDDKAQIEADIERIFGI--FPRLKERRNQlagTMSGGEQQMLAMGRALMTRPKVLLLDEPsmg 171
Cdd:PRK11000 87 YPHLSVAENMSFGLKLaGAKKEEINQRVNQVAEVlqLAHLLDRKPK---ALSGGQRQRVAIGRTLVAEPSVFLLDEP--- 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032805432 172 LSPImvDKIFEV-----VNDIHSQ-GVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLNDPKVR--AAYLG 240
Cdd:PRK11000 161 LSNL--DAALRVqmrieISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRfvAGFIG 235
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1-233 |
3.57e-17 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 78.98 E-value: 3.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 1 MADSKEILLKVSGLKVAYG-------------GIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEF 67
Cdd:PRK15079 1 VTEGKKVLLEVADLKVHFDikdgkqwfwqppkTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 68 MGKTLKGQGA--WDLVKQGLVMV---------PegrgtftRMTITENL---LMGAYIRDDKAQIEADIERIF---GIFPR 130
Cdd:PRK15079 81 LGKDLLGMKDdeWRAVRSDIQMIfqdplaslnP-------RMTIGEIIaepLRTYHPKLSRQEVKDRVKAMMlkvGLLPN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 131 LKerrNQLAGTMSGGEQQMLAMGRALMTRPKVLLLDEPsmgLSPIMVDKIFEVVNDIHS----QGVTVLLVEQNASRALQ 206
Cdd:PRK15079 154 LI---NRYPHEFSGGQCQRIGIARALILEPKLIICDEP---VSALDVSIQAQVVNLLQQlqreMGLSLIFIAHDLAVVKH 227
|
250 260
....*....|....*....|....*..
gi 2032805432 207 LASRGYVMESGLITMTGEGKTLLNDPK 233
Cdd:PRK15079 228 ISDRVLVMYLGHAVELGTYDEVYHNPL 254
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
9-230 |
4.73e-17 |
|
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: 79.78 E-value: 4.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYG-GIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLvKQGLVM 87
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTL-RQFINY 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 88 VPEGRGTFTRmTITENLLMGAY--IRDDK-------AQIEADIERI-FGIFPRLKERrnqlAGTMSGGEQQMLAMGRALM 157
Cdd:TIGR01193 553 LPQEPYIFSG-SILENLLLGAKenVSQDEiwaaceiAEIKDDIENMpLGYQTELSEE----GSSISGGQKQRIALARALL 627
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032805432 158 TRPKVLLLDEPSMGLSPIMVDKIFEvvNDIHSQGVTVLLVEQNASRAlQLASRGYVMESGLITMTGEGKTLLN 230
Cdd:TIGR01193 628 TDSKVLILDESTSNLDTITEKKIVN--NLLNLQDKTIIFVAHRLSVA-KQSDKIIVLDHGKIIEQGSHDELLD 697
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-233 |
4.76e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 78.21 E-value: 4.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 3 DSKEILLKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGeIEFMGKTLKGQGAWDLVK 82
Cdd:PRK14271 16 DAAAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG-YRYSGDVLLGGRSIFNYR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 83 QGLVMVPEGRGTFTR-----MTITENLLMGAYI------RDDKAQIEADIERIfGIFPRLKERRNQLAGTMSGGEQQMLA 151
Cdd:PRK14271 95 DVLEFRRRVGMLFQRpnpfpMSIMDNVLAGVRAhklvprKEFRGVAQARLTEV-GLWDAVKDRLSDSPFRLSGGQQQLLC 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 152 MGRALMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQgVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLND 231
Cdd:PRK14271 174 LARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSS 252
|
..
gi 2032805432 232 PK 233
Cdd:PRK14271 253 PK 254
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-233 |
4.95e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 77.78 E-value: 4.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 4 SKEILLKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLK-GQGAWDL-- 80
Cdd:PRK14246 6 SAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfGKDIFQIda 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 81 --VKQGLVMVPEGRGTFTRMTITENLL--MGAYIRDDKAQIEADIE---RIFGIFPRLKERRNQLAGTMSGGEQQMLAMG 153
Cdd:PRK14246 86 ikLRKEVGMVFQQPNPFPHLSIYDNIAypLKSHGIKEKREIKKIVEeclRKVGLWKEVYDRLNSPASQLSGGQQQRLTIA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 154 RALMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQgVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLNDPK 233
Cdd:PRK14246 166 RALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPK 244
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
19-223 |
1.04e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 77.15 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 19 GGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVK-QGLVMVPEGRGTFTR 97
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKfVGLVFQNPDDQIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 98 mTITENLLMGAY-IRDDKAQIEADIERIFGIFPrLKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLLDEPSMGLSPIM 176
Cdd:PRK13652 95 -TVEQDIAFGPInLGLDEETVAHRVSSALHMLG-LEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2032805432 177 VDKIFEVVNDI-HSQGVTVLLVEQNASRALQLASRGYVMESGLITMTG 223
Cdd:PRK13652 173 VKELIDFLNDLpETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYG 220
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
9-231 |
2.48e-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: 74.49 E-value: 2.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQ--PVAAGEIEFMGKTLkgqgawdlvkqglv 86
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDI-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 87 mvpegrgtfTRMTITENLLMGAYIrddKAQIEADIErifGIfpRLKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLLD 166
Cdd:cd03217 67 ---------TDLPPEERARLGIFL---AFQYPPEIP---GV--KNADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILD 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2032805432 167 EPSMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQNASRALQL-ASRGYVMESGLITMTGeGKTLLND 231
Cdd:cd03217 130 EPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG-DKELALE 194
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
22-223 |
4.53e-16 |
|
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: 74.23 E-value: 4.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 22 QAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAA---GEIEFMGKTLKGqgawDLVKQGLVMVPEGRGTFTRM 98
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKP----DQFQKCVAYVRQDDILLPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 99 TITENLLMGAYIR----DDKAQIEADIErifgiFPRLKE-----RRNQLAGTMSGGEQQMLAMGRALMTRPKVLLLDEPS 169
Cdd:cd03234 97 TVRETLTYTAILRlprkSSDAIRKKRVE-----DVLLRDlaltrIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2032805432 170 MGLSPIMVDKIFEVVNDIHSQGVTVLL-VEQNASRALQLASRGYVMESGLITMTG 223
Cdd:cd03234 172 SGLDSFTALNLVSTLSQLARRNRIVILtIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
17-220 |
6.18e-16 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 76.36 E-value: 6.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 17 AY-GGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKgqgAWDL--VKQGLVMVPEGRG 93
Cdd:COG1132 348 SYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIR---DLTLesLRRQIGVVPQDTF 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 94 TFTRmTITENLLMG------AYIRD--DKAQIEADIERifgiFP-----RLKERrnqlAGTMSGGEQQMLAMGRALMTRP 160
Cdd:COG1132 425 LFSG-TIRENIRYGrpdatdEEVEEaaKAAQAHEFIEA----LPdgydtVVGER----GVNLSGGQRQRIAIARALLKDP 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032805432 161 KVLLLDEPSMGLSPIMVDKIFEVVNDIhSQGVTVLLVeqnASR--ALQLASRGYVMESGLIT 220
Cdd:COG1132 496 PILILDEATSALDTETEALIQEALERL-MKGRTTIVI---AHRlsTIRNADRILVLDDGRIV 553
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
9-219 |
8.98e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 74.33 E-value: 8.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIefmgktLKGQGAWDLVKQGL-VM 87
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL------LAGTAPLAEAREDTrLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 88 VPEGRgTFTRMTITENL---LMGAYiRDDKAQIEADIErifgifprLKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLL 164
Cdd:PRK11247 87 FQDAR-LLPWKKVIDNVglgLKGQW-RDAALQALAAVG--------LADRANEWPAALSGGQKQRVALARALIHRPGLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2032805432 165 LDEPSMGLSPI----MVDKIfevVNDIHSQGVTVLLVEQNASRALQLASRGYVMESGLI 219
Cdd:PRK11247 157 LDEPLGALDALtrieMQDLI---ESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
8-234 |
9.63e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 74.50 E-value: 9.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 8 LLKVSGLKVAYG-GIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLkgqgawDLVKQGLV 86
Cdd:PRK13636 5 ILKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI------DYSRKGLM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 87 MVPEGRGTFtrMTITENLLMGAYIRDD-----------KAQIEADIERIF---GIFPrlkeRRNQLAGTMSGGEQQMLAM 152
Cdd:PRK13636 79 KLRESVGMV--FQDPDNQLFSASVYQDvsfgavnlklpEDEVRKRVDNALkrtGIEH----LKDKPTHCLSFGQKKRVAI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 153 GRALMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQ-GVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLND 231
Cdd:PRK13636 153 AGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
...
gi 2032805432 232 PKV 234
Cdd:PRK13636 233 KEM 235
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
8-209 |
2.08e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 73.20 E-value: 2.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 8 LLKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAwdlvKQGLVM 87
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA----ERGVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 88 VPEgrGTFTRMTITENLLMGAYIRD-DKAQIEADIERIFGIFPrLKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLLD 166
Cdd:PRK11248 77 QNE--GLLPWRNVQDNVAFGLQLAGvEKMQRLEIAHQMLKKVG-LEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLD 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2032805432 167 EPSMGLSPIMVDKIFEVVNDI-HSQGVTVLLVEQNASRALQLAS 209
Cdd:PRK11248 154 EPFGALDAFTREQMQTLLLKLwQETGKQVLLITHDIEEAVFMAT 197
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
22-223 |
2.88e-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: 71.19 E-value: 2.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 22 QAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTG-LQPvAAGEIEFMGKTLkgQGAWDLVKQGLVMVPEGRGTFTrMTI 100
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGdLKP-QQGEITLDGVPV--SDLEKALSSLISVLNQRPYLFD-TTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 101 TENLlmgayirddkaqieadierifgifprlkERRnqlagtMSGGEQQMLAMGRALMTRPKVLLLDEPSMGLSPIMVDKI 180
Cdd:cd03247 92 RNNL----------------------------GRR------FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQL 137
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2032805432 181 FEVVNDiHSQGVTVLLVEQNAsRALQLASRGYVMESGLITMTG 223
Cdd:cd03247 138 LSLIFE-VLKDKTLIWITHHL-TGIEHMDKILFLENGKIIMQG 178
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
9-241 |
2.88e-15 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 74.00 E-value: 2.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAageiefmGKTLKGQGAWDLVKQGLVMV 88
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDA-------GRRPWRF*TWCANRRALRRT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 89 -----PEGRGTFTRMTITENLLM-GAYI----RDDKAQIEADIERIfgifpRLKERRNQLAGTMSGGEQQMLAMGRALMT 158
Cdd:NF000106 87 ig*hrPVR*GRRESFSGRENLYMiGR*LdlsrKDARARADELLERF-----SLTEAAGRAAAKYSGGMRRRLDLAASMIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 159 RPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESGLITMTGE---------GKTLl 229
Cdd:NF000106 162 RPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKvdelktkvgGRTL- 240
|
250
....*....|..
gi 2032805432 230 ndpKVRAAYLGE 241
Cdd:NF000106 241 ---QIRPAHAAE 249
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-217 |
3.93e-15 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 74.00 E-value: 3.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 20 GIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQGLVMVPEGRGTFTRMT 99
Cdd:PRK10982 10 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQELNLVLQRS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 100 ITENLLMGAYIRD----DKAQIEADIERIFG-----IFPRLKerrnqlAGTMSGGEQQMLAMGRALMTRPKVLLLDEPSM 170
Cdd:PRK10982 90 VMDNMWLGRYPTKgmfvDQDKMYRDTKAIFDeldidIDPRAK------VATLSVSQMQMIEIAKAFSYNAKIVIMDEPTS 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2032805432 171 GLSPIMVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESG 217
Cdd:PRK10982 164 SLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
9-172 |
4.99e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 71.06 E-value: 4.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIefmgkTLKGQGAWDLVKQGLV-- 86
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTI-----KLDGGDIDDPDVAEAChy 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 87 ------MVPEgrgtftrMTITENLLMGAYIR-DDKAQIEADIERiFGIfPRLKERRnqlAGTMSGGEQQMLAMGRALMTR 159
Cdd:PRK13539 78 lghrnaMKPA-------LTVAENLEFWAAFLgGEELDIAAALEA-VGL-APLAHLP---FGYLSAGQKRRVALARLLVSN 145
|
170
....*....|...
gi 2032805432 160 PKVLLLDEPSMGL 172
Cdd:PRK13539 146 RPIWILDEPTAAL 158
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
8-219 |
5.03e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 72.43 E-value: 5.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 8 LLKVSGLKVAY---GGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQG 84
Cdd:PRK13642 4 ILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 85 LVMVPEGRGTFTRMTITENLLMGayIRDDKAQIEADIERIFG--IFPRLKERRNQLAGTMSGGEQQMLAMGRALMTRPKV 162
Cdd:PRK13642 84 GMVFQNPDNQFVGATVEDDVAFG--MENQGIPREEMIKRVDEalLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2032805432 163 LLLDEPSMGLSPIMVDKIFEVVNDIHSQ-GVTVLLVEQNASRALQlASRGYVMESGLI 219
Cdd:PRK13642 162 IILDESTSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEI 218
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
23-224 |
6.37e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 72.39 E-value: 6.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 23 AVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGA--WDLVKQ-GLVM-VPEGRgtFTRM 98
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVklSDIRKKvGLVFqYPEYQ--LFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 99 TITENLLMGAYIRD-DKAQIEADIER---IFGI-FPRLKERRnqlAGTMSGGEQQMLAMGRALMTRPKVLLLDEPSMGLS 173
Cdd:PRK13637 100 TIEKDIAFGPINLGlSEEEIENRVKRamnIVGLdYEDYKDKS---PFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2032805432 174 PIMVDKIFEVVNDIHSQ-GVTVLLVEQNASRALQLASRGYVMESGLITMTGE 224
Cdd:PRK13637 177 PKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGT 228
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
23-229 |
8.34e-15 |
|
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: 71.36 E-value: 8.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 23 AVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLK-GQGAWDLVKQGLVMvpegrgtftrmtiT 101
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLAlADPAWLRRQVGVVL-------------Q 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 102 ENLLMGAYIRDDKAQIE--ADIERIF---------GIFPRLKERRNQLAG----TMSGGEQQMLAMGRALMTRPKVLLLD 166
Cdd:cd03252 84 ENVLFNRSIRDNIALADpgMSMERVIeaaklagahDFISELPEGYDTIVGeqgaGLSGGQRQRIAIARALIHNPRILIFD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032805432 167 EPSMGLSPIMVDKIFEVVNDIhSQGVTVLLVEQNASrALQLASRGYVMESGLITMTGEGKTLL 229
Cdd:cd03252 164 EATSALDYESEHAIMRNMHDI-CAGRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDELL 224
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
21-223 |
1.10e-14 |
|
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: 70.70 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 21 IQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLvKQGLVMVPEGRGTFTRmTI 100
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL-RRNIGYVPQDVTLFYG-TL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 101 TENLLMGAYIRDDKAQIEAdiERIFGIFP-----------RLKERRNQLagtmSGGEQQMLAMGRALMTRPKVLLLDEPS 169
Cdd:cd03245 95 RDNITLGAPLADDERILRA--AELAGVTDfvnkhpngldlQIGERGRGL----SGGQRQAVALARALLNDPPILLLDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2032805432 170 MGLSPIMVDKIFEVVNDIHSqGVTVLLVEQNASrALQLASRGYVMESGLITMTG 223
Cdd:cd03245 169 SAMDMNSEERLKERLRQLLG-DKTLIIITHRPS-LLDLVDRIIVMDSGRIVADG 220
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
24-211 |
1.30e-14 |
|
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: 69.10 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 24 VKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFmgktlkgqgawdLVKQGLVMVPEgRGTFTRMTITEN 103
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM------------PEGEDLLFLPQ-RPYLPLGTLREQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 104 LlmgAYIRDDkaqieadierifgifprlkerrnqlagTMSGGEQQMLAMGRALMTRPKVLLLDEPSMGLSPIMVDKIFEV 183
Cdd:cd03223 84 L---IYPWDD---------------------------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQL 133
|
170 180 190
....*....|....*....|....*....|....
gi 2032805432 184 VNDihsQGVTVLLV------EQNASRALQLASRG 211
Cdd:cd03223 134 LKE---LGITVISVghrpslWKFHDRVLDLDGEG 164
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
8-233 |
1.53e-14 |
|
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: 72.41 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 8 LLKVSGLKVAYGG----IQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQP----VAAGEIEFMGKTLKGQGAWD 79
Cdd:COG4172 6 LLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPdpaaHPSGSILFDGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 80 LvkQGL-----VMV---PegrgtftrMT-----------ITENLLMGAYIRDDKAQIEA----------DIERIFGIFPr 130
Cdd:COG4172 86 L--RRIrgnriAMIfqeP--------MTslnplhtigkqIAEVLRLHRGLSGAAARARAlellervgipDPERRLDAYP- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 131 lkerrNQLagtmSGGEQQ--MLAMgrALMTRPKVLLLDEPSMGLspimvD-----KIFEVVNDI-HSQGVTVLLVEQNAS 202
Cdd:COG4172 155 -----HQL----SGGQRQrvMIAM--ALANEPDLLIADEPTTAL-----DvtvqaQILDLLKDLqRELGMALLLITHDLG 218
|
250 260 270
....*....|....*....|....*....|.
gi 2032805432 203 RALQLASRGYVMESGLITMTGEGKTLLNDPK 233
Cdd:COG4172 219 VVRRFADRVAVMRQGEIVEQGPTAELFAAPQ 249
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
22-241 |
2.15e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 70.63 E-value: 2.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 22 QAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQ----GAWDLVKQ-GLVM-VPEGRgtF 95
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPEtgnkNLKKLRKKvSLVFqFPEAQ--L 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 96 TRMTITENLLMGAY---IRDDKAQIEAD--IERIfGIFPRLKERRnqlAGTMSGGEQQMLAMGRALMTRPKVLLLDEPSM 170
Cdd:PRK13641 99 FENTVLKDVEFGPKnfgFSEDEAKEKALkwLKKV-GLSEDLISKS---PFELSGGQMRRVAIAGVMAYEPEILCLDEPAA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032805432 171 GLSPIMVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLNDPK-VRAAYLGE 241
Cdd:PRK13641 175 GLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEwLKKHYLDE 246
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
9-167 |
2.54e-14 |
|
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: 69.36 E-value: 2.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGG--IQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLvKQGLV 86
Cdd:cd03369 7 IEVENLSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL-RSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 87 MVPEGRGTFTRmTITENLlmgayirdDKAQIEADIErIFGIFpRLKERRNQLagtmSGGEQQMLAMGRALMTRPKVLLLD 166
Cdd:cd03369 86 IIPQDPTLFSG-TIRSNL--------DPFDEYSDEE-IYGAL-RVSEGGLNL----SQGQRQLLCLARALLKRPRVLVLD 150
|
.
gi 2032805432 167 E 167
Cdd:cd03369 151 E 151
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
9-240 |
2.86e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 70.30 E-value: 2.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAY-GGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKgqgawDLVKQGLVM 87
Cdd:PRK15056 7 IVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR-----QALQKNLVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 88 -VPEGRG---TFTrMTITENLLMGAY---------IRDDKAQIEADIERIfgifpRLKERRNQLAGTMSGGEQQMLAMGR 154
Cdd:PRK15056 82 yVPQSEEvdwSFP-VLVEDVVMMGRYghmgwlrraKKRDRQIVTAALARV-----DMVEFRHRQIGELSGGQKKRVFLAR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 155 ALMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGyVMESGLITMTGEGKTLLNDPKV 234
Cdd:PRK15056 156 AIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYT-VMVKGTVLASGPTETTFTAENL 234
|
....*.
gi 2032805432 235 RAAYLG 240
Cdd:PRK15056 235 ELAFSG 240
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
22-223 |
2.99e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 70.53 E-value: 2.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 22 QAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGL-QP----VAAGEIEFMGKTLKGQGAWDLVKQGLVM-VPEGRgtF 95
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLlQPtegkVTVGDIVVSSTSKQKEIKPVRKKVGVVFqFPESQ--L 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 96 TRMTITENLLMG----AYIRDDKAQIEADIERIFGIFPRLKERRnqlAGTMSGGEQQMLAMGRALMTRPKVLLLDEPSMG 171
Cdd:PRK13643 98 FEETVLKDVAFGpqnfGIPKEKAEKIAAEKLEMVGLADEFWEKS---PFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2032805432 172 LSPIMVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESGLITMTG 223
Cdd:PRK13643 175 LDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCG 226
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
8-224 |
3.86e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 70.04 E-value: 3.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 8 LLKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLkgqgawDLVKQGLVM 87
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL------DYSKRGLLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 88 V----------PEGRGTFTrmTITENLlmgAYIRDDKAQIEADIERifgifpRLKER---------RNQLAGTMSGGEQQ 148
Cdd:PRK13638 75 LrqqvatvfqdPEQQIFYT--DIDSDI---AFSLRNLGVPEAEITR------RVDEAltlvdaqhfRHQPIQCLSHGQKK 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2032805432 149 MLAMGRALMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESGLITMTGE 224
Cdd:PRK13638 144 RVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGA 219
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
19-167 |
5.17e-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: 68.79 E-value: 5.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 19 GGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKgQGAWDLVKQGLVMVPEGRGTFTRm 98
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIR-DISRKSLRSMIGVVLQDTFLFSG- 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032805432 99 TITENLLMGA-YIRDDKAQIEADIERIFGIFPRLKE----RRNQLAGTMSGGEQQMLAMGRALMTRPKVLLLDE 167
Cdd:cd03254 92 TIMENIRLGRpNATDEEVIEAAKEAGAHDFIMKLPNgydtVLGENGGNLSQGERQLLAIARAMLRDPKILILDE 165
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
24-217 |
6.74e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 69.38 E-value: 6.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 24 VKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLvKQGLVMVPEGrgtftrmtiTEN 103
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDI-RHKIGMVFQN---------PDN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 104 LLMGAYIRDDKAqieadieriFGI------FPRLKERRNQ---LAGTM----------SGGEQQMLAMGRALMTRPKVLL 164
Cdd:PRK13650 93 QFVGATVEDDVA---------FGLenkgipHEEMKERVNEaleLVGMQdfkereparlSGGQKQRVAIAGAVAMRPKIII 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2032805432 165 LDEPSMGLSPIMVDKIFEVVNDIHSQ-GVTVLLVEQNASRaLQLASRGYVMESG 217
Cdd:PRK13650 164 LDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDE-VALSDRVLVMKNG 216
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-234 |
7.49e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 68.86 E-value: 7.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 3 DSKEILLKVSGLKVAYGGIQ--AVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDL 80
Cdd:PRK13632 2 KNKSVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 81 VKQ-GLVmvpegrgtFTRmtiTENLLMGAYIRDDKA--------------QIEADIERIFGIFPRLKERRNQLagtmSGG 145
Cdd:PRK13632 82 RKKiGII--------FQN---PDNQFIGATVEDDIAfglenkkvppkkmkDIIDDLAKKVGMEDYLDKEPQNL----SGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 146 EQQMLAMGRALMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQGV-TVLLVEQNASRALqLASRGYVMESGLITMTGE 224
Cdd:PRK13632 147 QKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAI-LADKVIVFSEGKLIAQGK 225
|
250
....*....|
gi 2032805432 225 GKTLLNDPKV 234
Cdd:PRK13632 226 PKEILNNKEI 235
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
9-229 |
9.62e-14 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 68.17 E-value: 9.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGL--QPVAAGEIEFMGKTLKGQGAWDLVKQGLV 86
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPDERARAGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 87 MV----PEGRG----TFTRMTITENLLMGAYIRDDKAQIEADIERIfGIFPRLKERrnQLAGTMSGGEQ------QMLAM 152
Cdd:COG0396 81 LAfqypVEIPGvsvsNFLRTALNARRGEELSAREFLKLLKEKMKEL-GLDEDFLDR--YVNEGFSGGEKkrneilQMLLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 153 gralmtRPKVLLLDEPSMGLSpimVD---KIFEVVNDIHSQGVTVLLVEQNAsRALQL--ASRGYVMESGLITMTGeGKT 227
Cdd:COG0396 158 ------EPKLAILDETDSGLD---IDalrIVAEGVNKLRSPDRGILIITHYQ-RILDYikPDFVHVLVDGRIVKSG-GKE 226
|
..
gi 2032805432 228 LL 229
Cdd:COG0396 227 LA 228
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
22-217 |
1.33e-13 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 69.60 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 22 QAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIefmgkTLKGQGAWDLVKQGL----VMVPEGRGTFTR 97
Cdd:PRK13657 349 QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRI-----LIDGTDIRTVTRASLrrniAVVFQDAGLFNR 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 98 mTITENLLMG------AYIRD--DKAQIEADIER-IFGIFPRLKERRNQLagtmSGGEQQMLAMGRALMTRPKVLLLDEP 168
Cdd:PRK13657 424 -SIEDNIRVGrpdatdEEMRAaaERAQAHDFIERkPDGYDTVVGERGRQL----SGGERQRLAIARALLKDPPILILDEA 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2032805432 169 SMGLSPIMVDKIFEVVNDIhSQGVTVLLVE------QNASRALQLaSRGYVMESG 217
Cdd:PRK13657 499 TSALDVETEAKVKAALDEL-MKGRTTFIIAhrlstvRNADRILVF-DNGRVVESG 551
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
24-197 |
1.69e-13 |
|
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: 66.81 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 24 VKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAA--GEIEFMGKTLKGqgawDLVKQGLVMVPEGRGTFTRMTIT 101
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLDK----RSFRKIIGYVPQDDILHPTLTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 102 ENLLMGAYIRddkaqieadierifGIfprlkerrnqlagtmSGGEQQMLAMGRALMTRPKVLLLDEPSMGLSPIMVDKIF 181
Cdd:cd03213 101 ETLMFAAKLR--------------GL---------------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVM 151
|
170
....*....|....*.
gi 2032805432 182 EVVNDIHSQGVTVLLV 197
Cdd:cd03213 152 SLLRRLADTGRTIICS 167
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
8-235 |
1.87e-13 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 67.87 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 8 LLKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDL--VKQGL 85
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 86 VMVPEGRGTFTRMTITENLlmgAYIRDDKAQIEADIERIFGIFPR----LKERRNQLAGTMSGGEQQMLAMGRALMTRPK 161
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNV---AYPLREHTQLPAPLLHSTVMMKLeavgLRGAAKLMPSELSGGMARRAALARAIALEPD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032805432 162 VLLLDEPSMGLSPIMVDKIFEVVNDI-HSQGVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLN--DPKVR 235
Cdd:PRK11831 164 LIMFDEPFVGQDPITMGVLVKLISELnSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQAnpDPRVR 240
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
20-167 |
2.19e-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: 2.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 20 GIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQ-GLVmvpEGRGTFTRM 98
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQiGLV---SQEPVLFDG 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2032805432 99 TITENLLMGAYIRDDKAQIEA----DIERIFGIFP-----RLKERRNQLagtmSGGEQQMLAMGRALMTRPKVLLLDE 167
Cdd:cd03249 92 TIAENIRYGKPDATDEEVEEAakkaNIHDFIMSLPdgydtLVGERGSQL----SGGQKQRIAIARALLRNPKILLLDE 165
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
15-197 |
2.72e-13 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 67.90 E-value: 2.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 15 KVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVK--QGLVMVPEGR 92
Cdd:PRK11153 12 PQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKarRQIGMIFQHF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 93 GTFTRMTITENL-----LMGAyirdDKAQIEAdieRIFGIFPR--LKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLL 165
Cdd:PRK11153 92 NLLSSRTVFDNValpleLAGT----PKAEIKA---RVTELLELvgLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLC 164
|
170 180 190
....*....|....*....|....*....|...
gi 2032805432 166 DEPSMGLSPIMVDKIFEVVNDIHSQ-GVTVLLV 197
Cdd:PRK11153 165 DEATSALDPATTRSILELLKDINRElGLTIVLI 197
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
12-219 |
2.85e-13 |
|
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: 67.52 E-value: 2.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 12 SGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGK---TLKGQGAWDLVKQGLVMV 88
Cdd:TIGR02769 15 GGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQdlyQLDRKQRRAFRRDVQLVF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 89 PEGRGTFT-RMTITENLL--MGAYIRDDKAQIEADIERIFGIFPRLKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLL 165
Cdd:TIGR02769 95 QDSPSAVNpRMTVRQIIGepLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2032805432 166 DEPSMGLSPIMVDKIFEVVNDIHSQ-GVTVLLVEQNASRALQLASRGYVMESGLI 219
Cdd:TIGR02769 175 DEAVSNLDMVLQAVILELLRKLQQAfGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
23-175 |
2.91e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 68.61 E-value: 2.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 23 AVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLkgqGAWDLVkqglvmvpegrgtfTRM---- 98
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---DAGDIA--------------TRRrvgy 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 99 -----------TITENLLMGAYI-----RDDKAQIEADIERiFGifprLKERRNQLAGTMSGGEQQMLAMGRALMTRPKV 162
Cdd:NF033858 344 msqafslygelTVRQNLELHARLfhlpaAEIAARVAEMLER-FD----LADVADALPDSLPLGIRQRLSLAVAVIHKPEL 418
|
170
....*....|...
gi 2032805432 163 LLLDEPSMGLSPI 175
Cdd:NF033858 419 LILDEPTSGVDPV 431
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
10-168 |
3.55e-13 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 66.65 E-value: 3.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 10 KVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQgLVMVP 89
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKR-LAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 90 EGRGTFTRMTITEnLLM--------GAYIRDDKAQIEADIERiFGifprLKERRNQLAGTMSGGEQQM--LAMGRALMTr 159
Cdd:COG4604 82 QENHINSRLTVRE-LVAfgrfpyskGRLTAEDREIIDEAIAY-LD----LEDLADRYLDELSGGQRQRafIAMVLAQDT- 154
|
....*....
gi 2032805432 160 pKVLLLDEP 168
Cdd:COG4604 155 -DYVLLDEP 162
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
26-168 |
3.61e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 65.98 E-value: 3.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 26 GVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGawDLVKQGLVMVPEGRGTFTRMTITENLL 105
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQR--DEYHQDLLYLGHQPGIKTELTALENLR 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032805432 106 MGAYIRDdkaqiEADIERIFGIFPR--LKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLLDEP 168
Cdd:PRK13538 97 FYQRLHG-----PGDDEALWEALAQvgLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEP 156
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
24-237 |
4.05e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 66.65 E-value: 4.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 24 VKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQP----VAAGEIEFMGK-----TLKGQgawdlvKQGLVMvPEGRGT 94
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPagvrQTAGRVLLDGKpvapcALRGR------KIATIM-QNPRSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 95 FT-----RMTITENLLMGAYIRDDKAQIEA-------DIERIFGIFPRlkerrnqlagTMSGGEQQ--MLAMgrALMTRP 160
Cdd:PRK10418 92 FNplhtmHTHARETCLALGKPADDATLTAAleavgleNAARVLKLYPF----------EMSGGMLQrmMIAL--ALLCEA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2032805432 161 KVLLLDEPSMGLSPIMVDKIFEVVNDI-HSQGVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLNDPKVRAA 237
Cdd:PRK10418 160 PFIIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVT 237
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
24-197 |
4.79e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 67.91 E-value: 4.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 24 VKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIE--------FM--------GkTLKGQgawdlvkqglVM 87
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIArpagarvlFLpqrpylplG-TLREA----------LL 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 88 VPEGRGTFTRMTITENLlmgayirdDKAQIEADIERIfgifprlkERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLLDE 167
Cdd:COG4178 448 YPATAEAFSDAELREAL--------EAVGLGHLAERL--------DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDE 511
|
170 180 190
....*....|....*....|....*....|
gi 2032805432 168 PSMGLSPIMVDKIFEVVNDiHSQGVTVLLV 197
Cdd:COG4178 512 ATSALDEENEAALYQLLRE-ELPGTTVISV 540
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
9-197 |
4.97e-13 |
|
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: 64.39 E-value: 4.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFmGKTLKgqgawdlvkqglvmv 88
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-GSTVK--------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 89 pegrgtftrmtitenllmgayirddkaqieadieriFGIFPRLkerrnqlagtmSGGEQQMLAMGRALMTRPKVLLLDEP 168
Cdd:cd03221 65 ------------------------------------IGYFEQL-----------SGGEKMRLALAKLLLENPNLLLLDEP 97
|
170 180
....*....|....*....|....*....
gi 2032805432 169 SMGLSPIMVDKIFEVVNDIHSqgvTVLLV 197
Cdd:cd03221 98 TNHLDLESIEALEEALKEYPG---TVILV 123
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
25-217 |
5.24e-13 |
|
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: 65.57 E-value: 5.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 25 KGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKT-LKGQGAWdlvkqglVMvpegrgtftRMTITEN 103
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIaYVSQEPW-------IQ---------NGTIREN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 104 LLMGAYIRDDK-------AQIEADIErifgIFP-----RLKERrnqlaG-TMSGGEQQMLAMGRALMTRPKVLLLDEPsm 170
Cdd:cd03250 86 ILFGKPFDEERyekvikaCALEPDLE----ILPdgdltEIGEK-----GiNLSGGQKQRISLARAVYSDADIYLLDDP-- 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2032805432 171 gLSPimVD-----KIFE-VVNDIHSQGVTVLLVEQNASrALQLASRGYVMESG 217
Cdd:cd03250 155 -LSA--VDahvgrHIFEnCILGLLLNNKTRILVTHQLQ-LLPHADQIVVLDNG 203
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
9-224 |
5.60e-13 |
|
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: 67.85 E-value: 5.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGGIQA--VKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKgqgAWDlvkqglv 86
Cdd:COG4618 331 LSVENLTVVPPGSKRpiLRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLS---QWD------- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 87 mvpegRGTFTRM-------------TITENL-LMGayirddkaqiEADIERIF------GI------FP-----RLKERR 135
Cdd:COG4618 401 -----REELGRHigylpqdvelfdgTIAENIaRFG----------DADPEKVVaaaklaGVhemilrLPdgydtRIGEGG 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 136 NQLagtmSGGEQQMLAMGRALMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQNASrALQLASRGYVME 215
Cdd:COG4618 466 ARL----SGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLR 540
|
....*....
gi 2032805432 216 SGLITMTGE 224
Cdd:COG4618 541 DGRVQAFGP 549
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
23-223 |
5.62e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 66.65 E-value: 5.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 23 AVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMG-KTLKGQGAWDlVKQGLVMVPEGRGTFTRMTIT 101
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGlDTSDEENLWD-IRNKAGMVFQNPDNQIVATIV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 102 E--------NLlmGAYIRDDKAQIEADIERIfGIFprlkERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLLDEPSMGLS 173
Cdd:PRK13633 104 EedvafgpeNL--GIPPEEIRERVDESLKKV-GMY----EYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2032805432 174 PIMVDKIFEVVNDIHSQ-GVTVLLVEQNASRALQlASRGYVMESGLITMTG 223
Cdd:PRK13633 177 PSGRREVVNTIKELNKKyGITIILITHYMEEAVE-ADRIIVMDSGKVVMEG 226
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
9-217 |
2.12e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 64.65 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQ----- 83
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRlallp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 84 GLVMVPEGrgtftrMTITE---------NLLMGAYIRDDKAQIEADIERIfgifpRLKERRNQLAGTMSGGEQQ--MLAM 152
Cdd:PRK11231 83 QHHLTPEG------ITVRElvaygrspwLSLWGRLSAEDNARVNQAMEQT-----RINHLADRRLTDLSGGQRQraFLAM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032805432 153 grALMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQN---ASR---ALQLASRGYVMESG 217
Cdd:PRK11231 152 --VLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDlnqASRycdHLVVLANGHVMAQG 220
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
16-241 |
2.85e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 65.64 E-value: 2.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 16 VAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAaGEIEFMGKTLK--------GQGAWdlVKQGlVM 87
Cdd:PRK11174 358 LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELReldpeswrKHLSW--VGQN-PQ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 88 VPEGrgtftrmTITENLLMGAYIRDDkAQIEADIERIFgifprLKERRNQL-----------AGTMSGGEQQMLAMGRAL 156
Cdd:PRK11174 434 LPHG-------TLRDNVLLGNPDASD-EQLQQALENAW-----VSEFLPLLpqgldtpigdqAAGLSVGQAQRLALARAL 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 157 MTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIhSQGVTVLLVEQNASrALQLASRGYVMESGLITMTGEGKTLLNDPKVRA 236
Cdd:PRK11174 501 LQPCQLLLLDEPTASLDAHSEQLVMQALNAA-SRRQTTLMVTHQLE-DLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFA 578
|
....*
gi 2032805432 237 AYLGE 241
Cdd:PRK11174 579 TLLAH 583
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
20-230 |
2.90e-12 |
|
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: 64.17 E-value: 2.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 20 GIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKgQGAWDLVKQGLVMVPEGRGTFTRmT 99
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIR-EVTLDSLRRAIGVVPQDTVLFND-T 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 100 ITENLlmgAYIRDD-----------KAQIEADIERI-FGIFPRLKERrnqlaGTM-SGGEQQMLAMGRALMTRPKVLLLD 166
Cdd:cd03253 91 IGYNI---RYGRPDatdeevieaakAAQIHDKIMRFpDGYDTIVGER-----GLKlSGGEKQRVAIARAILKNPPILLLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032805432 167 EPSMGLSPIMVDKIFEVVNDIhSQGVTVLLVEQNASRALQlASRGYVMESGLITMTGEGKTLLN 230
Cdd:cd03253 163 EATSALDTHTEREIQAALRDV-SKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLA 224
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
41-168 |
3.07e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 64.90 E-value: 3.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 41 GANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLkgqgaWDlVKQGLVMVPEGRGT---------FTRMTITENLLMGaYIR 111
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGRVL-----FD-AEKGICLPPEKRRIgyvfqdarlFPHYKVRGNLRYG-MAK 103
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2032805432 112 DDKAQIEaDIERIFGIFPRLKerrnQLAGTMSGGEQQMLAMGRALMTRPKVLLLDEP 168
Cdd:PRK11144 104 SMVAQFD-KIVALLGIEPLLD----RYPGSLSGGEKQRVAIGRALLTAPELLLMDEP 155
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
22-219 |
5.61e-12 |
|
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: 63.26 E-value: 5.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 22 QAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQgLVMVPEGRGTFTRmTIT 101
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK-VSLVGQEPVLFAR-SLQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 102 ENLLMG-AYIRDDKAQIEADIERIFGIFPRLK--------ERRNQLagtmSGGEQQMLAMGRALMTRPKVLLLDEPSMGL 172
Cdd:cd03248 106 DNIAYGlQSCSFECVKEAAQKAHAHSFISELAsgydtevgEKGSQL----SGGQKQRVAIARALIRNPQVLILDEATSAL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2032805432 173 SPIMVDKIFEVVNDIHsQGVTVLLVEQNASrALQLASRGYVMESGLI 219
Cdd:cd03248 182 DAESEQQVQQALYDWP-ERRTVLVIAHRLS-TVERADQILVLDGGRI 226
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
23-231 |
5.71e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 64.00 E-value: 5.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 23 AVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQ-----GLVM-VPEGRgTFT 96
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQirkkvGLVFqFPESQ-LFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 97 RmTITENLLMG----AYIRDDKAQIEADIERIFGIFPRLKERRnqlAGTMSGGEQQMLAMGRALMTRPKVLLLDEPSMGL 172
Cdd:PRK13649 101 E-TVLKDVAFGpqnfGVSQEEAEALAREKLALVGISESLFEKN---PFELSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2032805432 173 SPIMVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLND 231
Cdd:PRK13649 177 DPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
9-200 |
7.88e-12 |
|
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: 61.96 E-value: 7.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVayggiQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVtglqpvaageiefmgktlkgqgawdLVKQGLVMV 88
Cdd:cd03238 1 LTVSGANV-----HNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG-------------------------LYASGKARL 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 89 PEGRGTFTRMTItenllmgayIRDDKAQIEADIerifGI-FPRLkerrNQLAGTMSGGEQQMLAMGRALMTRPK--VLLL 165
Cdd:cd03238 51 ISFLPKFSRNKL---------IFIDQLQFLIDV----GLgYLTL----GQKLSTLSGGELQRVKLASELFSEPPgtLFIL 113
|
170 180 190
....*....|....*....|....*....|....*
gi 2032805432 166 DEPSMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQN 200
Cdd:cd03238 114 DEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHN 148
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
29-238 |
1.37e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 62.26 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 29 FEVRRGELVSLIGANGAGKTTTLKAVTGLQPvAAGEIEFMGKTLkgqGAWDLVKQGLVmvpegRGTFTR-------MTIT 101
Cdd:PRK03695 17 AEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPL---EAWSAAELARH-----RAYLSQqqtppfaMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 102 ENLLM----GAYIRDDKAQIEaDIERIFGIFPRLKERRNQLagtmSGGEQQ-------MLAMGRALMTRPKVLLLDEPSM 170
Cdd:PRK03695 88 QYLTLhqpdKTRTEAVASALN-EVAEALGLDDKLGRSVNQL----SGGEWQrvrlaavVLQVWPDINPAGQLLLLDEPMN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2032805432 171 GLSPIMVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLNDPKVRAAY 238
Cdd:PRK03695 163 SLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVF 230
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
18-193 |
2.26e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 62.88 E-value: 2.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 18 YGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVA--AGEIEFMGKTLKGQGAWDLVKQGLV-------MV 88
Cdd:NF040905 11 FPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGEVCRFKDIRDSEALGIViihqelaLI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 89 PEgrgtftrMTITENLLMG------AYIRDDKAQIEAD--IERIfgifpRLKERRNQLAGTMSGGEQQMLAMGRALMTRP 160
Cdd:NF040905 91 PY-------LSIAENIFLGnerakrGVIDWNETNRRARelLAKV-----GLDESPDTLVTDIGVGKQQLVEIAKALSKDV 158
|
170 180 190
....*....|....*....|....*....|...
gi 2032805432 161 KVLLLDEPSMGLSPIMVDKIFEVVNDIHSQGVT 193
Cdd:NF040905 159 KLLILDEPTAALNEEDSAALLDLLLELKAQGIT 191
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
8-232 |
2.46e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 62.80 E-value: 2.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 8 LLKVSGLKVAY--GGI--QAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVA-----AGEIEFMGKTLKGQGAW 78
Cdd:PRK15134 5 LLAIENLSVAFrqQQTvrTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 79 DLvkQGLvmvpegRGTFTRM-----------------TITENLLMGAYIRDDKAQIE--ADIERIfGI---FPRLKERRN 136
Cdd:PRK15134 85 TL--RGV------RGNKIAMifqepmvslnplhtlekQLYEVLSLHRGMRREAARGEilNCLDRV-GIrqaAKRLTDYPH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 137 QLagtmSGGEQQ--MLAMgrALMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQ-GVTVLLVEQNASRALQLASRGYV 213
Cdd:PRK15134 156 QL----SGGERQrvMIAM--ALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAV 229
|
250
....*....|....*....
gi 2032805432 214 MESGLITMTGEGKTLLNDP 232
Cdd:PRK15134 230 MQNGRCVEQNRAATLFSAP 248
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
25-223 |
3.65e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 62.37 E-value: 3.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 25 KGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQP---VAAGEIEFMGKTLkgqGAWDL------VKQGLVMVPEgrgtf 95
Cdd:TIGR00955 42 KNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLNGMPI---DAKEMraisayVQQDDLFIPT----- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 96 trMTITENLLMGAYIRDD--------KAQIEADIERIfgifpRLKERRNQLAGT------MSGGEQQMLAMGRALMTRPK 161
Cdd:TIGR00955 114 --LTVREHLMFQAHLRMPrrvtkkekRERVDEVLQAL-----GLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPP 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032805432 162 VLLLDEPSMGLSPIMVDKIFEVVNDIHSQGVTVLL-VEQNASRALQLASRGYVMESGLITMTG 223
Cdd:TIGR00955 187 LLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICtIHQPSSELFELFDKIILMAEGRVAYLG 249
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
8-172 |
5.14e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 62.03 E-value: 5.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 8 LLKVSGLKVAY---GGI--------QAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPvAAGEIEFMGKTLKGqg 76
Cdd:PRK15134 275 LLDVEQLQVAFpirKGIlkrtvdhnVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHN-- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 77 aWDLvKQGLVMVPEGRGTFT--------RMTITENLLMGAYIRD---DKAQIEADIERIF---GIFPrlkERRNQLAGTM 142
Cdd:PRK15134 352 -LNR-RQLLPVRHRIQVVFQdpnsslnpRLNVLQIIEEGLRVHQptlSAAQREQQVIAVMeevGLDP---ETRHRYPAEF 426
|
170 180 190
....*....|....*....|....*....|
gi 2032805432 143 SGGEQQMLAMGRALMTRPKVLLLDEPSMGL 172
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSL 456
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4-232 |
5.15e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 61.40 E-value: 5.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 4 SKEILLKVSGLKVAYGG-----IQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFmgKTLKGQGAW 78
Cdd:PRK13631 17 SDDIILRVKNLYCVFDEkqeneLVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQV--GDIYIGDKK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 79 DLVKQGLVMVPEGRGTFTRM--TITENLLMGAYiRDDKAQIEADIerIFG--IFPRLKERRNQLAG-------------- 140
Cdd:PRK13631 95 NNHELITNPYSKKIKNFKELrrRVSMVFQFPEY-QLFKDTIEKDI--MFGpvALGVKKSEAKKLAKfylnkmglddsyle 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 141 ----TMSGGEQQMLAMGRALMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMES 216
Cdd:PRK13631 172 rspfGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDK 251
|
250
....*....|....*.
gi 2032805432 217 GLITMTGEGKTLLNDP 232
Cdd:PRK13631 252 GKILKTGTPYEIFTDQ 267
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-169 |
5.16e-11 |
|
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: 61.87 E-value: 5.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 6 EILLKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFmGKTLKgqgawdlvkqgL 85
Cdd:TIGR03719 320 DKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK-----------L 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 86 VMVPEGRGTFT-RMTITENLLMGA-YIRDDKAQIEAdieRIF-GIFPRLKERRNQLAGTMSGGEQQMLAMGRALMTRPKV 162
Cdd:TIGR03719 388 AYVDQSRDALDpNKTVWEEISGGLdIIKLGKREIPS---RAYvGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNV 464
|
....*..
gi 2032805432 163 LLLDEPS 169
Cdd:TIGR03719 465 LLLDEPT 471
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-197 |
6.19e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 60.11 E-value: 6.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 1 MADSKEIL-LKVSGLKVayGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGK---TLKGQG 76
Cdd:PRK10247 1 MQENSPLLqLQNVGYLA--GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdisTLKPEI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 77 AWDLVK---QGLVMVPEgrgtftrmTITENLLMGAYIRDDKAQ---IEADIERiFGIfPR--LKERRNQLagtmSGGEQQ 148
Cdd:PRK10247 79 YRQQVSycaQTPTLFGD--------TVYDNLIFPWQIRNQQPDpaiFLDDLER-FAL-PDtiLTKNIAEL----SGGEKQ 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2032805432 149 MLAMGRALMTRPKVLLLDEPSMGLSpimvDKIFEVVND-IH----SQGVTVLLV 197
Cdd:PRK10247 145 RISLIRNLQFMPKVLLLDEITSALD----ESNKHNVNEiIHryvrEQNIAVLWV 194
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
20-167 |
6.30e-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: 60.32 E-value: 6.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 20 GIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQgLVMVPEGRGTFTRmT 99
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQ-IGLVSQDVFLFND-T 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032805432 100 ITENLLMGAYIRDDKAQIEAD--------IERI-FGIFPRLKERRNQLagtmSGGEQQMLAMGRALMTRPKVLLLDE 167
Cdd:cd03251 92 VAENIAYGRPGATREEVEEAAraanahefIMELpEGYDTVIGERGVKL----SGGQRQRIAIARALLKDPPILILDE 164
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-231 |
7.76e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 61.38 E-value: 7.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 2 ADSKEILLKVSGLKVAY--GGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKgqgAWD 79
Cdd:PRK11160 332 AAADQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIA---DYS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 80 --LVKQGLVMVPEGRGTFTRmTITENLLMGAYIRDDKAQIEA--------DIERIFGIFPRLKERRNQLagtmSGGEQQM 149
Cdd:PRK11160 409 eaALRQAISVVSQRVHLFSA-TLRDNLLLAAPNASDEALIEVlqqvglekLLEDDKGLNAWLGEGGRQL----SGGEQRR 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 150 LAMGRALMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDiHSQGVTVLLVEQNAsRALQLASRGYVMESGLITMTGEGKTLL 229
Cdd:PRK11160 484 LGIARALLHDAPLLLLDEPTEGLDAETERQILELLAE-HAQNKTVLMITHRL-TGLEQFDRICVMDNGQIIEQGTHQELL 561
|
..
gi 2032805432 230 ND 231
Cdd:PRK11160 562 AQ 563
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
23-232 |
1.23e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 59.81 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 23 AVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTG-LQPVAAGE--IEFMGKTLKGQGAWDLV-KQGLVmvpegrgtFTRm 98
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlLLPDDNPNskITVDGITLTAKTVWDIReKVGIV--------FQN- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 99 tiTENLLMGAYIRDDKAqieadieriFGI----FPR---LKERRNQLA------------GTMSGGEQQMLAMGRALMTR 159
Cdd:PRK13640 93 --PDNQFVGATVGDDVA---------FGLenraVPRpemIKIVRDVLAdvgmldyidsepANLSGGQKQRVAIAGILAVE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032805432 160 PKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQ-GVTVLLVEQNASRAlQLASRGYVMESGLITMTGEGKTLLNDP 232
Cdd:PRK13640 162 PKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
8-168 |
1.37e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 60.73 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 8 LLKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMG------------KTLKGq 75
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQdlivarlqqdppRNVEG- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 76 GAWDLVKQGLVMVPEGRGTFTRMTiteNLLMGAYirDDK-----AQIEADIE---------RIFGIFPRLKERRNQLAGT 141
Cdd:PRK11147 82 TVYDFVAEGIEEQAEYLKRYHDIS---HLVETDP--SEKnlnelAKLQEQLDhhnlwqlenRINEVLAQLGLDPDAALSS 156
|
170 180
....*....|....*....|....*..
gi 2032805432 142 MSGGEQQMLAMGRALMTRPKVLLLDEP 168
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEP 183
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
8-172 |
1.40e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 59.36 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 8 LLKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGqgawdLVKQGLVM 87
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIG-----YVPQKLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 88 VPegrgtftrmtiTENLLMGAYIRDDKAQIEADierifgIFPRLKERR-----NQLAGTMSGGEQQMLAMGRALMTRPKV 162
Cdd:PRK09544 79 DT-----------TLPLTVNRFLRLRPGTKKED------ILPALKRVQaghliDAPMQKLSGGETQRVLLARALLNRPQL 141
|
170
....*....|
gi 2032805432 163 LLLDEPSMGL 172
Cdd:PRK09544 142 LVLDEPTQGV 151
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
4-232 |
1.42e-10 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 60.43 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 4 SKEILLKVSGLKVAyggiqaVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLV-- 81
Cdd:PRK10070 30 SKEQILEKTGLSLG------VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRev 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 82 -KQGLVMVPEGRGTFTRMTITENLLMGAYIR----DDKAQIEADIERIFGifprLKERRNQLAGTMSGGEQQMLAMGRAL 156
Cdd:PRK10070 104 rRKKIAMVFQSFALMPHMTVLDNTAFGMELAginaEERREKALDALRQVG----LENYAHSYPDELSGGMRQRVGLARAL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032805432 157 MTRPKVLLLDEPSMGLSPIMVDKIF-EVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLNDP 232
Cdd:PRK10070 180 AINPDILLMDEAFSALDPLIRTEMQdELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNP 256
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
8-229 |
1.99e-10 |
|
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: 60.12 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 8 LLKVSGLKVAYGG--IQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMG--------KTLKGQGA 77
Cdd:TIGR02203 330 DVEFRNVTFRYPGrdRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGhdladytlASLRRQVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 78 wdLVKQGLVMVPEgrgtftrmTITENLLMGAYIRDDKAQIEADIERIFgifprLKERRNQL-----------AGTMSGGE 146
Cdd:TIGR02203 410 --LVSQDVVLFND--------TIANNIAYGRTEQADRAEIERALAAAY-----AQDFVDKLplgldtpigenGVLLSGGQ 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 147 QQMLAMGRALMTRPKVLLLDEPSMGL---SPIMVDKIFEVVndihSQGVTVLLVEQNASrALQLASRGYVMESGLITMTG 223
Cdd:TIGR02203 475 RQRLAIARALLKDAPILILDEATSALdneSERLVQAALERL----MQGRTTLVIAHRLS-TIEKADRIVVMDDGRIVERG 549
|
....*.
gi 2032805432 224 EGKTLL 229
Cdd:TIGR02203 550 THNELL 555
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
22-233 |
2.37e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 59.02 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 22 QAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGL-QP----VAAGEIEFMGKTlKGQGAWDLVKQ-GLVM-VPEGRgt 94
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALlKPttgtVTVDDITITHKT-KDKYIRPVRKRiGMVFqFPESQ-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 95 FTRMTITENLLMGAyiRDDKAQIEADIERIFGIFPRLKERRNQLAGT---MSGGEQQMLAMGRALMTRPKVLLLDEPSMG 171
Cdd:PRK13646 98 LFEDTVEREIIFGP--KNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSpfqMSGGQMRKIAIVSILAMNPDIIVLDEPTAG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032805432 172 LSPIMVDKIFEVVNDIH-SQGVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLNDPK 233
Cdd:PRK13646 176 LDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKK 238
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
22-224 |
4.06e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 59.03 E-value: 4.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 22 QAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQ--PVAAGEIEFMGKTLKGQGAWDLVKQGLVMVPEGR---GTFT 96
Cdd:NF040905 274 KVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISGTVFKDGKEVDVSTVSDAIDAGLAYVTEDRkgyGLNL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 97 RMTITENLLMgayirddkaqieADIERI--FGIFPRLKERR----------------NQLAGTMSGGEQQMLAMGRALMT 158
Cdd:NF040905 354 IDDIKRNITL------------ANLGKVsrRGVIDENEEIKvaeeyrkkmniktpsvFQKVGNLSGGNQQKVVLSKWLFT 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032805432 159 RPKVLLLDEPSMGlspIMVD---KIFEVVNDIHSQGVTVLLVEQNASRALQLASRGYVMESGLItmTGE 224
Cdd:NF040905 422 DPDVLILDEPTRG---IDVGakyEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRI--TGE 485
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
13-168 |
4.75e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 58.44 E-value: 4.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 13 GLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKG--QGAWDLVKQGLVMV-- 88
Cdd:PRK11308 20 GLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKadPEAQKLLRQKIQIVfq 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 89 -PEGRGTfTRMTItenllmgAYIRDDKAQIEADIERifgifprlKERRNQLAGTM-----------------SGGEQQML 150
Cdd:PRK11308 100 nPYGSLN-PRKKV-------GQILEEPLLINTSLSA--------AERREKALAMMakvglrpehydryphmfSGGQRQRI 163
|
170
....*....|....*...
gi 2032805432 151 AMGRALMTRPKVLLLDEP 168
Cdd:PRK11308 164 AIARALMLDPDVVVADEP 181
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
3-231 |
6.78e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 57.73 E-value: 6.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 3 DSKEILLKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGlQP---VAAGEIEFMGKTLkgqgawd 79
Cdd:CHL00131 2 NKNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG-HPaykILEGDILFKGESI------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 80 lvkqgLVMVPEGR---GTFTR----MTIT----ENLLMGAYIRDDKAQIEADIERIFG---IFPRLKE--------RRNQ 137
Cdd:CHL00131 74 -----LDLEPEERahlGIFLAfqypIEIPgvsnADFLRLAYNSKRKFQGLPELDPLEFleiINEKLKLvgmdpsflSRNV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 138 LAGtMSGGEQ---QMLAMgrALMtRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQGVTVLLVeQNASRALQLASRGYV- 213
Cdd:CHL00131 149 NEG-FSGGEKkrnEILQM--ALL-DSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILI-THYQRLLDYIKPDYVh 223
|
250
....*....|....*....
gi 2032805432 214 -MESGLITMTGeGKTLLND 231
Cdd:CHL00131 224 vMQNGKIIKTG-DAELAKE 241
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
9-206 |
1.07e-09 |
|
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: 58.38 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAY--GGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAaGEIEFMGKTlkgqgaWDLV----- 81
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVS------WNSVtlqtw 1290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 82 KQGLVMVPEGRGTFTRmTITENLLMGAYIRDD---KAQIEADIERIFGIFP-RLKERRNQLAGTMSGGEQQMLAMGRALM 157
Cdd:TIGR01271 1291 RKAFGVIPQKVFIFSG-TFRKNLDPYEQWSDEeiwKVAEEVGLKSVIEQFPdKLDFVLVDGGYVLSNGHKQLMCLARSIL 1369
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2032805432 158 TRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQgVTVLLVEQNASRALQ 206
Cdd:TIGR01271 1370 SKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSN-CTVILSEHRVEALLE 1417
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
9-230 |
1.44e-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: 57.50 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQ--PVAAGEI----------------EFMGK 70
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIiyhvalcekcgyverpSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 71 -------TLKGQGA--WDL--------VKQGLVMVPEGRGTFTRMTITENLLMG----AYIRDDKAQIEAD-IERIfgif 128
Cdd:TIGR03269 81 pcpvcggTLEPEEVdfWNLsdklrrriRKRIAIMLQRTFALYGDDTVLDNVLEAleeiGYEGKEAVGRAVDlIEMV---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 129 pRLKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLLDEPSMGLSPIMVDKIFEVVND-IHSQGVTVLLVEQNASRALQL 207
Cdd:TIGR03269 157 -QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEaVKASGISMVLTSHWPEVIEDL 235
|
250 260
....*....|....*....|...
gi 2032805432 208 ASRGYVMESGLITMTGEGKTLLN 230
Cdd:TIGR03269 236 SDKAIWLENGEIKEEGTPDEVVA 258
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-233 |
1.53e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.56 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 3 DSKEILlKVSGLKVAY----GGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTL--KGQG 76
Cdd:PRK10261 8 DARDVL-AVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLrrRSRQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 77 AWDLVKQGLVMVPEGRGTFTRM-----------------TITENLLMGAYIRDDKAQIEA----DIERIfgifPRLKERR 135
Cdd:PRK10261 87 VIELSEQSAAQMRHVRGADMAMifqepmtslnpvftvgeQIAESIRLHQGASREEAMVEAkrmlDQVRI----PEAQTIL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 136 NQLAGTMSGGEQQMLAMGRALMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQ-GVTVLLVEQNASRALQLASRGYVM 214
Cdd:PRK10261 163 SRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVM 242
|
250
....*....|....*....
gi 2032805432 215 ESGLITMTGEGKTLLNDPK 233
Cdd:PRK10261 243 YQGEAVETGSVEQIFHAPQ 261
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
8-206 |
1.73e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 57.43 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 8 LLKVSGLKVAY----GGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGK---TLKGQGAWDL 80
Cdd:PRK10535 4 LLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQdvaTLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 81 VKQGLVMVPEGRGTFTRMTITEN-----LLMGAYIRDDKAQIEADIERIfGIFPRLKERRNQLagtmSGGEQQMLAMGRA 155
Cdd:PRK10535 84 RREHFGFIFQRYHLLSHLTAAQNvevpaVYAGLERKQRLLRAQELLQRL-GLEDRVEYQPSQL----SGGQQQRVSIARA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2032805432 156 LMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQNASRALQ 206
Cdd:PRK10535 159 LMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ 209
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
7-219 |
2.41e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 56.23 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 7 ILLKVSGLKVAYGG---------IQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGK---TLKG 74
Cdd:PRK10419 2 TLLNVSGLSHHYAHgglsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEplaKLNR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 75 QGAWDLVKQGLVMVPEGRGTFT-RMTItenllmGAYIRD--------DKAQIEADIE---RIFGIFPRLKERRNQlagTM 142
Cdd:PRK10419 82 AQRKAFRRDIQMVFQDSISAVNpRKTV------REIIREplrhllslDKAERLARASemlRAVDLDDSVLDKRPP---QL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2032805432 143 SGGEQQMLAMGRALMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQ-GVTVLLVEQNASRALQLASRGYVMESGLI 219
Cdd:PRK10419 153 SGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
9-168 |
2.58e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.82 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQglvmv 88
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHAYD----- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 89 pegrgtF-TRMTITEnlLMGAYirddkAQIEADIERIFGIFPRL---KERRNQLAGTMSGGEQQMLAMGRALMTRPKVLL 164
Cdd:PRK15064 395 ------FeNDLTLFD--WMSQW-----RQEGDDEQAVRGTLGRLlfsQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLV 461
|
....
gi 2032805432 165 LDEP 168
Cdd:PRK15064 462 MDEP 465
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
23-197 |
3.35e-09 |
|
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: 55.19 E-value: 3.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 23 AVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLvKQGLVMVPEGRGTFTRmTITE 102
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDL-RSRISIIPQDPVLFSG-TIRS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 103 NL-LMGAYirDDKAQIEAdIERIfgifpRLKERRNQLAGTM-----------SGGEQQMLAMGRALMTRPKVLLLDEPSM 170
Cdd:cd03244 97 NLdPFGEY--SDEELWQA-LERV-----GLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALLRKSKILVLDEATA 168
|
170 180
....*....|....*....|....*..
gi 2032805432 171 GLSPIMVDKIFEVVNDiHSQGVTVLLV 197
Cdd:cd03244 169 SVDPETDALIQKTIRE-AFKDCTVLTI 194
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
9-238 |
3.66e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 55.76 E-value: 3.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKgQGAWDLVKQGLVMV 88
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQ-HYASKEVARRIGLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 89 PEGRGTFTRMTITENLLMGAY--------IRDDKAQIEADIERIFGIfprlKERRNQLAGTMSGGEQQMLAMGRALMTRP 160
Cdd:PRK10253 87 AQNATTPGDITVQELVARGRYphqplftrWRKEDEEAVTKAMQATGI----THLADQSVDTLSGGQRQRAWIAMVLAQET 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032805432 161 KVLLLDEPSMGLSPIMVDKIFEVVNDIH-SQGVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLNDPKVRAAY 238
Cdd:PRK10253 163 AIMLLDEPTTWLDISHQIDLLELLSELNrEKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIY 241
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
23-231 |
5.15e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 55.14 E-value: 5.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 23 AVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQ-GLVMV-PEGR--GTFTRM 98
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHiGIVFQnPDNQfvGSIVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 99 TITENLLMGAYIRDDK----AQIEADIERIfgifprlkERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLLDEPSMGLSP 174
Cdd:PRK13648 104 DVAFGLENHAVPYDEMhrrvSEALKQVDML--------ERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDP 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2032805432 175 IMVDKIFEVVNDIHS-QGVTVLLVEQNASRALQlASRGYVMESGLITMTGEGKTLLND 231
Cdd:PRK13648 176 DARQNLLDLVRKVKSeHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
34-238 |
6.83e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 54.79 E-value: 6.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 34 GELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLkgqGAWD--LVKQGLVMVPEGRGTFTRMTITENLLMGAYI- 110
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPL---ESWSskAFARKVAYLPQQLPAAEGMTVRELVAIGRYPw 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 111 --------RDDKAQIEADIERIfgifpRLKERRNQLAGTMSGGEQQM--LAMGRALMTRpkVLLLDEPSMGLSpimVDKI 180
Cdd:PRK10575 114 hgalgrfgAADREKVEEAISLV-----GLKPLAHRLVDSLSGGERQRawIAMLVAQDSR--CLLLDEPTSALD---IAHQ 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032805432 181 FEVVNDIH--SQ--GVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLNDPKVRAAY 238
Cdd:PRK10575 184 VDVLALVHrlSQerGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIY 245
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
21-232 |
6.84e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 54.80 E-value: 6.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 21 IQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKgQGAWDLVKQGLVMV---------PEG 91
Cdd:PRK15112 26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH-FGDYSYRSQRIRMIfqdpstslnPRQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 92 R-GTFTRMTITENLLMGAYIRDDkaQIEADIeRIFGIFPrlkERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLLDEPSM 170
Cdd:PRK15112 105 RiSQILDFPLRLNTDLEPEQREK--QIIETL-RQVGLLP---DHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032805432 171 GLSPIMVDKIFEVVNDIH-SQGVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLNDP 232
Cdd:PRK15112 179 SLDMSMRSQLINLMLELQeKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASP 241
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
11-167 |
8.40e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 55.49 E-value: 8.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 11 VSGLKVAYGGIQAV-KGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLvKQGLVMVP 89
Cdd:PRK10790 343 IDNVSFAYRDDNLVlQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL-RQGVAMVQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 90 EGRGTFTRmTITENLLMGAYIRDDK-------AQIeADIERIF--GIFPRLKERRNqlagTMSGGEQQMLAMGRALMTRP 160
Cdd:PRK10790 422 QDPVVLAD-TFLANVTLGRDISEEQvwqaletVQL-AELARSLpdGLYTPLGEQGN----NLSVGQKQLLALARVLVQTP 495
|
....*..
gi 2032805432 161 KVLLLDE 167
Cdd:PRK10790 496 QILILDE 502
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
23-167 |
9.03e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 54.98 E-value: 9.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 23 AVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGL-QPVaAGEIEFMGKTLKGqGAWDLVKQGLVMVpegrgtFTRMTIT 101
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLyQPQ-SGEILLDGKPVTA-EQPEDYRKLFSAV------FTDFHLF 409
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032805432 102 ENLLMGAYIRDDKAQIEADIERIfGIFPRLKERRNQLAGT-MSGGEQQMLAMGRALMTRPKVLLLDE 167
Cdd:PRK10522 410 DQLLGPEGKPANPALVEKWLERL-KMAHKLELEDGRISNLkLSKGQKKRLALLLALAEERDILLLDE 475
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
22-237 |
1.27e-08 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 54.73 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 22 QAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQgLVMVPEGRGTFTRmTIT 101
Cdd:TIGR00958 495 PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQ-VALVGQEPVLFSG-SVR 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 102 ENLLMGAYiRDDKAQIEADIERIF----------GIFPRLKERRNQlagtMSGGEQQMLAMGRALMTRPKVLLLDEPSmg 171
Cdd:TIGR00958 573 ENIAYGLT-DTPDEEIMAAAKAANahdfimefpnGYDTEVGEKGSQ----LSGGQKQRIAIARALVRKPRVLILDEAT-- 645
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032805432 172 lSPIMVDKIFEVVNDIHSQGVTVLLVEQNAS---RALQLAsrgyVMESGLITMTGEGKTLLNDPKVRAA 237
Cdd:TIGR00958 646 -SALDAECEQLLQESRSRASRTVLLIAHRLStveRADQIL----VLKKGSVVEMGTHKQLMEDQGCYKH 709
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
21-233 |
1.30e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.86 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 21 IQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGK---TLKGQGAWDLVK--QGLVMVP----EG 91
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSPGKLQALRRdiQFIFQDPyaslDP 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 92 RGTFTrMTITENLLMGAYIRDDKAQ--IEADIERIfGIFPrlkERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLLDEPS 169
Cdd:PRK10261 417 RQTVG-DSIMEPLRVHGLLPGKAAAarVAWLLERV-GLLP---EHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAV 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032805432 170 MGLSPIMVDKIFEVVNDIHSQ-GVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLNDPK 233
Cdd:PRK10261 492 SALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQ 556
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
28-197 |
1.32e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.64 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 28 DFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGE------------IEFMGKTLKGQgaW-----DLVKQGlvmvPE 90
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGErqsqfshitrlsFEQLQKLVSDE--WqrnntDMLSPG----ED 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 91 GRGTFTRMTITENLlmgayirdDKAQIEADIERIFGIFPRLKERRNQLagtmSGGEQQMLAMGRALMTRPKVLLLDEPSM 170
Cdd:PRK10938 97 DTGRTTAEIIQDEV--------KDPARCEQLAQQFGITALLDRRFKYL----STGETRKTLLCQALMSEPDLLILDEPFD 164
|
170 180
....*....|....*....|....*..
gi 2032805432 171 GLSPIMVDKIFEVVNDIHSQGVTVLLV 197
Cdd:PRK10938 165 GLDVASRQQLAELLASLHQSGITLVLV 191
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
9-169 |
1.47e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.35 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEfMGKTLK-------------GQ 75
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIK-IGETVKlayvdqsrdaldpNK 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 76 GAWDLVKQGLvmvpegrgtftrmtitENLLMGAYIRDDKAQIEAdieriFGifprLKERRNQ-LAGTMSGGEQQMLAMGR 154
Cdd:PRK11819 404 TVWEEISGGL----------------DIIKVGNREIPSRAYVGR-----FN----FKGGDQQkKVGVLSGGERNRLHLAK 458
|
170
....*....|....*
gi 2032805432 155 ALMTRPKVLLLDEPS 169
Cdd:PRK11819 459 TLKQGGNVLLLDEPT 473
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
11-174 |
1.79e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 54.36 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 11 VSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLV-------KQ 83
Cdd:NF033858 4 LEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVcpriaymPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 84 GLvmvpeGRGTFTRMTITENL-----LMGAyirdDKAQIEADIERIF---GIFPRLkERrnqLAGTMSGGEQQMLAMGRA 155
Cdd:NF033858 84 GL-----GKNLYPTLSVFENLdffgrLFGQ----DAAERRRRIDELLratGLAPFA-DR---PAGKLSGGMKQKLGLCCA 150
|
170
....*....|....*....
gi 2032805432 156 LMTRPKVLLLDEPSMGLSP 174
Cdd:NF033858 151 LIHDPDLLILDEPTTGVDP 169
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
22-223 |
2.59e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 53.47 E-value: 2.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 22 QAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGL------QPVAaGEIEFMGKTLKGQGAWDLVKQ-GLVM-VPEGRg 93
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLiisetgQTIV-GDYAIPANLKKIKEVKRLRKEiGLVFqFPEYQ- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 94 tFTRMTITENLLMG-AYIRDDKAQIEADIERIFGI--FPRLKERRNQLAgtMSGGEQQMLAMGRALMTRPKVLLLDEPSM 170
Cdd:PRK13645 103 -LFQETIEKDIAFGpVNLGENKQEAYKKVPELLKLvqLPEDYVKRSPFE--LSGGQKRRVALAGIIAMDGNTLVLDEPTG 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2032805432 171 GLSPIMVD---KIFEVVNdiHSQGVTVLLVEQNASRALQLASRGYVMESGLITMTG 223
Cdd:PRK13645 180 GLDPKGEEdfiNLFERLN--KEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIG 233
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
9-231 |
3.11e-08 |
|
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: 52.93 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 9 LKVSGLKVAY--GGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAaGEIEFMGKTlkgqgaWDLV----- 81
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVS------WNSVplqkw 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 82 KQGLVMVPEGRGTFTRmTITENLLMGAYIRDD---KAQIEADIERIFGIFP-RLKERRNQLAGTMSGGEQQMLAMGRALM 157
Cdd:cd03289 76 RKAFGVIPQKVFIFSG-TFRKNLDPYGKWSDEeiwKVAEEVGLKSVIEQFPgQLDFVLVDGGCVLSHGHKQLMCLARSVL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032805432 158 TRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSqGVTVLLVEQNASRALQlASRGYVMESGLITMTGEGKTLLND 231
Cdd:cd03289 155 SKAKILLLDEPSAHLDPITYQVIRKTLKQAFA-DCTVILSEHRIEAMLE-CQRFLVIEENKVRQYDSIQKLLNE 226
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
27-72 |
3.12e-08 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 53.65 E-value: 3.12e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2032805432 27 VDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTL 72
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV 396
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
4-187 |
3.77e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 52.80 E-value: 3.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 4 SKEILLKVSGLKVAY----GGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGL---QPVAAGEIEFMGKTLKGQG 76
Cdd:PRK09473 8 QADALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLlaaNGRIGGSATFNGREILNLP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 77 AWDLVK---QGLVMVPEGRGTFTR--MTITENL---LMgAYIRDDKAQ-IEADIERIFGI-FPRLKERRNQLAGTMSGGE 146
Cdd:PRK09473 88 EKELNKlraEQISMIFQDPMTSLNpyMRVGEQLmevLM-LHKGMSKAEaFEESVRMLDAVkMPEARKRMKMYPHEFSGGM 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2032805432 147 QQ--MLAMgrALMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDI 187
Cdd:PRK09473 167 RQrvMIAM--ALLCRPKLLIADEPTTALDVTVQAQIMTLLNEL 207
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
24-182 |
4.22e-08 |
|
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: 52.55 E-value: 4.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 24 VKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGK-TLKGQGAWdlvkqglvMVPEgrgtftrmTITE 102
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRiSFSSQFSW--------IMPG--------TIKE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 103 NLLMGA------YIRDDKA-QIEADIERifgiFPrlkERRNQLAG----TMSGGEQQMLAMGRALMTRPKVLLLDEPSMG 171
Cdd:cd03291 117 NIIFGVsydeyrYKSVVKAcQLEEDITK----FP---EKDNTVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPFGY 189
|
170
....*....|.
gi 2032805432 172 LSPIMVDKIFE 182
Cdd:cd03291 190 LDVFTEKEIFE 200
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
24-182 |
5.07e-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: 53.38 E-value: 5.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 24 VKGVDFEVRRGELVSLIGANGAGKTTTLKAVTG-LQPvAAGEIEFMGK-TLKGQGAWdlvkqglvMVPEgrgtftrmTIT 101
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGeLEP-SEGKIKHSGRiSFSPQTSW--------IMPG--------TIK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 102 ENLLMGA------YIRDDKA-QIEADIerifGIFPrlkERRNQLAG----TMSGGEQQMLAMGRALMTRPKVLLLDEPSM 170
Cdd:TIGR01271 505 DNIIFGLsydeyrYTSVIKAcQLEEDI----ALFP---EKDKTVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPFT 577
|
170
....*....|..
gi 2032805432 171 GLSPIMVDKIFE 182
Cdd:TIGR01271 578 HLDVVTEKEIFE 589
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
20-202 |
5.14e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 52.83 E-value: 5.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 20 GIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIefmgkTLKGQGAWDLVKQGLVMvpeGRGTFTRMT 99
Cdd:TIGR00954 464 GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRL-----TKPAKGKLFYVPQRPYM---TLGTLRDQI 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 100 I----TENLLMGAYIRDDKAQI--EADIERIF---GIFPRLKERRNQLagtmSGGEQQMLAMGRALMTRPKVLLLDEPSM 170
Cdd:TIGR00954 536 IypdsSEDMKRRGLSDKDLEQIldNVQLTHILereGGWSAVQDWMDVL----SGGEKQRIAMARLFYHKPQFAILDECTS 611
|
170 180 190
....*....|....*....|....*....|..
gi 2032805432 171 GLSPIMVDKIFEVVNDIhsqGVTVLLVEQNAS 202
Cdd:TIGR00954 612 AVSVDVEGYMYRLCREF---GITLFSVSHRKS 640
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
8-187 |
6.63e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 52.14 E-value: 6.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 8 LLKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTG--LQPVAA------GEIEFMGKTLKGQGAWD 79
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdlTGGGAPrgarvtGDVTLNGEPLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 80 LVKQGLVMVPEGRGTFTrMTITENLLMGAYIRDDKAQieADIERIFGIFPRLKERRNQ--LAG----TMSGGEQQMLAMG 153
Cdd:PRK13547 81 LARLRAVLPQAAQPAFA-FSAREIVLLGRYPHARRAG--ALTHRDGEIAWQALALAGAtaLVGrdvtTLSGGELARVQFA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2032805432 154 RAL---------MTRPKVLLLDEPSMGLSPIMVDKIFEVVNDI 187
Cdd:PRK13547 158 RVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRL 200
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
8-233 |
7.84e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 52.05 E-value: 7.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 8 LLKVSGLKVAYGG----IQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGL----QPVAAGEIEFMG---KTLKGQG 76
Cdd:PRK11022 3 LLNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypGRVMAEKLEFNGqdlQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 77 AWDLVKQGLVMVPEGRGTFTRMTITENL-LMGAY------IRDDKAQIEADIERIFGI---FPRLKERRNQLAGTMSggE 146
Cdd:PRK11022 83 RRNLVGAEVAMIFQDPMTSLNPCYTVGFqIMEAIkvhqggNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMS--Q 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 147 QQMLAMgrALMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQ-GVTVLLVEQNASRALQLASRGYVMESGLITMTGEG 225
Cdd:PRK11022 161 RVMIAM--AIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQVVETGKA 238
|
....*...
gi 2032805432 226 KTLLNDPK 233
Cdd:PRK11022 239 HDIFRAPR 246
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
26-226 |
9.01e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 52.64 E-value: 9.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 26 GVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIefmgkTLKGQGAWdlvkqglvmVPEgRGTFTRMTITENLL 105
Cdd:TIGR00957 656 GITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV-----HMKGSVAY---------VPQ-QAWIQNDSLRENIL 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 106 MGAYIRDD--KAQIEA-----DIErifgIFPRLKERRNQLAG-TMSGGEQQMLAMGRALMTRPKVLLLDEPSMGLSPIMV 177
Cdd:TIGR00957 721 FGKALNEKyyQQVLEAcallpDLE----ILPSGDRTEIGEKGvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVG 796
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2032805432 178 DKIFEVVndIHSQGVTvllveQNASRALQLASRGYVMESGLITMTGEGK 226
Cdd:TIGR00957 797 KHIFEHV--IGPEGVL-----KNKTRILVTHGISYLPQVDVIIVMSGGK 838
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
141-210 |
1.07e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 52.14 E-value: 1.07e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032805432 141 TMSGGEQQMLAMGRALMTRPK--VLLLDEPSMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQNaSRALQLASR 210
Cdd:PRK00635 476 TLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD-EQMISLADR 546
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
2-169 |
2.06e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.96 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 2 ADSKEILLKVSGLKVAYGGIQ-AVKGVdfEVRRGELVSLIGANGAGKTTTLKAVTG-LQPVaAGEIEfmgktlkgqgaWD 79
Cdd:PRK13409 334 ESERETLVEYPDLTKKLGDFSlEVEGG--EIYEGEVIGIVGPNGIGKTTFAKLLAGvLKPD-EGEVD-----------PE 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 80 L---VK-QGLVMVPEGRgtftrmtiTENLLMGAYIRDDKAQIEADIERIFGIfPRLKERRnqlAGTMSGGEQQMLAMGRA 155
Cdd:PRK13409 400 LkisYKpQYIKPDYDGT--------VEDLLRSITDDLGSSYYKSEIIKPLQL-ERLLDKN---VKDLSGGELQRVAIAAC 467
|
170
....*....|....
gi 2032805432 156 LMTRPKVLLLDEPS 169
Cdd:PRK13409 468 LSRDADLYLLDEPS 481
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
20-197 |
2.45e-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: 50.02 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 20 GIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDL--VKQGLVMVPEGRGTFTR 97
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsRNRYSVAYAAQKPWLLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 98 MTITENLLMGAYIRDD--KAQIEA-----DIERI-FGIFPRLKERRNQLagtmSGGEQQMLAMGRALMTRPKVLLLDEPS 169
Cdd:cd03290 93 ATVEENITFGSPFNKQryKAVTDAcslqpDIDLLpFGDQTEIGERGINL----SGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190
....*....|....*....|....*....|
gi 2032805432 170 MGLSPIMVDKIFE--VVNDIHSQGVTVLLV 197
Cdd:cd03290 169 SALDIHLSDHLMQegILKFLQDDKRTLVLV 198
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
26-167 |
2.79e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.89 E-value: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 26 GVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQgLVMVPEGRGTFTRmTITENLl 105
Cdd:PLN03130 1257 GLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKV-LGIIPQAPVLFSG-TVRFNL- 1333
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032805432 106 mGAYIRDDKAQIEADIERifgifPRLKE--RRNQL--------AG-TMSGGEQQMLAMGRALMTRPKVLLLDE 167
Cdd:PLN03130 1334 -DPFNEHNDADLWESLER-----AHLKDviRRNSLgldaevseAGeNFSVGQRQLLSLARALLRRSKILVLDE 1400
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
41-173 |
2.88e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 49.48 E-value: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 41 GANGAGKTTTLKAVTGLQPVAAGEIEFmgktlKGQGAWDLVKQGLVMVPEGRGTFTRMTITENLLMGAYIRDDKAQIEAD 120
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYY-----KNCNINNIAKPYCTYIGHNLGLKLEMTVFENLKFWSEIYNSAETLYAA 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2032805432 121 IErifgiFPRLKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLLDEPSMGLS 173
Cdd:PRK13541 108 IH-----YFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
23-232 |
2.90e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 50.02 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 23 AVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGL-QP----VAAGEIEFMG----KTLKgqgawDLVKQ-GLVM-VPEG 91
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLlQPtsgtVTIGERVITAgkknKKLK-----PLRKKvGIVFqFPEH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 92 RgtFTRMTITENLLMGAY---IRDDKAQIEAD-IERIFGIFPRLKERRnqlAGTMSGGEQQMLAMGRALMTRPKVLLLDE 167
Cdd:PRK13634 97 Q--LFEETVEKDICFGPMnfgVSEEDAKQKAReMIELVGLPEELLARS---PFELSGGQMRRVAIAGVLAMEPEVLVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2032805432 168 PSMGLSPIMVDKIFEVVNDIH-SQGVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLLNDP 232
Cdd:PRK13634 172 PTAGLDPKGRKEMMEMFYKLHkEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
27-223 |
3.15e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 50.74 E-value: 3.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 27 VDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAageiEFMGKTLKGQGAWdlvkqglvmVPEGRGTFTrMTITENLLM 106
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHA----ETSSVVIRGSVAY---------VPQVSWIFN-ATVRENILF 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 107 GAYIRDDKAQIEADIERI---FGIFP-RLKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLLDEPSMGLSPIMVDKIFE 182
Cdd:PLN03232 702 GSDFESERYWRAIDVTALqhdLDLLPgRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFD 781
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2032805432 183 VVNDIHSQGVTVLLVeQNASRALQLASRGYVMESGLITMTG 223
Cdd:PLN03232 782 SCMKDELKGKTRVLV-TNQLHFLPLMDRIILVSEGMIKEEG 821
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
26-169 |
3.24e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 50.74 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 26 GVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLvKQGLVMVPEGRGTFT---RMTI-- 100
Cdd:PLN03232 1254 GLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDL-RRVLSIIPQSPVLFSgtvRFNIdp 1332
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032805432 101 -TENLLMGAYIRDDKAQIEADIER-IFGIFPRLKERrnqlAGTMSGGEQQMLAMGRALMTRPKVLLLDEPS 169
Cdd:PLN03232 1333 fSEHNDADLWEALERAHIKDVIDRnPFGLDAEVSEG----GENFSVGQRQLLSLARALLRRSKILVLDEAT 1399
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
16-196 |
3.76e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.40 E-value: 3.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 16 VAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVA-AGEIEFMGKTlKGQGA--WDlVKQGLVMVPEGR 92
Cdd:PRK10938 268 VSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGySNDLTLFGRR-RGSGEtiWD-IKKHIGYVSSSL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 93 GTFTRMTIT-ENLLMGAYIrddkaqieadiERIfGIFPRLKERRNQLAG------------------TMSGGEQQMLAMG 153
Cdd:PRK10938 346 HLDYRVSTSvRNVILSGFF-----------DSI-GIYQAVSDRQQKLAQqwldilgidkrtadapfhSLSWGQQRLALIV 413
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2032805432 154 RALMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQGVTVLL 196
Cdd:PRK10938 414 RALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLL 456
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
20-195 |
4.01e-07 |
|
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: 49.18 E-value: 4.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 20 GIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAA---GEIEFMGKTLKgqGAWDLVKQGLVMVPEGRGTFT 96
Cdd:cd03233 19 KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYK--EFAEKYPGEIIYVSEEDVHFP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 97 RMTITENLlmgayirdDKAqieadierifgifprLKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLLDEPSMGLSPIM 176
Cdd:cd03233 97 TLTVRETL--------DFA---------------LRCKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSST 153
|
170 180
....*....|....*....|...
gi 2032805432 177 VdkiFEVVNDI----HSQGVTVL 195
Cdd:cd03233 154 A---LEILKCIrtmaDVLKTTTF 173
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
23-219 |
6.00e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 49.89 E-value: 6.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 23 AVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLqpvaageiefmgkTLKGQGAWDlVKQGLVMVPEGRGTFTRMTITE 102
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGV-------------TMPNKGTVD-IKGSAALIAISSGLNGQLTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 103 NL-LMGAYIRDDKAQIEADIERIFGiFPRLKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLLDEP-SMGlSPIMVDKI 180
Cdd:PRK13545 105 NIeLKGLMMGLTKEKIKEIIPEIIE-FADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEAlSVG-DQTFTKKC 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2032805432 181 FEVVNDIHSQGVTVLLVEQNASRALQLASR------GYVMESGLI 219
Cdd:PRK13545 183 LDKMNEFKEQGKTIFFISHSLSQVKSFCTKalwlhyGQVKEYGDI 227
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
8-210 |
6.31e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 48.69 E-value: 6.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 8 LLKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQgLVM 87
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAY-LGH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 88 VPegrGTFTRMTITENL--LMGAYIRDDKaQIEADIERIFGifprLKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLL 165
Cdd:PRK13543 90 LP---GLKADLSTLENLhfLCGLHGRRAK-QMPGSALAIVG----LAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2032805432 166 DEPSMGLSP---IMVDKIfeVVNDIHSQGVTvLLVEQNASRALQLASR 210
Cdd:PRK13543 162 DEPYANLDLegiTLVNRM--ISAHLRGGGAA-LVTTHGAYAAPPVRTR 206
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
34-226 |
7.46e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 49.49 E-value: 7.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 34 GELVSLIGANGAGKTTTLKAVtglqpvaAGEIE---FMGKTLKGQGawDLVKQGLV---MVPEGRGTFTRMTITENLLMG 107
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNAL-------AGRIQgnnFTGTILANNR--KPTKQILKrtgFVTQDDILYPHLTVRETLVFC 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 108 AYIR-------DDKAQIEADIERIFGifprLKERRNQLAGT-----MSGGEQQMLAMGRALMTRPKVLLLDEPSMGLSPI 175
Cdd:PLN03211 165 SLLRlpksltkQEKILVAESVISELG----LTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDAT 240
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2032805432 176 MVDKIFEVVNDIHSQGVTVLL-VEQNASRALQLASRGYVMESGLITMTGEGK 226
Cdd:PLN03211 241 AAYRLVLTLGSLAQKGKTIVTsMHQPSSRVYQMFDSVLVLSEGRCLFFGKGS 292
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
14-232 |
9.54e-07 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 48.75 E-value: 9.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 14 LKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQP----VAAGEIEFMGKtlkgqgawDLVKqglvMVP 89
Cdd:COG4170 13 IDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGI--------DLLK----LSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 90 EGRgtftRMTITENLLM-----GAYIrDDKAQIEADI-ERIFGI------FPRLKERRNQLAGTM--------------- 142
Cdd:COG4170 81 RER----RKIIGREIAMifqepSSCL-DPSAKIGDQLiEAIPSWtfkgkwWQRFKWRKKRAIELLhrvgikdhkdimnsy 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 143 ----SGGEQQ--MLAMgrALMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIH-SQGVTVLLVEQNASRALQLASRGYVME 215
Cdd:COG4170 156 phelTEGECQkvMIAM--AIANQPRLLIADEPTNAMESTTQAQIFRLLARLNqLQGTSILLISHDLESISQWADTITVLY 233
|
250
....*....|....*..
gi 2032805432 216 SGLITMTGEGKTLLNDP 232
Cdd:COG4170 234 CGQTVESGPTEQILKSP 250
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
25-167 |
1.70e-06 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 48.28 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 25 KGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIefmgkTLKGQgawDL--VKQGLV-----MVPEGrgtfTR 97
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRI-----LIDGQ---DIrdVTQASLraaigIVPQD----TV 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 98 M---TITENLlmgAYIRDD--KAQIEADIE--RIFGIFPRLKERRNQLAG----TMSGGEQQMLAMGRALMTRPKVLLLD 166
Cdd:COG5265 443 LfndTIAYNI---AYGRPDasEEEVEAAARaaQIHDFIESLPDGYDTRVGerglKLSGGEKQRVAIARTLLKNPPILIFD 519
|
.
gi 2032805432 167 E 167
Cdd:COG5265 520 E 520
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
23-167 |
2.31e-06 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 48.09 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 23 AVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQgLVMVPEGRGTFTRmTITE 102
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQ-VALVSQNVHLFND-TIAN 435
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032805432 103 NLlmgAYIRDDK---AQIE--ADIERIFGIFPRLKERRNQLAG----TMSGGEQQMLAMGRALMTRPKVLLLDE 167
Cdd:PRK11176 436 NI---AYARTEQysrEQIEeaARMAYAMDFINKMDNGLDTVIGengvLLSGGQRQRIAIARALLRDSPILILDE 506
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-215 |
3.03e-06 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 47.02 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 30 EVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEfmgktlkgqgaWDLVK-----QGLVMVPEGRGTFTRMTITENL 104
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIE-----------IELDTvsykpQYIKADYEGTVRDLLSSITKDF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 105 LMGAYIRDDKAQiEADIERIFgifprlkerrNQLAGTMSGGEQQMLAMGRALMTRPKVLLLDEPSMGLSP---IMVDKIF 181
Cdd:cd03237 90 YTHPYFKTEIAK-PLQIEQIL----------DREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVeqrLMASKVI 158
|
170 180 190
....*....|....*....|....*....|....
gi 2032805432 182 EVVNDIHSQgvTVLLVEQNASRALQLASRGYVME 215
Cdd:cd03237 159 RRFAENNEK--TAFVVEHDIIMIDYLADRLIVFE 190
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
23-232 |
3.05e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 47.40 E-value: 3.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 23 AVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKgQGAWDLVKQGLVMVPEGRGTFTRmTITE 102
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLT-KLQLDSWRSRLAVVSQTPFLFSD-TVAN 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 103 NLLMGayiRDD--KAQIEA---------DIERI-FGIFPRLKERrnqlaGTM-SGGEQQMLAMGRALMTRPKVLLLDEps 169
Cdd:PRK10789 408 NIALG---RPDatQQEIEHvarlasvhdDILRLpQGYDTEVGER-----GVMlSGGQKQRISIARALLLNAEILILDD-- 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032805432 170 mGLSPIMVDKIFEVVNDIHS--QGVTVLLVEQNASrALQLASRGYVMESGLITMTGEGKTLLNDP 232
Cdd:PRK10789 478 -ALSAVDGRTEHQILHNLRQwgEGRTVIISAHRLS-ALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
8-87 |
4.35e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 46.32 E-value: 4.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 8 LLKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQ--PVAAGEIEFMGKTLKGQGAWDLVKQGL 85
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAGEGI 80
|
..
gi 2032805432 86 VM 87
Cdd:PRK09580 81 FM 82
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
137-200 |
7.86e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 46.54 E-value: 7.86e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032805432 137 QLAGTMSGGEQQMLAMGRALMTR---PKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQN 200
Cdd:TIGR00630 825 QPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHN 891
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
4-169 |
1.13e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 45.93 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 4 SKEILLKVSGLKVAYGGIQ-AVKGVdfEVRRGELVSLIGANGAGKTTTLKAVTG-LQPVaAGEIEFMGK-TLKGQgawdl 80
Cdd:COG1245 337 EEETLVEYPDLTKSYGGFSlEVEGG--EIREGEVLGIVGPNGIGKTTFAKILAGvLKPD-EGEVDEDLKiSYKPQ----- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 81 vkqglVMVPEGRGT---FTRMTITENLlmgayirdDKAQIEADIERIFGIfPRLKERRnqlAGTMSGGEQQMLAMGRALM 157
Cdd:COG1245 409 -----YISPDYDGTveeFLRSANTDDF--------GSSYYKTEIIKPLGL-EKLLDKN---VKDLSGGELQRVAIAACLS 471
|
170
....*....|..
gi 2032805432 158 TRPKVLLLDEPS 169
Cdd:COG1245 472 RDADLYLLDEPS 483
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
25-167 |
1.24e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 44.95 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 25 KGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQpvaageiefmgKTLKGQGAWDLVKqglvmvpegrGTFTR-MTITEN 103
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL-----------KGTPVAGCVDVPD----------NQFGReASLIDA 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032805432 104 LlmgaYIRDDKAQIeadIERI--------FGIFPRLKErrnqlagtMSGGEQQMLAMGRALMTRPKVLLLDE 167
Cdd:COG2401 106 I----GRKGDFKDA---VELLnavglsdaVLWLRRFKE--------LSTGQKFRFRLALLLAERPKLLVIDE 162
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
137-200 |
1.42e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 44.91 E-value: 1.42e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032805432 137 QLAGTMSGGEQQMLAMGRALM---TRPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQN 200
Cdd:cd03271 165 QPATTLSGGEAQRIKLAKELSkrsTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHN 231
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
139-198 |
1.48e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 44.56 E-value: 1.48e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032805432 139 AGTMSGGEQQMLAMGRALMTRPKVLL--LDEPSMGLSPIMVDKIFEVVNDIHSQGVTVLLVE 198
Cdd:cd03270 135 APTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVE 196
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
27-168 |
1.92e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.50 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 27 VDFEVRRGELVSLIGANGAGKTTTLKAVTG-LQPVAAGEIefmgkTLKGQGAWdlvkqglvmVPEGRGTFTrMTITENLL 105
Cdd:PLN03130 636 INLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASV-----VIRGTVAY---------VPQVSWIFN-ATVRDNIL 700
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032805432 106 MGAYI---RDDKAQIEADIERIFGIFP-----RLKERrnqlAGTMSGGEQQMLAMGRALMTRPKVLLLDEP 168
Cdd:PLN03130 701 FGSPFdpeRYERAIDVTALQHDLDLLPggdltEIGER----GVNISGGQKQRVSMARAVYSNSDVYIFDDP 767
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
22-172 |
3.38e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 44.71 E-value: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 22 QAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTglQPVAAGEIEfMGKTLKGQGAWD--------LVKQGLVMVPEgrg 93
Cdd:TIGR00956 777 VILNNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTGVIT-GGDRLVNGRPLDssfqrsigYVQQQDLHLPT--- 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 94 tftrMTITENLLMGAYIRDDK--AQIEAD--IERIFGIFpRLKERRNQLAGTMSGG---EQ-QMLAMGRALMTRPKVLL- 164
Cdd:TIGR00956 851 ----STVRESLRFSAYLRQPKsvSKSEKMeyVEEVIKLL-EMESYADAVVGVPGEGlnvEQrKRLTIGVELVAKPKLLLf 925
|
....*...
gi 2032805432 165 LDEPSMGL 172
Cdd:TIGR00956 926 LDEPTSGL 933
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
22-172 |
4.99e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 43.94 E-value: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 22 QAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVT----GLQPVAAGEIEFMGKTLKgqgawDLVKQ---GLVMVPEGRGT 94
Cdd:TIGR00956 75 DILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPE-----EIKKHyrgDVVYNAETDVH 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 95 FTRMTITENLLMGAYI-----------RDDKAQIEAD-IERIFGifprLKERRNQLAGT-----MSGGEQQMLAMGRALM 157
Cdd:TIGR00956 150 FPHLTVGETLDFAARCktpqnrpdgvsREEYAKHIADvYMATYG----LSHTRNTKVGNdfvrgVSGGERKRVSIAEASL 225
|
170
....*....|....*
gi 2032805432 158 TRPKVLLLDEPSMGL 172
Cdd:TIGR00956 226 GGAKIQCWDNATRGL 240
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-59 |
5.71e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 43.79 E-value: 5.71e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2032805432 4 SKEILLKVSGLKVAYGGIQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTG-LQP 59
Cdd:PRK11147 315 SGKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGqLQA 371
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
95-198 |
1.24e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 42.69 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 95 FTRMTITENL--LMGAYIRDDKAQIEADIERifGIFPRLK------------ERRnqlAGTMSGGEQQMLAM----GRAL 156
Cdd:TIGR00630 433 VSELSIREAHefFNQLTLTPEEKKIAEEVLK--EIRERLGflidvgldylslSRA---AGTLSGGEAQRIRLatqiGSGL 507
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2032805432 157 MtrpKVL-LLDEPSMGLSPIMVDKIFEVVNDIHSQGVTVLLVE 198
Cdd:TIGR00630 508 T---GVLyVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVE 547
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
141-200 |
1.35e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 1.35e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032805432 141 TMSGGEQQMLAMGRALMT---RPKVLLLDEPSMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQN 200
Cdd:PRK00635 809 SLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHN 871
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
24-167 |
2.72e-04 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 41.85 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 24 VKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEFMGKTLKGQGAWDLVKQgLVMVPEGRGTFT---RMTI 100
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFK-ITIIPQDPVLFSgslRMNL 1380
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032805432 101 TEnllMGAYiRDDKAQIEADIERIFGIFPRLKERRNQLAG----TMSGGEQQMLAMGRALMTRPKVLLLDE 167
Cdd:TIGR00957 1381 DP---FSQY-SDEEVWWALELAHLKTFVSALPDKLDHECAeggeNLSVGQRQLVCLARALLRKTKILVLDE 1447
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
141-172 |
2.72e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.94 E-value: 2.72e-04
10 20 30
....*....|....*....|....*....|..
gi 2032805432 141 TMSGGEQQMLAMGRALMTRPKVLLLDEPSMGL 172
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSL 1389
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
142-232 |
9.13e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 39.79 E-value: 9.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 142 MSGGEQQMLAMGRALMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIH-SQGVTVLLVEQNASRALQLASRGYVMESGLIT 220
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNqNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
90
....*....|..
gi 2032805432 221 MTGEGKTLLNDP 232
Cdd:PRK15093 239 ETAPSKELVTTP 250
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
23-229 |
1.02e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 39.41 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 23 AVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQPVAAGEIEfmgktlkgqgawdlvKQGLVMVPE-GRGTFTRMTIT 101
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD---------------RNGEVSVIAiSAGLSGQLTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 102 EN-----LLMGAYIRDDKAQIEADIErifgiFPRLKERRNQLAGTMSGGEQQMLAMGRALMTRPKVLLLDEP-SMG---L 172
Cdd:PRK13546 104 ENiefkmLCMGFKRKEIKAMTPKIIE-----FSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEAlSVGdqtF 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2032805432 173 SPIMVDKIFEvvndIHSQGVTVLLVEQNASRALQLASRGYVMESGLITMTGEGKTLL 229
Cdd:PRK13546 179 AQKCLDKIYE----FKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL 231
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
137-200 |
1.05e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.06 E-value: 1.05e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032805432 137 QLAGTMSGGEQQMLAMGRALMTRP--KVL-LLDEPSMGLSPIMVDKIFEVVNDIHSQGVTVLLVEQN 200
Cdd:PRK00349 826 QPATTLSGGEAQRVKLAKELSKRStgKTLyILDEPTTGLHFEDIRKLLEVLHRLVDKGNTVVVIEHN 892
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
33-198 |
1.08e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 38.49 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 33 RGELVSLIGANGAGKTTTLKAVtGLqpVAAGEiefmgktlkgqgawdlvkqglvMVPEGRGTftrmtitenllmGAYIRD 112
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDAI-GL--ALGGA----------------------QSATRRRS------------GVKAGC 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 113 DKAQIEAdiERIFgifprlkeRRNQLagtmSGGEQQM----LAMGRALMTRPKVLLLDEPSMGLSPIMVDKIFEVVNDIH 188
Cdd:cd03227 63 IVAAVSA--ELIF--------TRLQL----SGGEKELsalaLILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHL 128
|
170
....*....|
gi 2032805432 189 SQGVTVLLVE 198
Cdd:cd03227 129 VKGAQVIVIT 138
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-198 |
1.28e-03 |
|
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: 39.38 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 32 RRGELVSLIGANGAGKTTTLKAVTG-LQPvAAGEIEfmgktlkGQGAWDLVKQglvmvpEGRGT-----FTRM------- 98
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGeLKP-NLGDYD-------EEPSWDEVLK------RFRGTelqdyFKKLangeikv 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 99 ----------------TITEnLLMGAyirDDKAQIEADIERIfgifpRLKERRNQLAGTMSGGEQQMLAMGRALMTRPKV 162
Cdd:COG1245 163 ahkpqyvdlipkvfkgTVRE-LLEKV---DERGKLDELAEKL-----GLENILDRDISELSGGELQRVAIAAALLRDADF 233
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2032805432 163 LLLDEPSMGLspimvDkIFE------VVNDIHSQGVTVLLVE 198
Cdd:COG1245 234 YFFDEPSSYL-----D-IYQrlnvarLIRELAEEGKYVLVVE 269
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
139-172 |
1.42e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 39.63 E-value: 1.42e-03
10 20 30
....*....|....*....|....*....|....
gi 2032805432 139 AGTMSGGEQQMLAMGRALMTRPKVLLLDEPSMGL 172
Cdd:PTZ00265 577 ASKLSGGQKQRISIARAIIRNPKILILDEATSSL 610
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
39-168 |
2.76e-03 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 38.38 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 39 LIGANGAGKTTTLKAVTGLqpvaagEIEFMGKTLKGQGA-----------------WDLVKQGlvmVPEGRGTFTRMtit 101
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGV------DKDFNGEARPQPGIkvgylpqepqldptktvRENVEEG---VAEIKDALDRF--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 102 eNLLMGAYIRDD-------------KAQIEA----DIERifgifpRLKERRNQL--------AGTMSGGEQQMLAMGRAL 156
Cdd:TIGR03719 104 -NEISAKYAEPDadfdklaaeqaelQEIIDAadawDLDS------QLEIAMDALrcppwdadVTKLSGGERRRVALCRLL 176
|
170
....*....|..
gi 2032805432 157 MTRPKVLLLDEP 168
Cdd:TIGR03719 177 LSKPDMLLLDEP 188
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
39-169 |
2.98e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 38.69 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 39 LIGANGAGKTTTLK-----AVTGL----------QPVAAGEIEFMGKTLKGQgawdlVKQGLVMVPEGRGTFTRMTITEN 103
Cdd:PLN03073 208 LVGRNGTGKTTFLRymamhAIDGIpkncqilhveQEVVGDDTTALQCVLNTD-----IERTQLLEEEAQLVAQQRELEFE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 104 LLMGAYIRDDKAQIEADI--ERIFGIFPRLK-------ERRNQ--LAG-------------TMSGGEQQMLAMGRALMTR 159
Cdd:PLN03073 283 TETGKGKGANKDGVDKDAvsQRLEEIYKRLElidaytaEARAAsiLAGlsftpemqvkatkTFSGGWRMRIALARALFIE 362
|
170
....*....|
gi 2032805432 160 PKVLLLDEPS 169
Cdd:PLN03073 363 PDLLLLDEPT 372
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
21-172 |
9.30e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 37.13 E-value: 9.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 21 IQAVKGVDFEVRRGELVSLIGANGAGKTTTLKAVTGLQpvAAGEIEfmgktlkgqgaWDLVKQGLvmvPEGRGTFTRM-- 98
Cdd:PLN03140 893 LQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRK--TGGYIE-----------GDIRISGF---PKKQETFARIsg 956
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032805432 99 ------------TITENLLMGAYIR-------DDKAQIEADIERIFGIfPRLKERRNQLAGT--MSGGEQQMLAMGRALM 157
Cdd:PLN03140 957 yceqndihspqvTVRESLIYSAFLRlpkevskEEKMMFVDEVMELVEL-DNLKDAIVGLPGVtgLSTEQRKRLTIAVELV 1035
|
170
....*....|....*
gi 2032805432 158 TRPKVLLLDEPSMGL 172
Cdd:PLN03140 1036 ANPSIIFMDEPTSGL 1050
|
|
| |
