|
Name |
Accession |
Description |
Interval |
E-value |
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-243 |
6.36e-133 |
|
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: 375.09 E-value: 6.36e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 2 TQDAIIQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAMV 81
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 82 ERRFGVLFQRGALFSSLTVTENVALPLIENAGLPRSEAERLAQVKLALAGLpPGTGSKYPASLSGGMVKRVALARALALD 161
Cdd:COG1127 81 RRRIGMLFQGGALFDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGL-PGAADKMPSELSGGMRKRVALARALALD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 162 PDILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDTLDKVAATDDGWIQA 241
Cdd:COG1127 160 PEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASDDPWVRQ 239
|
..
gi 553371603 242 YF 243
Cdd:COG1127 240 FL 241
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
7-242 |
3.49e-113 |
|
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: 324.84 E-value: 3.49e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 7 IQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAMVERRFG 86
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 87 VLFQRGALFSSLTVTENVALPLIENAGLPRSEAERLAQVKLALAGLPpGTGSKYPASLSGGMVKRVALARALALDPDILF 166
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLR-GAEDLYPAELSGGMKKRVALARALALDPELLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 553371603 167 LDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDTLDKVAATDDGWIQAY 242
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASDDPLVRQF 235
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-222 |
1.67e-63 |
|
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: 198.57 E-value: 1.67e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 6 IIQIRDLVNCFGVQCVH----QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAMV 81
Cdd:cd03258 1 MIELKNVSKVFGDTGGKvtalKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 82 ERRFGVLFQRGALFSSLTVTENVALPLiENAGLPRSEAERLAQVKLALAGLpPGTGSKYPASLSGGMVKRVALARALALD 161
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPL-EIAGVPKAEIEERVLELLELVGL-EDKADAYPAQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 553371603 162 PDILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKV 222
Cdd:cd03258 159 PKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
23-222 |
9.79e-63 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 199.92 E-value: 9.79e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 23 QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAMVERRFGVLFQRGALFSSLTVTE 102
Cdd:COG1135 22 DDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAARRKIGMIFQHFNLLSSRTVAE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 103 NVALPLiENAGLPRseAERLAQVK--LALAGLpPGTGSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAA 180
Cdd:COG1135 102 NVALPL-EIAGVPK--AEIRKRVAelLELVGL-SDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTR 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 553371603 181 AFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKV 222
Cdd:COG1135 178 SILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
7-233 |
1.20e-62 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 196.44 E-value: 1.20e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 7 IQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRamveRRFG 86
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVR----RRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 87 VLFQRGALFSSLTVTENVALpLIENAGLPRSEAERLAQVKLALAGLPPgTGSKYPASLSGGMVKRVALARALALDPDILF 166
Cdd:COG1131 77 YVPQEPALYPDLTVRENLRF-FARLYGLPRKEARERIDELLELFGLTD-AADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 553371603 167 LDEPTAGLDPIGAAAFDSLIRTLRDAlNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDTLDKVAA 233
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKA 220
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-217 |
1.22e-61 |
|
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: 193.49 E-value: 1.22e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 6 IIQIRDLVNCFGVQCVH----QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAMV 81
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSvkalDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 82 ERRFGVLFQ--RGALFSSLTVTENVALPLIENAGLPRSEAERLAQVKLALA-GLPPGTGSKYPASLSGGMVKRVALARAL 158
Cdd:cd03257 81 RKEIQMVFQdpMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGvGLPEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 553371603 159 ALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVL 217
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVM 219
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-219 |
1.64e-61 |
|
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: 201.67 E-value: 1.64e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 2 TQDAIIQIRDLVNCFGVQCVH-----QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQ 76
Cdd:COG1123 256 AAEPLLEVRNLSKRYPVRGKGgvravDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 77 SRAMVERRFGVLFQ--RGALFSSLTVTENVALPLIENAGLPRSEAERLAQVKLALAGLPPGTGSKYPASLSGGMVKRVAL 154
Cdd:COG1123 336 SLRELRRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQRVAI 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 553371603 155 ARALALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQ 219
Cdd:COG1123 416 ARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYD 480
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
7-219 |
1.40e-58 |
|
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: 184.31 E-value: 1.40e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 7 IQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAMvERRFG 86
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPL-RRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 87 VLFQRGALFSSLTVTENVALPLienaglprseaerlaqvklalaglppgtgskypaslSGGMVKRVALARALALDPDILF 166
Cdd:cd03229 80 MVFQDFALFPHLTVLENIALGL------------------------------------SGGQQQRVALARALAMDPDVLL 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 553371603 167 LDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQ 219
Cdd:cd03229 124 LDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
7-229 |
2.34e-58 |
|
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: 184.98 E-value: 2.34e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 7 IQIRDLVNCFG----VQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKdlmALSGQSRAMve 82
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE---PVTGPGPDR-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 83 rrfGVLFQRGALFSSLTVTENVALPLiENAGLPRSEAERLAQVKLALAGLPpGTGSKYPASLSGGMVKRVALARALALDP 162
Cdd:cd03293 76 ---GYVFQQDALLPWLTVLDNVALGL-ELQGVPKAEARERAEELLELVGLS-GFENAYPHQLSGGMRQRVALARALAVDP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 553371603 163 DILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDTLD 229
Cdd:cd03293 151 DVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSARPGRIVAEVE 217
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
23-218 |
2.06e-57 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 183.75 E-value: 2.06e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 23 QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQsRAMVerrfgvlFQRGALFSSLTVTE 102
Cdd:COG1116 28 DDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-RGVV-------FQEPALLPWLTVLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 103 NVALPLiENAGLPRSEAERLAQVKLALAGLPpGTGSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAAAF 182
Cdd:COG1116 100 NVALGL-ELRGVPKAERRERARELLELVGLA-GFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERL 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 553371603 183 DSLIRTLRDALNLTVFLVTHDLD-TLYtLCDRVAVLS 218
Cdd:COG1116 178 QDELLRLWQETGKTVLFVTHDVDeAVF-LADRVVVLS 213
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
3-227 |
9.01e-56 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 182.61 E-value: 9.01e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 3 QDAIIQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQsramvE 82
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE-----K 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 83 RRFGVLFQRGALFSSLTVTENVALPLiENAGLPRSEAERLAQVKLALAGLpPGTGSKYPASLSGGMVKRVALARALALDP 162
Cdd:COG3842 77 RNVGMVFQDYALFPHLTVAENVAFGL-RMRGVPKAEIRARVAELLELVGL-EGLADRYPHQLSGGQQQRVALARALAPEP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 553371603 163 DILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDT 227
Cdd:COG3842 155 RVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGT 219
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
23-221 |
1.50e-55 |
|
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: 177.66 E-value: 1.50e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 23 QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAmveRRFGVLFQRGAL-FSSLTVT 101
Cdd:cd03225 18 DDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELR---RKVGLVFQNPDDqFFGPTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 102 ENVALPLiENAGLPRSEAERLAQVKLALAGLPpGTGSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAAA 181
Cdd:cd03225 95 EEVAFGL-ENLGLPEEEIEERVEEALELVGLE-GLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 553371603 182 FDSLIRTLRDAlNLTVFLVTHDLDTLYTLCDRVAVLSQKK 221
Cdd:cd03225 173 LLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
23-231 |
3.29e-55 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 177.14 E-value: 3.29e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 23 QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAmveRRFGVLFQ--RGALFSSlTV 100
Cdd:COG1122 18 DDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELR---RKVGLVFQnpDDQLFAP-TV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 101 TENVALPLiENAGLPRSEAERLAQVKLALAGLPpGTGSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAA 180
Cdd:COG1122 94 EEDVAFGP-ENLGLPREEIRERVEEALELVGLE-HLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRR 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 553371603 181 AFDSLIRTLRDAlNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDTLDKV 231
Cdd:COG1122 172 ELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
7-222 |
8.18e-55 |
|
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: 174.12 E-value: 8.18e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 7 IQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLmalsGQSRAMVERRFG 86
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI----KKEPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 87 VLFQRGALFSSLTVTENValplienaglprseaerlaqvklalaglppgtgskypaSLSGGMVKRVALARALALDPDILF 166
Cdd:cd03230 77 YLPEEPSLYENLTVRENL--------------------------------------KLSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 553371603 167 LDEPTAGLDPIGAAAFDSLIRTLRDAlNLTVFLVTHDLDTLYTLCDRVAVLSQKKV 222
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
7-226 |
1.04e-54 |
|
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: 175.40 E-value: 1.04e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 7 IQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQsramvERRFG 86
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE-----RRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 87 VLFQRGALFSSLTVTENVALPLiENAGLPRSEAERLAQVKLALAGLPpGTGSKYPASLSGGMVKRVALARALALDPDILF 166
Cdd:cd03259 76 MVFQDYALFPHLTVAENIAFGL-KLRGVPKAEIRARVRELLELVGLE-GLLNRYPHELSGGQQQRVALARALAREPSLLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 167 LDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVD 226
Cdd:cd03259 154 LDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
4-218 |
1.48e-53 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 172.92 E-value: 1.48e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 4 DAIIQIRDLVNCF--GVQCVH--QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRA 79
Cdd:COG1136 2 SPLLELRNLTKSYgtGEGEVTalRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 80 MVERR-FGVLFQRGALFSSLTVTENVALPLIeNAGLPRSEAERLAQVKLALAGLPpGTGSKYPASLSGGMVKRVALARAL 158
Cdd:COG1136 82 RLRRRhIGFVFQFFNLLPELTALENVALPLL-LAGVSRKERRERARELLERVGLG-DRLDHRPSQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 159 ALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDtLYTLCDRVAVLS 218
Cdd:COG1136 160 VNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPE-LAARADRVIRLR 218
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
6-223 |
8.26e-53 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 171.33 E-value: 8.26e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 6 IIQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLmALSGQSRAMVERRF 85
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDINKLRRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 86 GVLFQRGALFSSLTVTENVALPLIENAGLPRSEAERLAQVKLALAGLPpGTGSKYPASLSGGMVKRVALARALALDPDIL 165
Cdd:COG1126 80 GMVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLA-DKADAYPAQLSGGQQQRVAIARALAMEPKVM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 553371603 166 FLDEPTAGLDP--IGaaafDSL--IRTLRDAlNLTVFLVTHDLDTLYTLCDRVAVLSQKKVL 223
Cdd:COG1126 159 LFDEPTSALDPelVG----EVLdvMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIV 215
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
4-227 |
8.86e-53 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 174.84 E-value: 8.86e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 4 DAIIQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAmver 83
Cdd:TIGR03265 2 SPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRD---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 84 rFGVLFQRGALFSSLTVTENVALPLiENAGLPRSEAERLAQVKLALAGLPpGTGSKYPASLSGGMVKRVALARALALDPD 163
Cdd:TIGR03265 78 -YGIVFQSYALFPNLTVADNIAYGL-KNRGMGRAEVAERVAELLDLVGLP-GSERKYPGQLSGGQQQRVALARALATSPG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 553371603 164 ILFLDEPTAGLDpigAAAFDSL---IRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDT 227
Cdd:TIGR03265 155 LLLLDEPLSALD---ARVREHLrteIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGT 218
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
7-222 |
1.50e-52 |
|
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: 169.98 E-value: 1.50e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 7 IQIRDLVNCFGVQCVH----QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAMVE 82
Cdd:cd03255 1 IELKNLSKTYGGGGEKvqalKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 83 RR-FGVLFQRGALFSSLTVTENVALPLIEnAGLPRSEAERLAQVKLALAGLPpGTGSKYPASLSGGMVKRVALARALALD 161
Cdd:cd03255 81 RRhIGFVFQSFNLLPDLTALENVELPLLL-AGVPKKERRERAEELLERVGLG-DRLNHYPSELSGGQQQRVAIARALAND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 553371603 162 PDILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDtLYTLCDRVAVLSQKKV 222
Cdd:cd03255 159 PKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPE-LAEYADRIIELRDGKI 218
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
7-231 |
2.35e-52 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 173.41 E-value: 2.35e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 7 IQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMA-LSGQsramvERRF 85
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTnLPPR-----ERRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 86 GVLFQRGALFSSLTVTENVAlplienAGL---PRSEAERLAQVK--LALAGLPpGTGSKYPASLSGGMVKRVALARALAL 160
Cdd:COG1118 78 GFVFQHYALFPHMTVAENIA------FGLrvrPPSKAEIRARVEelLELVQLE-GLADRYPSQLSGGQRQRVALARALAV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 553371603 161 DPDILFLDEPTAGLDpigAAAFDSLIRTLR---DALNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDTLDKV 231
Cdd:COG1118 151 EPEVLLLDEPFGALD---AKVRKELRRWLRrlhDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
7-217 |
3.62e-52 |
|
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: 169.98 E-value: 3.62e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 7 IQIRDLVNCFGV----QCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAmve 82
Cdd:COG1124 2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 83 RRFGVLFQ--RGALFSSLTVTENVALPLiENAGLPRSEaERLAQVkLALAGLPPGTGSKYPASLSGGMVKRVALARALAL 160
Cdd:COG1124 79 RRVQMVFQdpYASLHPRHTVDRILAEPL-RIHGLPDRE-ERIAEL-LEQVGLPPSFLDRYPHQLSGGQRQRVAIARALIL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 553371603 161 DPDILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVL 217
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVM 212
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
23-222 |
4.14e-52 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 172.68 E-value: 4.14e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 23 QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAMVERRFGVLFQRGALFSSLTVTE 102
Cdd:PRK11153 22 NNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKARRQIGMIFQHFNLLSSRTVFD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 103 NVALPLiENAGLPRSEAERLAQVKLALAGLppgtgS----KYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIG 178
Cdd:PRK11153 102 NVALPL-ELAGTPKAEIKARVTELLELVGL-----SdkadRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPAT 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 553371603 179 AAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKV 222
Cdd:PRK11153 176 TRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
26-227 |
5.40e-52 |
|
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: 170.52 E-value: 5.40e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 26 NLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALS-GQSRAMVERRFGVLFQRGALFSSLTVTENV 104
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrKELRELRRKKISMVFQSFALLPHRTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 105 ALPLiENAGLPRSEAERLAQVKLALAGLPpGTGSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPigaaafds 184
Cdd:cd03294 124 AFGL-EVQGVPRAEREERAAEALELVGLE-GWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDP-------- 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 553371603 185 LIRT--------LRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDT 227
Cdd:cd03294 194 LIRRemqdellrLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGT 244
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-217 |
4.46e-51 |
|
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: 169.46 E-value: 4.46e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 6 IIQIRDLVNCFGV--QCVH--QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRP---TDGKIHVFGKDLMALSG-QS 77
Cdd:COG0444 1 LLEVRNLKVYFPTrrGVVKavDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEkEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 78 RAMVERRFGVLFQrgALFSSL----TVTENVALPLIENAGLPRSEAERLAQVKLALAGLPPGTG--SKYPASLSGGMVKR 151
Cdd:COG0444 81 RKIRGREIQMIFQ--DPMTSLnpvmTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERrlDRYPHELSGGMRQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 553371603 152 VALARALALDPDILFLDEPTAGLDP-IGAAAFDsLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVL 217
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVtIQAQILN-LLKDLQRELGLAILFITHDLGVVAEIADRVAVM 224
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
26-227 |
5.08e-51 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 168.01 E-value: 5.08e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 26 NLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAMVERRFGVLFQRGA--LFSsLTVTEN 103
Cdd:TIGR04521 25 SLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLRKKVGLVFQFPEhqLFE-ETVYKD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 104 VAL-PLieNAGLPRSEAERLAQVKLALAGLPPGTGSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAAAF 182
Cdd:TIGR04521 104 IAFgPK--NLGLSEEEAEERVKEALELVGLDEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEI 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 553371603 183 DSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDT 227
Cdd:TIGR04521 182 LDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGT 226
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
7-219 |
5.43e-51 |
|
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: 165.78 E-value: 5.43e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 7 IQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMAlSGQSRAMVERRFG 86
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 87 VLFQRGALFSSLTVTENVALPLIENAGLPRSEAERLAQVKLALAGLPPgTGSKYPASLSGGMVKRVALARALALDPDILF 166
Cdd:cd03262 80 MVFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLAD-KADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 553371603 167 LDEPTAGLDPigaaafdSLIRTLRDAL------NLTVFLVTHDLDTLYTLCDRVAVLSQ 219
Cdd:cd03262 159 FDEPTSALDP-------ELVGEVLDVMkdlaeeGMTMVVVTHEMGFAREVADRVIFMDD 210
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-222 |
1.98e-49 |
|
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: 170.08 E-value: 1.98e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 4 DAIIQIRDLVNCFGVQCVH--QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPT---DGKIHVFGKDLMALSGQSR 78
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVPavDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 79 AmveRRFGVLFQR-GALFSSLTVTENVALPLiENAGLPRSEAERLAQVKLALAGLPpGTGSKYPASLSGGMVKRVALARA 157
Cdd:COG1123 82 G---RRIGMVFQDpMTQLNPVTVGDQIAEAL-ENLGLSRAEARARVLELLEAVGLE-RRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 553371603 158 LALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKV 222
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRI 221
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-245 |
2.56e-49 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 163.40 E-value: 2.56e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 1 MTQDAIIQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAM 80
Cdd:PRK11831 2 QSVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 81 VERRFGVLFQRGALFSSLTVTENVALPLIENAGLPRSEAERLAQVKLALAGLpPGTGSKYPASLSGGMVKRVALARALAL 160
Cdd:PRK11831 82 VRKRMSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGL-RGAAKLMPSELSGGMARRAALARAIAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 161 DPDILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDTLDKVAATDDGWIQ 240
Cdd:PRK11831 161 EPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPRVR 240
|
....*
gi 553371603 241 AYFHG 245
Cdd:PRK11831 241 QFLDG 245
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
7-218 |
4.27e-49 |
|
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: 161.58 E-value: 4.27e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 7 IQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLR-----RPTDGKIHVFGKDLMALsGQSRAMV 81
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDL-DVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 82 ERRFGVLFQRGALFSsLTVTENVALPLIENAGLPRSEAERLAQVKLALAGLPPGTGSKYPA-SLSGGMVKRVALARALAL 160
Cdd:cd03260 80 RRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRLHAlGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 553371603 161 DPDILFLDEPTAGLDPIGAAAFDSLIRTLRDalNLTVFLVTHDLDTLYTLCDRVAVLS 218
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKK--EYTIVIVTHNMQQAARVADRTAFLL 214
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
26-217 |
1.76e-48 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 164.51 E-value: 1.76e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 26 NLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQS-RAMVERRFGVLFQRGALFSSLTVTENV 104
Cdd:COG4175 47 SFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKElRELRRKKMSMVFQHFALLPHRTVLENV 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 105 ALPLiENAGLPRSEAERLAQVKLALAGLPpGTGSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPigaaafds 184
Cdd:COG4175 127 AFGL-EIQGVPKAERRERAREALELVGLA-GWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDP-------- 196
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 553371603 185 LIRT--------LRDALNLTVFLVTHDLDTLYTLCDRVAVL 217
Cdd:COG4175 197 LIRRemqdelleLQAKLKKTIVFITHDLDEALRLGDRIAIM 237
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
4-245 |
2.21e-48 |
|
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: 160.59 E-value: 2.21e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 4 DAIIQIRDLVNCFG-VQCVhQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAmve 82
Cdd:COG0411 2 DPLLEVRGLTKRFGgLVAV-DDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIA--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 83 rRFGVL--FQRGALFSSLTVTENVALPLIENAG---------LPRSEAER----------LAQVKLA-LAGLPPGtgsky 140
Cdd:COG0411 78 -RLGIArtFQNPRLFPELTVLENVLVAAHARLGrgllaallrLPRARREEreareraeelLERVGLAdRADEPAG----- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 141 paSLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQK 220
Cdd:COG0411 152 --NLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFG 229
|
250 260
....*....|....*....|....*
gi 553371603 221 KVLVVDTLDKVAAtDDGWIQAYFHG 245
Cdd:COG0411 230 RVIAEGTPAEVRA-DPRVIEAYLGE 253
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
23-231 |
7.62e-48 |
|
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: 159.00 E-value: 7.62e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 23 QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGqsramVE--RRFGVLFQRGALFSSLTV 100
Cdd:cd03295 18 NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDP-----VElrRKIGYVIQQIGLFPHMTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 101 TENVAL-PLIEnaGLPRSEAERLAQVKLALAGLPPGT-GSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIG 178
Cdd:cd03295 93 EENIALvPKLL--KWPKEKIRERADELLALVGLDPAEfADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPIT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 553371603 179 AAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDTLDKV 231
Cdd:cd03295 171 RDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
7-233 |
4.11e-47 |
|
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: 156.94 E-value: 4.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 7 IQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDlmalSGQSRAMVERRFG 86
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGED----VRKEPREARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 87 VLFQRGALFSSLTVTENVALpLIENAGLPRSEAERLAQVKLALAGLPPGTGSKYpASLSGGMVKRVALARALALDPDILF 166
Cdd:COG4555 78 VLPDERGLYDRLTVRENIRY-FAELYGLFDEELKKRIEELIELLGLEEFLDRRV-GELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 553371603 167 LDEPTAGLDPIGAAAFDSLIRTLRDaLNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDTLDKVAA 233
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRALKK-EGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELRE 221
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
7-231 |
1.53e-46 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 155.34 E-value: 1.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 7 IQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQsramvERRFG 86
Cdd:TIGR00968 1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHAR-----DRKIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 87 VLFQRGALFSSLTVTENVALPLI---ENAGLPRSEAERLAQVkLALAGLppgtGSKYPASLSGGMVKRVALARALALDPD 163
Cdd:TIGR00968 76 FVFQHYALFKHLTVRDNIAFGLEirkHPKAKIKARVEELLEL-VQLEGL----GDRYPNQLSGGQRQRVALARALAVEPQ 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 553371603 164 ILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDTLDKV 231
Cdd:TIGR00968 151 VLLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEV 218
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
7-231 |
5.12e-46 |
|
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: 154.03 E-value: 5.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 7 IQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQsramvERRFG 86
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ-----ERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 87 VLFQRGALFSSLTVTENVALPLIENAGLPR-SEAERLAQVK--LALAGLPpGTGSKYPASLSGGMVKRVALARALALDPD 163
Cdd:cd03296 78 FVFQHYALFRHMTVFDNVAFGLRVKPRSERpPEAEIRAKVHelLKLVQLD-WLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 553371603 164 ILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDTLDKV 231
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-222 |
1.21e-45 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 153.32 E-value: 1.21e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 1 MTQDAIIQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLmalsgqsrAM 80
Cdd:COG1121 1 MMMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP--------RR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 81 VERRFGVLFQRGALFSS--LTVTENVALPLIENAGLPR--SEAER------LAQVKLA-LAGLPPGTgskypasLSGGMV 149
Cdd:COG1121 73 ARRRIGYVPQRAEVDWDfpITVRDVVLMGRYGRRGLFRrpSRADReavdeaLERVGLEdLADRPIGE-------LSGGQQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 553371603 150 KRVALARALALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDAlNLTVFLVTHDLDTLYTLCDRVAVLSQKKV 222
Cdd:COG1121 146 QRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
23-222 |
1.24e-45 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 152.51 E-value: 1.24e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 23 QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAMVERRFGVLFQRGALFSSLTVTE 102
Cdd:COG2884 19 SDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRRIGVVFQDFRLLPDRTVYE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 103 NVALPLiENAGLPRSEAER-----LAQVKLAlaglppGTGSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPI 177
Cdd:COG2884 99 NVALPL-RVTGKSRKEIRRrvrevLDLVGLS------DKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 553371603 178 GAaafDSLIRTLRD--ALNLTVFLVTHDLDTLYTLCDRVAVLSQKKV 222
Cdd:COG2884 172 TS---WEIMELLEEinRRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
7-227 |
1.90e-45 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 152.14 E-value: 1.90e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 7 IQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQsramVERRFG 86
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE----VRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 87 VLFQRGALFSSLTVTENVALpLIENAGLPRSEA-ERLAQVkLALAGLPPgTGSKYPASLSGGMVKRVALARALALDPDIL 165
Cdd:cd03265 77 IVFQDLSVDDELTGWENLYI-HARLYGVPGAERrERIDEL-LDFVGLLE-AADRLVKTYSGGMRRRLEIARSLVHRPEVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 553371603 166 FLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDT 227
Cdd:cd03265 154 FLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGT 215
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
23-218 |
3.33e-45 |
|
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: 151.82 E-value: 3.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 23 QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAMVERR-FGVLFQRGALFSSLTVT 101
Cdd:COG4181 29 KGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARLRARhVGFVFQSFQLLPTLTAL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 102 ENVALPLiENAGlpRSEAERLAQVKLALAGLppgtGSK---YPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIG 178
Cdd:COG4181 109 ENVMLPL-ELAG--RRDARARARALLERVGL----GHRldhYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAAT 181
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 553371603 179 AAAFDSLIRTLRDALNLTVFLVTHDLdTLYTLCDRVAVLS 218
Cdd:COG4181 182 GEQIIDLLFELNRERGTTLVLVTHDP-ALAARCDRVLRLR 220
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
7-227 |
9.59e-45 |
|
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: 150.46 E-value: 9.59e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 7 IQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQsramvERRFG 86
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH-----KRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 87 VLFQRGALFSSLTVTENVALPLiENAGLPRSE-----AERLAQVKLAlaglppGTGSKYPASLSGGMVKRVALARALALD 161
Cdd:cd03300 76 TVFQNYALFPHLTVFENIAFGL-RLKKLPKAEikervAEALDLVQLE------GYANRKPSQLSGGQQQRVAIARALVNE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 553371603 162 PDILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDT 227
Cdd:cd03300 149 PKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
5-227 |
3.22e-43 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 149.84 E-value: 3.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 5 AIIQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSR--AMVe 82
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRniAMV- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 83 rrfgvlFQRGALFSSLTVTENVALPLiENAGLPRSE-AERLAQV--KLALAGLppgtGSKYPASLSGGMVKRVALARALA 159
Cdd:COG3839 81 ------FQSYALYPHMTVYENIAFPL-KLRKVPKAEiDRRVREAaeLLGLEDL----LDRKPKQLSGGQRQRVALGRALV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 553371603 160 LDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDT 227
Cdd:COG3839 150 REPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGT 217
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
7-222 |
3.63e-43 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 145.73 E-value: 3.63e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 7 IQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQS-RamveRRF 85
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwR----RQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 86 GVLFQRGALFSSlTVTENVALPL-IENAGLPRSEAERLaqvkLALAGLPPGTGSKYPASLSGGMVKRVALARALALDPDI 164
Cdd:COG4619 77 AYVPQEPALWGG-TVRDNLPFPFqLRERKFDRERALEL----LERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 553371603 165 LFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKV 222
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
6-223 |
4.47e-43 |
|
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: 146.73 E-value: 4.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 6 IIQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAmveRRF 85
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELA---RRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 86 GVLFQRGALFSSLTVTENVAL---PLIENAGLPRSEAERLAQVKLALAGLppgTG--SKYPASLSGGMVKRVALARALAL 160
Cdd:COG1120 78 AYVPQEPPAPFGLTVRELVALgryPHLGLFGRPSAEDREAVEEALERTGL---EHlaDRPVDELSGGERQRVLIARALAQ 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 553371603 161 DPDILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKVL 223
Cdd:COG1120 155 EPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIV 217
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
24-227 |
5.11e-43 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 148.31 E-value: 5.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 24 GLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMalsgQSRAMVERRFGVLFQRGALFSSLTVTEN 103
Cdd:TIGR01188 11 GVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVV----REPRKVRRSIGIVPQYASVDEDLTGREN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 104 VALpLIENAGLPRSEAERLAQVKLALAGLPPgTGSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAAAFD 183
Cdd:TIGR01188 87 LEM-MGRLYGLPKDEAEERAEELLELFELGE-AADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIW 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 553371603 184 SLIRTLRDAlNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDT 227
Cdd:TIGR01188 165 DYIRALKEE-GVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGT 207
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-216 |
3.51e-42 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 146.80 E-value: 3.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 1 MTQDAIIQIRDLVNCFGV---------QCVH--QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKD 69
Cdd:COG4608 2 AMAEPLLEVRDLKKHFPVrgglfgrtvGVVKavDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 70 LMALSGQSRAMVERRFGVLFQ--RGALFSSLTVTENVALPLIENAGLPRSEAERLAQVKLALAGLPPGTGSKYPASLSGG 147
Cdd:COG4608 82 ITGLSGRELRPLRRRMQMVFQdpYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRPEHADRYPHEFSGG 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 553371603 148 MVKRVALARALALDPDILFLDEPTAGLDPigaaafdS-------LIRTLRDALNLTVFLVTHDLDTLYTLCDRVAV 216
Cdd:COG4608 162 QRQRIGIARALALNPKLIVCDEPVSALDV-------SiqaqvlnLLEDLQDELGLTYLFISHDLSVVRHISDRVAV 230
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
8-222 |
1.04e-41 |
|
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: 141.90 E-value: 1.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 8 QIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLmalsgqsrAMVERRFGV 87
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL--------EKERKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 88 LFQRGALFSS--LTVTENVALPLIENAGL---PRSEAERLAQVKLALAGLppgtgSKYP----ASLSGGMVKRVALARAL 158
Cdd:cd03235 73 VPQRRSIDRDfpISVRDVVLMGLYGHKGLfrrLSKADKAKVDEALERVGL-----SELAdrqiGELSGGQQQRVLLARAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 553371603 159 ALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDaLNLTVFLVTHDLDTLYTLCDRVAVLSQKKV 222
Cdd:cd03235 148 VQDPDLLLLDEPFAGVDPKTQEDIYELLRELRR-EGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
24-231 |
1.27e-41 |
|
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: 142.47 E-value: 1.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 24 GLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQsramvERRFGVLFQRGALFSSLTVTEN 103
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE-----KRDISYVPQNYALFPHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 104 VALPLIeNAGLPRSEAERlaQVK-----LALAGLPpgtgSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIG 178
Cdd:cd03299 92 IAYGLK-KRKVDKKEIER--KVLeiaemLGIDHLL----NRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 553371603 179 AAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDTLDKV 231
Cdd:cd03299 165 KEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEV 217
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
7-231 |
1.61e-41 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 145.61 E-value: 1.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 7 IQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQsramvERRFG 86
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR-----DRKVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 87 VLFQRGALFSSLTVTENVALPLienAGLPRSE-----------AERLAQVKLA-LAGlppgtgsKYPASLSGGMVKRVAL 154
Cdd:PRK10851 78 FVFQHYALFRHMTVFDNIAFGL---TVLPRRErpnaaaikakvTQLLEMVQLAhLAD-------RYPAQLSGGQKQRVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 553371603 155 ARALALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDTLDKV 231
Cdd:PRK10851 148 ARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
23-223 |
1.82e-41 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 142.95 E-value: 1.82e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 23 QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLmaLSGQSRAMVERRFGVLFQR------GAlfs 96
Cdd:TIGR04520 19 KNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDT--LDEENLWEIRKKVGMVFQNpdnqfvGA--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 97 slTVTENVALPLiENAGLPRSEAERLAQVKLALAGLppgtgSKY----PASLSGGMVKRVALARALALDPDILFLDEPTA 172
Cdd:TIGR04520 94 --TVEDDVAFGL-ENLGVPREEMRKRVDEALKLVGM-----EDFrdrePHLLSGGQKQRVAIAGVLAMRPDIIILDEATS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 553371603 173 GLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLyTLCDRVAVLSQKKVL 223
Cdd:TIGR04520 166 MLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIV 215
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
5-222 |
4.33e-41 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 141.35 E-value: 4.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 5 AIIQIRDLVNCF-GVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAMVER 83
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 84 RFGVLFQRGALFSSLTVTENVALPLIENAGLPRS------EAER------LAQVKLA-LAGLPPGTgskypasLSGGMVK 150
Cdd:COG3638 81 RIGMIFQQFNLVPRLSVLTNVLAGRLGRTSTWRSllglfpPEDReraleaLERVGLAdKAYQRADQ-------LSGGQQQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 553371603 151 RVALARALALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKV 222
Cdd:COG3638 154 RVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRV 225
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
23-233 |
5.71e-41 |
|
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: 141.04 E-value: 5.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 23 QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAmverRFGVL--FQRGALFSSLTV 100
Cdd:cd03219 17 DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIA----RLGIGrtFQIPRLFPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 101 TENVALPL-------IENAGLPRSEAERLAQVK--LALAGLPpGTGSKYPASLSGGMVKRVALARALALDPDILFLDEPT 171
Cdd:cd03219 93 LENVMVAAqartgsgLLLARARREEREARERAEelLERVGLA-DLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 553371603 172 AGLDPIGAAAFDSLIRTLRDAlNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDTLDKVAA 233
Cdd:cd03219 172 AGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
7-222 |
1.22e-40 |
|
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: 139.31 E-value: 1.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 7 IQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSR--AMVerr 84
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRdiAMV--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 85 fgvlFQRGALFSSLTVTENVALPLiENAGLPRSE-AERLAQV--KLALAGLPpgtgSKYPASLSGGMVKRVALARALALD 161
Cdd:cd03301 78 ----FQNYALYPHMTVYDNIAFGL-KLRKVPKDEiDERVREVaeLLQIEHLL----DRKPKQLSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 553371603 162 PDILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKV 222
Cdd:cd03301 149 PKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
7-223 |
2.47e-40 |
|
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: 138.50 E-value: 2.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 7 IQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGqsramVERRFG 86
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIE-----ALRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 87 VLFQRGALFSSLTVTENVALPLIEnAGLPRSEAERLaqvkLALAGLPpGTGSKYPASLSGGMVKRVALARALALDPDILF 166
Cdd:cd03268 76 ALIEAPGFYPNLTARENLRLLARL-LGIRKKRIDEV----LDVVGLK-DSAKKKVKGFSLGMKQRLGIALALLGNPDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 553371603 167 LDEPTAGLDPIGAAAFDSLIRTLRDAlNLTVFLVTHDLDTLYTLCDRVAVLSQKKVL 223
Cdd:cd03268 150 LDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
26-231 |
3.84e-40 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 142.30 E-value: 3.84e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 26 NLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALS-GQSRAMVERRFGVLFQRGALFSSLTVTENV 104
Cdd:TIGR01186 13 DLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSpVELREVRRKKIGMVFQQFALFPHMTILQNT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 105 ALPLiENAGLPRSEAERLAQVKLALAGLPpGTGSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAAAFDS 184
Cdd:TIGR01186 93 SLGP-ELLGWPEQERKEKALELLKLVGLE-EYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLIRDSMQD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 553371603 185 LIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDTLDKV 231
Cdd:TIGR01186 171 ELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEI 217
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
23-223 |
6.57e-40 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 139.38 E-value: 6.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 23 QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGkdlMALSGQSRAMVERRFGVLFQR-GALFSSLTVT 101
Cdd:PRK13635 24 KDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG---MVLSEETVWDVRRQVGMVFQNpDNQFVGATVQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 102 ENVALPLiENAGLPRSEAERLAQVKLALAGLPPgTGSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAAA 181
Cdd:PRK13635 101 DDVAFGL-ENIGVPREEMVERVDQALRQVGMED-FLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRRE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 553371603 182 FDSLIRTLRDALNLTVFLVTHDLDTLYTlCDRVAVLSQKKVL 223
Cdd:PRK13635 179 VLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEIL 219
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
8-223 |
1.06e-39 |
|
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: 135.64 E-value: 1.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 8 QIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAmveRRFGV 87
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELA---RKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 88 LFQrgalfssltvtenvalpLIENAGLprseaERLAQvklalaglppgtgsKYPASLSGGMVKRVALARALALDPDILFL 167
Cdd:cd03214 78 VPQ-----------------ALELLGL-----AHLAD--------------RPFNELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 553371603 168 DEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKVL 223
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
15-217 |
2.66e-39 |
|
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: 135.89 E-value: 2.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 15 CFGVQCVHQGLNLDVK---RGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDL------MALSGQsramvERRF 85
Cdd:cd03297 3 CVDIEKRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrkkINLPPQ-----QRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 86 GVLFQRGALFSSLTVTENVALplienaGLPR-SEAERLAQVK--LALAGLPPgTGSKYPASLSGGMVKRVALARALALDP 162
Cdd:cd03297 78 GLVFQQYALFPHLNVRENLAF------GLKRkRNREDRISVDelLDLLGLDH-LLNRYPAQLSGGEKQRVALARALAAQP 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 553371603 163 DILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVL 217
Cdd:cd03297 151 ELLLLDEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVM 205
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
26-236 |
1.00e-38 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 134.88 E-value: 1.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 26 NLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALsgqsrAMVERRFGVLFQRGALFSSLTVTENVA 105
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTAL-----PPAERPVSMLFQENNLFPHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 106 LPLieNAGLPRSEAER------LAQVKLAlaglppGTGSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGA 179
Cdd:COG3840 94 LGL--RPGLKLTAEQRaqveqaLERVGLA------GLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 553371603 180 AAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDTLDKVAATDD 236
Cdd:COG3840 166 QEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEP 222
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
23-222 |
1.24e-38 |
|
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: 141.36 E-value: 1.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 23 QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRrPTDGKIHVFGKDLMALSGQSRAMVERRFGVLFQRGalFSSL---- 98
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRALRPLRRRMQVVFQDP--FGSLsprm 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 99 TVTENVALPLIENaGLPRSEAERLAQVKLALA--GLPPGTGSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDP 176
Cdd:COG4172 380 TVGQIIAEGLRVH-GPGLSAAERRARVAEALEevGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDV 458
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 553371603 177 IGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKV 222
Cdd:COG4172 459 SVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKV 504
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
19-217 |
1.66e-38 |
|
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: 135.32 E-value: 1.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 19 QCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAMVERRFGVLFQR--GALFS 96
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAFRRDVQLVFQDspSAVNP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 97 SLTVTENVALPLIENAGLPRSEAERLAQVKLALAGLPPGTGSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDP 176
Cdd:TIGR02769 104 RMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDM 183
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 553371603 177 IGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVL 217
Cdd:TIGR02769 184 VLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVM 224
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
23-229 |
2.24e-38 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 134.99 E-value: 2.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 23 QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKdlmALSGQSramVERrfGVLFQRGALFSSLTVTE 102
Cdd:COG4525 24 QDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGV---PVTGPG---ADR--GVVFQKDALLPWLNVLD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 103 NVALPLiENAGLPRSEAERLAQVKLALAGLPpGTGSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAAAF 182
Cdd:COG4525 96 NVAFGL-RLRGVPKAERRARAEELLALVGLA-DFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQM 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 553371603 183 DSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDTLD 229
Cdd:COG4525 174 QELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPGPGRIVERLE 220
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
7-230 |
2.65e-38 |
|
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: 133.40 E-value: 2.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 7 IQIRDLVNCFGVQCVH--QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMalsgQSRAMVERR 84
Cdd:cd03263 1 LQIRNLTKTYKKGTKPavDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR----TDRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 85 FGVLFQRGALFSSLTVTENVAL--PLienAGLPRSEAERLAQVKLALAGLPPgTGSKYPASLSGGMVKRVALARALALDP 162
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLRFyaRL---KGLPKSEIKEEVELLLRVLGLTD-KANKRARTLSGGMKRKLSLAIALIGGP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 553371603 163 DILFLDEPTAGLDPIGAAAFDSLIRTLRDalNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDTLDK 230
Cdd:cd03263 153 SVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
16-221 |
3.24e-38 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 131.21 E-value: 3.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 16 FGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSramVERRFGVLFQrgalf 95
Cdd:cd00267 9 YGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEE---LRRRIGYVPQ----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 96 ssltvtenvalplienaglprseaerlaqvklalaglppgtgskypasLSGGMVKRVALARALALDPDILFLDEPTAGLD 175
Cdd:cd00267 81 ------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLD 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 553371603 176 PIGAAAFDSLIRTLRDAlNLTVFLVTHDLDTLYTLCDRVAVLSQKK 221
Cdd:cd00267 113 PASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
23-172 |
4.31e-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: 130.85 E-value: 4.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 23 QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDlmaLSGQSRAMVERRFGVLFQRGALFSSLTVTE 102
Cdd:pfam00005 2 KNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQD---LTDDERKSLRKEIGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 553371603 103 NVALPLIEnAGLPRSEAERLAQVKLALAGLPPGTGSK---YPASLSGGMVKRVALARALALDPDILFLDEPTA 172
Cdd:pfam00005 79 NLRLGLLL-KGLSKREKDARAEEALEKLGLGDLADRPvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
23-235 |
5.05e-38 |
|
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: 141.12 E-value: 5.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 23 QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSgqsRAMVERRFGVLFQRGALFSSlTVTE 102
Cdd:COG2274 492 DNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID---PASLRRQIGVVLQDVFLFSG-TIRE 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 103 NVALpliENAGLPRSEAERLAQvklaLAGL-------------PPGTGSkypASLSGGMVKRVALARALALDPDILFLDE 169
Cdd:COG2274 568 NITL---GDPDATDEEIIEAAR----LAGLhdfiealpmgydtVVGEGG---SNLSGGQRQRLAIARALLRNPRILILDE 637
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 553371603 170 PTAGLDPIGAAAFDSLIRTLRDalNLTVFLVTHDLDTLyTLCDRVAVLSQKKVLVVDTLDKVAATD 235
Cdd:COG2274 638 ATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTI-RLADRIIVLDKGRIVEDGTHEELLARK 700
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
5-223 |
7.32e-38 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 133.34 E-value: 7.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 5 AIIQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHV------FGKDLMALSGQSR 78
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidTARSLSQQKGLIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 79 AMvERRFGVLFQRGALFSSLTVTENVALPLIENAGLPRSEAERLAQVKLALAGLpPGTGSKYPASLSGGMVKRVALARAL 158
Cdd:PRK11264 82 QL-RQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGL-AGKETSYPRRLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 553371603 159 ALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDAlNLTVFLVTHDLDTLYTLCDRVAVLSQKKVL 223
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
21-204 |
1.05e-37 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 132.09 E-value: 1.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 21 VHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAMVE-RRFGVLFQRGALFSSLT 99
Cdd:TIGR02211 20 VLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKLRnKKLGFIYQFHHLLPDFT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 100 VTENVALPLIEnAGLPRSEAERLAQVKLALAGLPPGTgSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGA 179
Cdd:TIGR02211 100 ALENVAMPLLI-GKKSVKEAKERAYEMLEKVGLEHRI-NHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNNA 177
|
170 180
....*....|....*....|....*
gi 553371603 180 AAFDSLIRTLRDALNLTVFLVTHDL 204
Cdd:TIGR02211 178 KIIFDLMLELNRELNTSFLVVTHDL 202
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
23-221 |
1.12e-37 |
|
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: 130.20 E-value: 1.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 23 QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAmveRRFGVLFQRGALFSSlTVTE 102
Cdd:cd03228 19 KDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLR---KNIAYVPQDPFLFSG-TIRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 103 NValplienaglprseaerlaqvklalaglppgtgskypasLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAAAF 182
Cdd:cd03228 95 NI---------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALI 135
|
170 180 190
....*....|....*....|....*....|....*....
gi 553371603 183 DSLIRTLRDalNLTVFLVTHDLDTLyTLCDRVAVLSQKK 221
Cdd:cd03228 136 LEALRALAK--GKTVIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-223 |
1.23e-37 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 135.23 E-value: 1.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 1 MTQDAIIQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSR-- 78
Cdd:PRK11432 1 MTQKNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRdi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 79 AMVerrfgvlFQRGALFSSLTVTENVALPLienAGLPRSEAERLAQVK--LALAGLpPGTGSKYPASLSGGMVKRVALAR 156
Cdd:PRK11432 81 CMV-------FQSYALFPHMSLGENVGYGL---KMLGVPKEERKQRVKeaLELVDL-AGFEDRYVDQISGGQQQRVALAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 553371603 157 ALALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKVL 223
Cdd:PRK11432 150 ALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIM 216
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
23-218 |
1.23e-37 |
|
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: 132.20 E-value: 1.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 23 QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMAlSGQSRAmverrfgVLFQRGALFSSLTVTE 102
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE-PGPDRM-------VVFQNYSLLPWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 103 NVALPLIE-NAGLPRSEAERLAQVKLALAGLPPGtGSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAAA 181
Cdd:TIGR01184 74 NIALAVDRvLPDLSKSERRAIVEEHIALVGLTEA-ADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 553371603 182 F-DSLIRTLRDAlNLTVFLVTHDLDTLYTLCDRVAVLS 218
Cdd:TIGR01184 153 LqEELMQIWEEH-RVTVLMVTHDVDEALLLSDRVVMLT 189
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
24-222 |
2.10e-37 |
|
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: 130.99 E-value: 2.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 24 GLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAMVERRFGVLFQRGALFSSLTVTEN 103
Cdd:cd03292 19 GINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKIGVVFQDFRLLPDRNVYEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 104 VALPLiENAGLPRSEAERLAQVKLALAGLpPGTGSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAAAFD 183
Cdd:cd03292 99 VAFAL-EVTGVPPREIRKRVPAALELVGL-SHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIM 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 553371603 184 SLIRTLRDAlNLTVFLVTHDLDTLYTLCDRVAVLSQKKV 222
Cdd:cd03292 177 NLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
7-223 |
8.34e-37 |
|
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: 129.97 E-value: 8.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 7 IQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAmverRFG 86
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRA----RLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 87 V--LFQRGALFSSLTVTENVALPLiENAGLPRSEAERLAQVKLALAGLPPGTGSKyPASLSGGMVKRVALARALALDPDI 164
Cdd:cd03218 77 IgyLPQEASIFRKLTVEENILAVL-EIRGLSKKEREEKLEELLEEFHITHLRKSK-ASSLSGGERRRVEIARALATNPKF 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 553371603 165 LFLDEPTAGLDPIGAAAFDSLIRTLRDaLNLTVFLVTHDLDTLYTLCDRVAVLSQKKVL 223
Cdd:cd03218 155 LLLDEPFAGVDPIAVQDIQKIIKILKD-RGIGVLITDHNVRETLSITDRAYIIYEGKVL 212
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-233 |
1.01e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 131.12 E-value: 1.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 3 QDAIIQIRDLvnCF----GVQCVhQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIhVFGKDLMALSGQSR 78
Cdd:PRK13636 2 EDYILKVEEL--NYnysdGTHAL-KGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRI-LFDGKPIDYSRKGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 79 AMVERRFGVLFQR--GALFSSlTVTENVALPLIeNAGLPRSEAERLAQVKLALAGLPPgTGSKYPASLSGGMVKRVALAR 156
Cdd:PRK13636 78 MKLRESVGMVFQDpdNQLFSA-SVYQDVSFGAV-NLKLPEDEVRKRVDNALKRTGIEH-LKDKPTHCLSFGQKKRVAIAG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 553371603 157 ALALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDTLDKVAA 233
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFA 231
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-222 |
1.28e-36 |
|
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: 127.93 E-value: 1.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 4 DAIIQIRDLvncfGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRamveR 83
Cdd:cd03215 2 EPVLEVRGL----SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDA----I 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 84 RFGVLF-----QRGALFSSLTVTENVALPLIenaglprseaerlaqvklalaglppgtgskypasLSGGMVKRVALARAL 158
Cdd:cd03215 74 RAGIAYvpedrKREGLVLDLSVAENIALSSL----------------------------------LSGGNQQKVVLARWL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 553371603 159 ALDPDILFLDEPTAGLDpIGAAAF-DSLIRTLRDAlNLTVFLVTHDLDTLYTLCDRVAVLSQKKV 222
Cdd:cd03215 120 ARDPRVLILDEPTRGVD-VGAKAEiYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
23-222 |
2.94e-36 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 128.84 E-value: 2.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 23 QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAMVERRFGVLFQRGALFSSLTVTE 102
Cdd:cd03256 18 KDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQIGMIFQQFNLIERLSVLE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 103 NV------ALPLIENAGLPRSEAER------LAQVKLAlaglppGTGSKYPASLSGGMVKRVALARALALDPDILFLDEP 170
Cdd:cd03256 98 NVlsgrlgRRSTWRSLFGLFPKEEKqralaaLERVGLL------DKAYQRADQLSGGQQQRVAIARALMQQPKLILADEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 553371603 171 TAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKV 222
Cdd:cd03256 172 VASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRI 223
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-176 |
3.53e-36 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 129.15 E-value: 3.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 1 MTQDAI--IQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLM------- 71
Cdd:COG4598 1 MTDTAPpaLEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpdrdg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 72 ALSGQSRAMVER---RFGVLFQRGALFSSLTVTENVALPLIENAGLPRSEAERLAQVKLALAGLPpGTGSKYPASLSGGM 148
Cdd:COG4598 81 ELVPADRRQLQRirtRLGMVFQSFNLWSHMTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGLA-DKRDAYPAHLSGGQ 159
|
170 180
....*....|....*....|....*...
gi 553371603 149 VKRVALARALALDPDILFLDEPTAGLDP 176
Cdd:COG4598 160 QQRAAIARALAMEPEVMLFDEPTSALDP 187
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
6-204 |
3.70e-36 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 128.67 E-value: 3.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 6 IIQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRaMVERRF 85
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDER-LIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 86 GVLFQRGALFSSLTVTENVALPLIENAGLPRSEAERLAQVKLALAGLPPGTGsKYPASLSGGMVKRVALARALALDPDIL 165
Cdd:PRK09493 80 GMVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAH-HYPSELSGGQQQRVAIARALAVKPKLM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 553371603 166 FLDEPTAGLDPigaAAFDSLIRTLRDALN--LTVFLVTHDL 204
Cdd:PRK09493 159 LFDEPTSALDP---ELRHEVLKVMQDLAEegMTMVIVTHEI 196
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
6-240 |
3.85e-36 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 128.57 E-value: 3.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 6 IIQIRDLVNCFGVQcvHQGL---NLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAMVE 82
Cdd:TIGR02315 1 MLEVENLSKVYPNG--KQALkniNLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 83 RRFGVLFQRGALFSSLTVTENVALPLIENAG--------LPRSEAER----LAQVKLAlaglppGTGSKYPASLSGGMVK 150
Cdd:TIGR02315 79 RRIGMIFQHYNLIERLTVLENVLHGRLGYKPtwrsllgrFSEEDKERalsaLERVGLA------DKAYQRADQLSGGQQQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 151 RVALARALALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKVlVVDtlDK 230
Cdd:TIGR02315 153 RVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEI-VFD--GA 229
|
250
....*....|
gi 553371603 231 VAATDDGWIQ 240
Cdd:TIGR02315 230 PSELDDEVLR 239
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
6-223 |
4.38e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 129.43 E-value: 4.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 6 IIQIRDLVNCF--GVQCVhQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLmALSGQSRAMVER 83
Cdd:PRK13639 1 ILETRDLKYSYpdGTEAL-KGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 84 RFGVLFQR--GALFSSlTVTENVAL-PLieNAGLPRSEAERLAQVKLALAGLPpGTGSKYPASLSGGMVKRVALARALAL 160
Cdd:PRK13639 79 TVGIVFQNpdDQLFAP-TVEEDVAFgPL--NLGLSKEEVEKRVKEALKAVGME-GFENKPPHHLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 553371603 161 DPDILFLDEPTAGLDPIGAAAFDSLIRTLRDAlNLTVFLVTHDLDTLYTLCDRVAVLSQKKVL 223
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKII 216
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
23-207 |
4.89e-36 |
|
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: 127.21 E-value: 4.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 23 QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLmalsGQSRAMVERRFGVLFQRGALFSSLTVTE 102
Cdd:COG4133 19 SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI----RDAREDYRRRLAYLGHADGLKPELTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 103 NVALpLIENAGLPRSEA---ERLAQVKLA-LAGLPPGTgskypasLSGGMVKRVALARALALDPDILFLDEPTAGLDPIG 178
Cdd:COG4133 95 NLRF-WAALYGLRADREaidEALEAVGLAgLADLPVRQ-------LSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAG 166
|
170 180
....*....|....*....|....*....
gi 553371603 179 AAAFDSLIRTLRDAlNLTVFLVTHDLDTL 207
Cdd:COG4133 167 VALLAELIAAHLAR-GGAVLLTTHQPLEL 194
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
7-222 |
8.29e-36 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 128.16 E-value: 8.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 7 IQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMAL---SGQSRA---- 79
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkDGQLKVadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 80 ---MVERRFGVLFQRGALFSSLTVTENVALPLIENAGLPRSEAERLAQVKLALAGLPPGTGSKYPASLSGGMVKRVALAR 156
Cdd:PRK10619 86 qlrLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 553371603 157 ALALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDAlNLTVFLVTHDLDTLYTLCDRVAVLSQKKV 222
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-204 |
1.05e-35 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 127.85 E-value: 1.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 2 TQDAIIQIRDLvNCF-GVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRS-------IVGLRrpTDGKIHVFGKDLMAl 73
Cdd:COG1117 7 TLEPKIEVRNL-NVYyGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRClnrmndlIPGAR--VEGEILLDGEDIYD- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 74 SGQSRAMVERRFGVLFQRGALFSsLTVTENVALPLIENAGLPRSEAERLAQVKLALAGLP---------PGTGskypasL 144
Cdd:COG1117 83 PDVDVVELRRRVGMVFQKPNPFP-KSIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALWdevkdrlkkSALG------L 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 145 SGGMVKRVALARALALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDalNLTVFLVTHDL 204
Cdd:COG1117 156 SGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKK--DYTIVIVTHNM 213
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
25-231 |
3.15e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 127.47 E-value: 3.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 25 LNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLmALSGQSRAMVERRFGVLFQ--RGALFSSlTVTE 102
Cdd:PRK13637 26 VNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDI-TDKKVKLSDIRKKVGLVFQypEYQLFEE-TIEK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 103 NVALPLIeNAGLPRSEAERLAQVKLALAGLP-PGTGSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAAA 181
Cdd:PRK13637 104 DIAFGPI-NLGLSEEEIENRVKRAMNIVGLDyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDE 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 553371603 182 FDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDTLDKV 231
Cdd:PRK13637 183 ILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
7-233 |
4.75e-35 |
|
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: 125.24 E-value: 4.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 7 IQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAmverRFG 86
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERA----RAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 87 VLF--QRGALFSSLTVTEN--VALPLIENAGLPRSEAE------RLAQVKLALAGlppgtgskypaSLSGGMVKRVALAR 156
Cdd:cd03224 77 IGYvpEGRRIFPELTVEENllLGAYARRRAKRKARLERvyelfpRLKERRKQLAG-----------TLSGGEQQMLAIAR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 553371603 157 ALALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDaLNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDTLDKVAA 233
Cdd:cd03224 146 ALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRD-EGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
26-223 |
5.88e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 126.67 E-value: 5.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 26 NLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVfG----------KDLMALsgqsRAMVerrfGVLFQ--RGA 93
Cdd:PRK13634 27 NVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GervitagkknKKLKPL----RKKV----GIVFQfpEHQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 94 LFSSlTVTENVAL-PLieNAGLPRSEAERLAQVKLALAGLPPGTGSKYPASLSGGMVKRVALARALALDPDILFLDEPTA 172
Cdd:PRK13634 98 LFEE-TVEKDICFgPM--NFGVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 553371603 173 GLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKVL 223
Cdd:PRK13634 175 GLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVF 225
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
37-227 |
6.76e-35 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 127.61 E-value: 6.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 37 VVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMalsgqSRAMVERRFGVLFQRGALFSSLTVTENVALPLiENAGLPR 116
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVT-----NVPPHLRHINMVFQSYALFPHMTVEENVAFGL-KMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 117 seAERLAQVKLALAGLPPGT-GSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDALNL 195
Cdd:TIGR01187 75 --AEIKPRVLEALRLVQLEEfADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGI 152
|
170 180 190
....*....|....*....|....*....|..
gi 553371603 196 TVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDT 227
Cdd:TIGR01187 153 TFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGT 184
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
24-223 |
7.07e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 126.40 E-value: 7.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 24 GLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALS-GQSRAMVERRFGVLFQ--RGALFSSlTV 100
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSkNKDIKQIRKKVGLVFQfpESQLFEE-TV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 101 TENVAL-PliENAGLPRSEAERLAQVKLALAGLPPGTGSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGA 179
Cdd:PRK13649 104 LKDVAFgP--QNFGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 553371603 180 AAFDSLIRTLRDAlNLTVFLVTHDLDTLYTLCDRVAVLSQKKVL 223
Cdd:PRK13649 182 KELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-218 |
8.35e-35 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 130.53 E-value: 8.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 4 DAIIQIRDLV--NCFGVQCVHqGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRamv 81
Cdd:COG3845 255 EVVLEVENLSvrDDRGVPALK-DVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRER--- 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 82 eRRFGVLF-----QRGALFSSLTVTENVALPLIENAG------LPRSEAERLAQ-------VKlalaglPPGTGSKyPAS 143
Cdd:COG3845 331 -RRLGVAYipedrLGRGLVPDMSVAENLILGRYRRPPfsrggfLDRKAIRAFAEelieefdVR------TPGPDTP-ARS 402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 553371603 144 LSGGMVKRVALARALALDPDILFLDEPTAGLDpIGAAAF-DSLIRTLRDAlNLTVFLVTHDLDTLYTLCDRVAVLS 218
Cdd:COG3845 403 LSGGNQQKVILARELSRDPKLLIAAQPTRGLD-VGAIEFiHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMY 476
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
21-205 |
9.96e-35 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 123.30 E-value: 9.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 21 VHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLmALSGQSRAMVERRFGVLFQR--GALFSSl 98
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPL-DYSRKGLLERRQRVGLVFQDpdDQLFAA- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 99 TVTENVALPLIeNAGLPRSEAERLAQVKLALAGLPpGTGSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIG 178
Cdd:TIGR01166 85 DVDQDVAFGPL-NLGLSEAEVERRVREALTAVGAS-GLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAG 162
|
170 180
....*....|....*....|....*..
gi 553371603 179 AAAFDSLIRTLRDALNlTVFLVTHDLD 205
Cdd:TIGR01166 163 REQMLAILRRLRAEGM-TVVISTHDVD 188
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
23-222 |
1.58e-34 |
|
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: 123.14 E-value: 1.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 23 QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLmalsgqSRAMVERRFGVLFQ--RGALFssltv 100
Cdd:cd03226 17 DDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI------KAKERRKSIGYVMQdvDYQLF----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 101 TENVALPLIENAGLPRSEAERLAQV--KLALAGLPpgtgSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIG 178
Cdd:cd03226 86 TDSVREELLLGLKELDAGNEQAETVlkDLDLYALK----ERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKN 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 553371603 179 AAAFDSLIRTLRDALNlTVFLVTHDLDTLYTLCDRVAVLSQKKV 222
Cdd:cd03226 162 MERVGELIRELAAQGK-AVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-217 |
1.97e-34 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 127.37 E-value: 1.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 1 MTQDAIIQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQsram 80
Cdd:PRK09452 9 SSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 81 vERRFGVLFQRGALFSSLTVTENVALPLiENAGLPRSE-----AERLAQVKLAlaglppGTGSKYPASLSGGMVKRVALA 155
Cdd:PRK09452 85 -NRHVNTVFQSYALFPHMTVFENVAFGL-RMQKTPAAEitprvMEALRMVQLE------EFAQRKPHQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 553371603 156 RALALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVL 217
Cdd:PRK09452 157 RAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVM 218
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
5-233 |
7.20e-34 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 122.45 E-value: 7.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 5 AIIQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSgqsraMVER- 83
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLP-----MHKRa 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 84 RFGV--LFQRGALFSSLTVTENVALPLiENAGLPRSE-AERLAQV--KLALAGLppgtgSKYPA-SLSGGMVKRVALARA 157
Cdd:COG1137 77 RLGIgyLPQEASIFRKLTVEDNILAVL-ELRKLSKKErEERLEELleEFGITHL-----RKSKAySLSGGERRRVEIARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 553371603 158 LALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDAlNLTVfLVT-HDL-DTLyTLCDRVAVLSQKKVLVVDTLDKVAA 233
Cdd:COG1137 151 LATNPKFILLDEPFAGVDPIAVADIQKIIRHLKER-GIGV-LITdHNVrETL-GICDRAYIISEGKVLAEGTPEEILN 225
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-223 |
8.28e-34 |
|
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: 128.00 E-value: 8.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 4 DAIIQIRDLVNCF-----GVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHV-FGK---DLMALS 74
Cdd:TIGR03269 277 EPIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrVGDewvDMTKPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 75 GQSRAMVERRFGVLFQRGALFSSLTVTENvalpLIENAGL--PRSEAERLAQVKLALAGLPPGTG----SKYPASLSGGM 148
Cdd:TIGR03269 357 PDGRGRAKRYIGILHQEYDLYPHRTVLDN----LTEAIGLelPDELARMKAVITLKMVGFDEEKAeeilDKYPDELSEGE 432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 553371603 149 VKRVALARALALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKVL 223
Cdd:TIGR03269 433 RHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIV 507
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
29-222 |
1.50e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 122.92 E-value: 1.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 29 VKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKdlmALSGQSRAMVERRFGVLFQR-GALFSSLTVTENVALP 107
Cdd:PRK13650 30 VKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD---LLTEENVWDIRHKIGMVFQNpDNQFVGATVEDDVAFG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 108 LiENAGLPRSEAERLAQVKLALAGLPpGTGSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAAAFDSLIR 187
Cdd:PRK13650 107 L-ENKGIPHEEMKERVNEALELVGMQ-DFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIK 184
|
170 180 190
....*....|....*....|....*....|....*
gi 553371603 188 TLRDALNLTVFLVTHDLDTLyTLCDRVAVLSQKKV 222
Cdd:PRK13650 185 GIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQV 218
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
5-222 |
1.83e-33 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 121.80 E-value: 1.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 5 AIIQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAmveRR 84
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELA---RR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 85 FGVLFQRGALFSSLTVTENVALPLIENAGLPRsEAERLAQVKLALAGLPPGTGSKYPAsLSGGMVKRVALARALA----- 159
Cdd:PRK13548 78 RAVLPQHSSLSFPFTVEEVVAMGRAPHGLSRA-EDDALVAAALAQVDLAHLAGRDYPQ-LSGGEQQRVQLARVLAqlwep 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 553371603 160 -LDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLD--TLYtlCDRVAVLSQKKV 222
Cdd:PRK13548 156 dGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNlaARY--ADRIVLLHQGRL 219
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
7-225 |
1.93e-33 |
|
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: 120.46 E-value: 1.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 7 IQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALsgqsramVERRFG 86
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIA-------ARNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 87 VLFQRGALFSSLTVTEnVALPLIENAGLPRSEAERLAQVKLALAGLPPGTGSKYpASLSGGMVKRVALARALALDPDILF 166
Cdd:cd03269 74 YLPEERGLYPKMKVID-QLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRV-EELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 553371603 167 LDEPTAGLDPIGAAAFDSLIRTLRDAlNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVV 225
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
25-227 |
1.96e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 122.92 E-value: 1.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 25 LNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAM-VERRFGVLFQ--RGALFSSlTVT 101
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKpVRKKVGVVFQfpESQLFEE-TVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 102 ENVAL-PliENAGLPRSEAERLAQVKLALAGLPPGTGSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAA 180
Cdd:PRK13643 104 KDVAFgP--QNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARI 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 553371603 181 AFDSLIRTLRDAlNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDT 227
Cdd:PRK13643 182 EMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGT 227
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
8-205 |
2.09e-33 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 120.66 E-value: 2.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 8 QIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRP---TDGKIHVFGKDLMALsgqsrAMVERR 84
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTAL-----PAEQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 85 FGVLFQRGALFSSLTVTENV--ALPlienAGLPRSEAERLAQVKLALAGLPpGTGSKYPASLSGGMVKRVALARALALDP 162
Cdd:COG4136 78 IGILFQDDLLFPHLSVGENLafALP----PTIGRAQRRARVEQALEEAGLA-GFADRDPATLSGGQRARVALLRALLAEP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 553371603 163 DILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLD 205
Cdd:COG4136 153 RALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEE 195
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
26-225 |
3.10e-33 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 120.35 E-value: 3.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 26 NLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALsgqsrAMVERRFGVLFQRGALFSSLTVTENVA 105
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGL-----APYQRPVSMLFQENNLFAHLTVRQNIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 106 LPLIENAGLPRSEAERLAQV--KLALAGLPpgtgSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAAAFD 183
Cdd:TIGR01277 93 LGLHPGLKLNAEQQEKVVDAaqQVGIADYL----DRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEML 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 553371603 184 SLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVV 225
Cdd:TIGR01277 169 ALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVV 210
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
7-231 |
3.16e-33 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 121.38 E-value: 3.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 7 IQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAmveRRFG 86
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELA---RRRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 87 VLFQRGALFSSLTVTENVALPLIeNAGLPRSEAERLAQVKLALAGLPPGTGSKYPaSLSGGMVKRVALARALA------- 159
Cdd:COG4559 79 VLPQHSSLAFPFTVEEVVALGRA-PHGSSAAQDRQIVREALALVGLAHLAGRSYQ-TLSGGEQQRVQLARVLAqlwepvd 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 553371603 160 LDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDAlNLTVFLVTHDLD--TLYtlCDRVAVLSQKKVLVVDTLDKV 231
Cdd:COG4559 157 GGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNlaAQY--ADRILLLHQGRLVAQGTPEEV 227
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-231 |
3.88e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 121.10 E-value: 3.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 7 IQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGL-----RRPTDGKIHVFGKDLMAlSGQSRAMV 81
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYS-PDVDPIEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 82 ERRFGVLFQRGALFSSLTVTENVALPLIENaGLPRSEAERLAQVKLAL--AGLPPGTGSK---YPASLSGGMVKRVALAR 156
Cdd:PRK14267 84 RREVGMVFQYPNPFPHLTIYDNVAIGVKLN-GLVKSKKELDERVEWALkkAALWDEVKDRlndYPSNLSGGQRQRLVIAR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 553371603 157 ALALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDalNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDTLDKV 231
Cdd:PRK14267 163 ALAMKPKILLMDEPTANIDPVGTAKIEELLFELKK--EYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKV 235
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
12-222 |
1.31e-32 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 120.18 E-value: 1.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 12 LVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAMVERRFGVLFQR 91
Cdd:PRK10419 18 LSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRDIQMVFQD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 92 --GALFSSLTVTENVALPLIENAGLprSEAERLAQVK--LALAGLPPGTGSKYPASLSGGMVKRVALARALALDPDILFL 167
Cdd:PRK10419 98 siSAVNPRKTVREIIREPLRHLLSL--DKAERLARASemLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLIL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 553371603 168 DEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKV 222
Cdd:PRK10419 176 DEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
21-222 |
1.42e-32 |
|
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: 124.87 E-value: 1.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 21 VHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAmveRRFGVLFQRGALFSSlTV 100
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWR---RQIAWVPQNPYLFAG-TI 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 101 TENVALplienaGLPRSEAERLAQVkLALAGL-------------PPGTGSkypASLSGGMVKRVALARALALDPDILFL 167
Cdd:COG4988 428 RENLRL------GRPDASDEELEAA-LEAAGLdefvaalpdgldtPLGEGG---RGLSGGQAQRLALARALLRDAPLLLL 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 553371603 168 DEPTAGLDPIGAAAFDSLIRTLrdALNLTVFLVTHDLDTLyTLCDRVAVLSQKKV 222
Cdd:COG4988 498 DEPTAHLDAETEAEILQALRRL--AKGRTVILITHRLALL-AQADRILVLDDGRI 549
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
26-236 |
2.23e-32 |
|
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: 121.36 E-value: 2.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 26 NLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLmaLSGQSRAMV---ERRFGVLFQRGALFSSLTVTE 102
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL--QDSARGIFLpphRRRIGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 103 NValplieNAGLPRSEAE----RLAQV--KLALAGLPpgtgSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDP 176
Cdd:COG4148 97 NL------LYGRKRAPRAerriSFDEVveLLGIGHLL----DRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 177 IGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDTLDKVAATDD 236
Cdd:COG4148 167 ARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPD 226
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
25-236 |
3.70e-32 |
|
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: 120.99 E-value: 3.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 25 LNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMalsgQSRAMV-----ERRFGVLFQRGALFSSLT 99
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLF----DSRKGIflppeKRRIGYVFQEARLFPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 100 VTENValplieNAGLPRSEAE----RLAQVkLALAGLPPGTGsKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLD 175
Cdd:TIGR02142 92 VRGNL------RYGMKRARPSerriSFERV-IELLGIGHLLG-RLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 553371603 176 PIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDTLDKVAATDD 236
Cdd:TIGR02142 164 DPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPD 224
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
23-223 |
3.72e-32 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 117.85 E-value: 3.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 23 QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRP----TDGKIHVFGKDLMALSGQSRAmverrFGVLFQ--RGAlFS 96
Cdd:TIGR02770 3 QDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRPLLPLSIRGRH-----IATIMQnpRTA-FN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 97 SLTVTENVALPLIENAGLPRSEAERLAQVKLALAGLPPGTG--SKYPASLSGGMVKRVALARALALDPDILFLDEPTAGL 174
Cdd:TIGR02770 77 PLFTMGNHAIETLRSLGKLSKQARALILEALEAVGLPDPEEvlKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 553371603 175 DPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKVL 223
Cdd:TIGR02770 157 DVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIV 205
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
24-223 |
5.24e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 119.42 E-value: 5.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 24 GLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAMVE--------------------- 82
Cdd:PRK13651 25 NVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEKVleklviqktrfkkikkikeir 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 83 RRFGVLFQRG--ALFSSlTVTENVALPLIeNAGLPRSEAERLAQVKLALAGLPPGTGSKYPASLSGGMVKRVALARALAL 160
Cdd:PRK13651 105 RRVGVVFQFAeyQLFEQ-TIEKDIIFGPV-SMGVSKEEAKKRAAKYIELVGLDESYLQRSPFELSGGQKRRVALAGILAM 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 553371603 161 DPDILFLDEPTAGLDPIGAAAFDSLIRTLRDAlNLTVFLVTHDLDTLYTLCDRVAVLSQKKVL 223
Cdd:PRK13651 183 EPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDGKII 244
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
23-242 |
5.32e-32 |
|
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: 123.34 E-value: 5.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 23 QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAmveRRFGVLFQRGALFSSlTVTE 102
Cdd:COG4987 352 DGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLR---RRIAVVPQRPHLFDT-TLRE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 103 NValpLIENAGLPRSEAER-LAQVKLA--LAGLPPG-------TGskypASLSGGMVKRVALARALALDPDILFLDEPTA 172
Cdd:COG4987 428 NL---RLARPDATDEELWAaLERVGLGdwLAALPDGldtwlgeGG----RRLSGGERRRLALARALLRDAPILLLDEPTE 500
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 553371603 173 GLDPIGAAAfdsLIRTLRDAL-NLTVFLVTHDLDTLyTLCDRVAVLSQKKVLVVDTLDKVAATDDGWIQAY 242
Cdd:COG4987 501 GLDAATEQA---LLADLLEALaGRTVLLITHRLAGL-ERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLY 567
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-242 |
7.19e-32 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 117.78 E-value: 7.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 1 MTQDaIIQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAm 80
Cdd:PRK11300 1 MSQP-LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 81 verRFGVL--FQRGALFSSLTVTEN--VALPLIENAGL-------P---RSEAERLAQVK--------LALAGLPPGTgs 138
Cdd:PRK11300 79 ---RMGVVrtFQHVRLFREMTVIENllVAQHQQLKTGLfsgllktPafrRAESEALDRAAtwlervglLEHANRQAGN-- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 139 kypasLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLS 218
Cdd:PRK11300 154 -----LAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVN 228
|
250 260
....*....|....*....|....
gi 553371603 219 QKKVLVVDTLDKVaATDDGWIQAY 242
Cdd:PRK11300 229 QGTPLANGTPEEI-RNNPDVIKAY 251
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-221 |
8.46e-32 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 120.33 E-value: 8.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 6 IIQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAMverrf 85
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPI----- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 86 GVLFQRGALFSSLTVTENVALPLIENAgLPRSE-AERLAQVkLALAGLPPGTGSKyPASLSGGMVKRVALARALALDPDI 164
Cdd:PRK11607 94 NMMFQSYALFPHMTVEQNIAFGLKQDK-LPKAEiASRVNEM-LGLVHMQEFAKRK-PHQLSGGQRQRVALARSLAKRPKL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 553371603 165 LFLDEPTAGLDpigaaafdsliRTLRDALNL-----------TVFLVTHDLDTLYTLCDRVAVLSQKK 221
Cdd:PRK11607 171 LLLDEPMGALD-----------KKLRDRMQLevvdilervgvTCVMVTHDQEEAMTMAGRIAIMNRGK 227
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
7-223 |
9.51e-32 |
|
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: 116.14 E-value: 9.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 7 IQIRDLVNCFGVQCVHQGLNLDVKRGeVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMAlsgqSRAMVERRFG 86
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK----QPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 87 VLFQRGALFSSLTVTENVALPLIENaGLPRSEAERLAQVKLALAGLPPgTGSKYPASLSGGMVKRVALARALALDPDILF 166
Cdd:cd03264 76 YLPQEFGVYPNFTVREFLDYIAWLK-GIPSKEVKARVDEVLELVNLGD-RAKKKIGSLSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 553371603 167 LDEPTAGLDPIGAAAFDSLIRTLrdALNLTVFLVTHDLDTLYTLCDRVAVLSQKKVL 223
Cdd:cd03264 154 VDEPTAGLDPEERIRFRNLLSEL--GEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
7-223 |
1.29e-31 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 116.65 E-value: 1.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 7 IQIRDlVNCF-GVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGK--DLMA-LSGQSRAMVE 82
Cdd:COG4161 3 IQLKN-INCFyGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQkPSEKAIRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 83 RRFGVLFQRGALFSSLTVTENvalpLIEN----AGLPRSEAERLAQVKLALAGLPPGTGSkYPASLSGGMVKRVALARAL 158
Cdd:COG4161 82 QKVGMVFQQYNLWPHLTVMEN----LIEApckvLGLSKEQAREKAMKLLARLRLTDKADR-FPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 553371603 159 ALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDAlNLTVFLVTHDLDTLYTLCDRVAVLSQKKVL 223
Cdd:COG4161 157 MMEPQVLLFDEPTAALDPEITAQVVEIIRELSQT-GITQVIVTHEVEFARKVASQVVYMEKGRII 220
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-222 |
2.08e-31 |
|
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: 121.33 E-value: 2.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 1 MTQDAIIQIRDLVNCFG-----VQCVHqGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGL----RRPTDGKIHVFGKDLM 71
Cdd:COG4172 1 MMSMPLLSVEDLSVAFGqgggtVEAVK-GVSFDIAAGETLALVGESGSGKSVTALSILRLlpdpAAHPSGSILFDGQDLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 72 ALS-GQSRAMVERRFGVLFQRGalFSSL----TVTENVALPLIENAGLPRSEAERLAQVKLALAGLPPGTG--SKYPASL 144
Cdd:COG4172 80 GLSeRELRRIRGNRIAMIFQEP--MTSLnplhTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERrlDAYPHQL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 553371603 145 SGGMVKRVALARALALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKV 222
Cdd:COG4172 158 SGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEI 235
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
4-245 |
2.38e-31 |
|
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: 115.85 E-value: 2.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 4 DAIIQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAmver 83
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIA---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 84 RFGVLF--QRGALFSSLTVTENVALPLIeNAGLPRSEAERLAQV-----KLA-----LAGlppgtgskypaSLSGG---M 148
Cdd:COG0410 77 RLGIGYvpEGRRIFPSLTVEENLLLGAY-ARRDRAEVRADLERVyelfpRLKerrrqRAG-----------TLSGGeqqM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 149 VkrvALARALALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDAlNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDTL 228
Cdd:COG0410 145 L---AIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTA 220
|
250
....*....|....*..
gi 553371603 229 DKVAATDDGwIQAYFHG 245
Cdd:COG0410 221 AELLADPEV-REAYLGV 236
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
6-233 |
4.07e-31 |
|
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: 115.45 E-value: 4.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 6 IIQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAmverRF 85
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERA----RL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 86 GV--LFQRGALFSSLTVTENV--ALPLIENagLPRSEAERLAQVKLALAGLPPgTGSKYPASLSGGMVKRVALARALALD 161
Cdd:TIGR04406 77 GIgyLPQEASIFRKLTVEENImaVLEIRKD--LDRAEREERLEALLEEFQISH-LRDNKAMSLSGGERRRVEIARALATN 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 553371603 162 PDILFLDEPTAGLDPIGAAAFDSLIRTLRDAlNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDTLDKVAA 233
Cdd:TIGR04406 154 PKFILLDEPFAGVDPIAVGDIKKIIKHLKER-GIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVA 224
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
24-217 |
4.09e-31 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 117.50 E-value: 4.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 24 GLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAMVERRFGVLFQR--GALFSSLTVT 101
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQDplASLNPRMTIG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 102 ENVALPL-IENAGLPRSEAERLAQVKLALAGLPPGTGSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAA 180
Cdd:PRK15079 119 EIIAEPLrTYHPKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQA 198
|
170 180 190
....*....|....*....|....*....|....*..
gi 553371603 181 AFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVL 217
Cdd:PRK15079 199 QVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVM 235
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
25-222 |
6.20e-31 |
|
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: 114.13 E-value: 6.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 25 LNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSgqsraMVERRFGVLFQRGALFSSLTVTENV 104
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAP-----PADRPVSMLFQENNLFAHLTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 105 ALPLieNAGLPRSEAERLA-QVKLALAGLPpGTGSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAAAFD 183
Cdd:cd03298 92 GLGL--SPGLKLTAEDRQAiEVALARVGLA-GLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 553371603 184 SLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKV 222
Cdd:cd03298 169 DLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
25-227 |
6.78e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 116.05 E-value: 6.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 25 LNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTD---GKIHVFGkdlMALSGQSRAMVERRFGVLFQR-GALFSSLTV 100
Cdd:PRK13640 26 ISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDG---ITLTAKTVWDIREKVGIVFQNpDNQFVGATV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 101 TENVALPLiENAGLPRSEAERLAQVKLALAGLPPGTGSKyPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAA 180
Cdd:PRK13640 103 GDDVAFGL-ENRAVPRPEMIKIVRDVLADVGMLDYIDSE-PANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKE 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 553371603 181 AFDSLIRTLRDALNLTVFLVTHDLDTLyTLCDRVAVLSQKKVLVVDT 227
Cdd:PRK13640 181 QILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGS 226
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-243 |
7.00e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 116.36 E-value: 7.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 6 IIQIRDLVNCFG-VQCVHqGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLmalsgqSRAMVeRR 84
Cdd:COG4152 1 MLELKGLTKRFGdKTAVD-DVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL------DPEDR-RR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 85 FGVLFQ-RGaLFSSLTVTEnVALPLIENAGLPRSEAERLAQVKLALAGLPPGTGSKYpASLSGGMVKRVALARALALDPD 163
Cdd:COG4152 73 IGYLPEeRG-LYPKMKVGE-QLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKV-EELSKGNQQKVQLIAALLHDPE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 164 ILFLDEPTAGLDPIGAAAFDSLIRTLRDAlNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDTLDKV------------ 231
Cdd:COG4152 150 LLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIrrqfgrntlrle 228
|
250
....*....|..
gi 553371603 232 AATDDGWIQAYF 243
Cdd:COG4152 229 ADGDAGWLRALP 240
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
23-222 |
7.05e-31 |
|
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: 112.69 E-value: 7.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 23 QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVfgkDLMALSGQSRAMVERRFGVLFQRGALFSSlTVTE 102
Cdd:cd03246 19 RNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRL---DGADISQWDPNELGDHVGYLPQDDELFSG-SIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 103 NValplienaglprseaerlaqvklalaglppgtgskypasLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAAAF 182
Cdd:cd03246 95 NI---------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERAL 135
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 553371603 183 DSLIRTLRdALNLTVFLVTHDLDTLyTLCDRVAVLSQKKV 222
Cdd:cd03246 136 NQAIAALK-AAGATRIVIAHRPETL-ASADRILVLEDGRV 173
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
25-222 |
9.04e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 115.47 E-value: 9.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 25 LNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLmalSGQSRAMVERRFGVLFQR-GALFSSLTVTEN 103
Cdd:PRK13632 28 VSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI---SKENLKEIRKKIGIIFQNpDNQFIGATVEDD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 104 VALPLiENAGLPRSEA----ERLAQVKLALAGLppgtgSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGA 179
Cdd:PRK13632 105 IAFGL-ENKKVPPKKMkdiiDDLAKKVGMEDYL-----DKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGK 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 553371603 180 AAFDSLIRTLRDALNLTVFLVTHDLDTLyTLCDRVAVLSQKKV 222
Cdd:PRK13632 179 REIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKL 220
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
7-223 |
1.06e-30 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 114.34 E-value: 1.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 7 IQIRDlVNCF-GVqcvHQGL---NLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGK--DLMALSGQSRAM 80
Cdd:PRK11124 3 IQLNG-INCFyGA---HQALfdiTLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSDKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 81 VERR-FGVLFQRGALFSSLTVTENvalpLIEN----AGLPRSEAERLAQVKLALAGLPPGTGsKYPASLSGGMVKRVALA 155
Cdd:PRK11124 79 ELRRnVGMVFQQYNLWPHLTVQQN----LIEApcrvLGLSKDQALARAEKLLERLRLKPYAD-RFPLHLSGGQQQRVAIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 553371603 156 RALALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDAlNLTVFLVTHDLDTLYTLCDRVAVLSQKKVL 223
Cdd:PRK11124 154 RALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENGHIV 220
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
26-245 |
1.58e-30 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 117.44 E-value: 1.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 26 NLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALS-GQSRAMVERRFGVLFQRGALFSSLTVTENV 104
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdAELREVRRKKIAMVFQSFALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 105 ALPLiENAGLPRSEAERLAQVKLALAGLPpGTGSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAAAFDS 184
Cdd:PRK10070 128 AFGM-ELAGINAEERREKALDALRQVGLE-NYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQD 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 553371603 185 LIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDTLDKVAATD-DGWIQAYFHG 245
Cdd:PRK10070 206 ELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPaNDYVRTFFRG 267
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
25-243 |
3.07e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 114.16 E-value: 3.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 25 LNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSG-QSRAMVERRFGVLFQrgalFSSLTVTEN 103
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGnKNLKKLRKKVSLVFQ----FPEAQLFEN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 104 VALPLIE----NAGLPRSEAERLAQVKLALAGLPPGTGSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGA 179
Cdd:PRK13641 102 TVLKDVEfgpkNFGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGR 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 553371603 180 AAFDSLIRTLRDALNlTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDTLDKVaATDDGWIQAYF 243
Cdd:PRK13641 182 KEMMQLFKDYQKAGH-TVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEI-FSDKEWLKKHY 243
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
6-223 |
4.84e-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: 4.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 6 IIQIRDLVNCFG-----VQCVhQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMalsgQSRAM 80
Cdd:cd03266 1 MITADALTKRFRdvkktVQAV-DGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV----KEPAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 81 VERRFGVLFQRGALFSSLTVTENVALpLIENAGLPRSEAERLAQVKLALAGLPPgTGSKYPASLSGGMVKRVALARALAL 160
Cdd:cd03266 76 ARRRLGFVSDSTGLYDRLTARENLEY-FAGLYGLKGDELTARLEELADRLGMEE-LLDRRVGGFSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 553371603 161 DPDILFLDEPTAGLDPIGAAAFDSLIRTLRDAlNLTVFLVTHDLDTLYTLCDRVAVLSQKKVL 223
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
7-230 |
5.40e-30 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 112.11 E-value: 5.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 7 IQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLmalsgqSRAMVeRRFG 86
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPW------TRKDL-HKIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 87 VLFQRGALFSSLTVTENVALpLIENAGLPRSEAERLaqvkLALAGLPpGTGSKYPASLSGGMVKRVALARALALDPDILF 166
Cdd:TIGR03740 74 SLIESPPLYENLTARENLKV-HTTLLGLPDSRIDEV----LNIVDLT-NTGKKKAKQFSLGMKQRLGIAIALLNHPKLLI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 553371603 167 LDEPTAGLDPIGAAAFDSLIRTLRDAlNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDTLDK 230
Cdd:TIGR03740 148 LDEPTNGLDPIGIQELRELIRSFPEQ-GITVILSSHILSEVQQLADHIGIISEGVLGYQGKINK 210
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
23-213 |
6.94e-30 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 111.79 E-value: 6.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 23 QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAMVE-RRFGVLFQRGALFSSLTVT 101
Cdd:PRK10584 27 TGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRaKHVGFVFQSFMLIPTLNAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 102 ENVALPlienaGLPRSEAERLA--QVKLALAGLPPGTGSKY-PASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIG 178
Cdd:PRK10584 107 ENVELP-----ALLRGESSRQSrnGAKALLEQLGLGKRLDHlPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQT 181
|
170 180 190
....*....|....*....|....*....|....*
gi 553371603 179 AAAFDSLIRTLRDALNLTVFLVTHDlDTLYTLCDR 213
Cdd:PRK10584 182 GDKIADLLFSLNREHGTTLILVTHD-LQLAARCDR 215
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
21-236 |
1.29e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 115.89 E-value: 1.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 21 VHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSgqSRAMVERRFGVL----FQRGaLFS 96
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRS--PRDAIRAGIAYVpedrKGEG-LVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 97 SLTVTENVALPLIE---NAGLPRSEAER-LAQ-------VKLALAGLPPGTgskypasLSGGMVKRVALARALALDPDIL 165
Cdd:COG1129 344 DLSIRENITLASLDrlsRGGLLDRRRERaLAEeyikrlrIKTPSPEQPVGN-------LSGGNQQKVVLAKWLATDPKVL 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 553371603 166 FLDEPTAGLDpIGA-AAFDSLIRTLRDAlNLTVFLVTHDLDTLYTLCDRVAVLSQKKvlVVDTLDKVAATDD 236
Cdd:COG1129 417 ILDEPTRGID-VGAkAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGR--IVGELDREEATEE 484
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-218 |
1.45e-29 |
|
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: 110.99 E-value: 1.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 1 MTqdAIIQIRDLVNCF------GVQC-VHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHV---FGK-D 69
Cdd:COG4778 1 MT--TLLEVENLSKTFtlhlqgGKRLpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdGGWvD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 70 LMALSgqSRAMVERRFGVL-----FQR-----GALfssltvtENVALPLIEnAGLPRSEAERLAQVKLALAGLPPGTGSK 139
Cdd:COG4778 79 LAQAS--PREILALRRRTIgyvsqFLRviprvSAL-------DVVAEPLLE-RGVDREEARARARELLARLNLPERLWDL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 140 YPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRD---ALnLTVFlvtHDLDTLYTLCDRVAV 216
Cdd:COG4778 149 PPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKArgtAI-IGIF---HDEEVREAVADRVVD 224
|
..
gi 553371603 217 LS 218
Cdd:COG4778 225 VT 226
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
23-233 |
1.75e-29 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 111.33 E-value: 1.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 23 QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVfgkdlmalSGQSRAMVErrFGVLFQrgalfSSLTVTE 102
Cdd:COG1134 43 KDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEV--------NGRVSALLE--LGAGFH-----PELTGRE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 103 NVALplieNA---GLPRSE-AERLAQVkLALAGL------PPGTgskYpaslSGGMVKRVALARALALDPDILFLDEPTA 172
Cdd:COG1134 108 NIYL----NGrllGLSRKEiDEKFDEI-VEFAELgdfidqPVKT---Y----SSGMRARLAFAVATAVDPDILLVDEVLA 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 553371603 173 gldpIGAAAF----DSLIRTLRDAlNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDTLDKVAA 233
Cdd:COG1134 176 ----VGDAAFqkkcLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
6-205 |
2.34e-29 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 111.33 E-value: 2.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 6 IIQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKdlmALSGQSramVERrf 85
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK---PVEGPG---AER-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 86 GVLFQRGALFSSLTVTENVALPLiENAGLPRSEAERLAQVKLALAGLPpGTGSKYPASLSGGMVKRVALARALALDPDIL 165
Cdd:PRK11248 73 GVVFQNEGLLPWRNVQDNVAFGL-QLAGVEKMQRLEIAHQMLKKVGLE-GAEKRYIWQLSGGQRQRVGIARALAANPQLL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 553371603 166 FLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLD 205
Cdd:PRK11248 151 LLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIE 190
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
21-222 |
2.96e-29 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 115.19 E-value: 2.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 21 VHQGLNLDVKRGEVLGVVGGSGTGKSV----LLRSIvglrrPTDGKIHVFGKDLMALSGQSRAMVERRFGVLFQ--RGAL 94
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQdpNSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 95 FSSLTVTENVALPL-IENAGLprSEAERLAQVKLALA--GLPPGTGSKYPASLSGGMVKRVALARALALDPDILFLDEPT 171
Cdd:PRK15134 376 NPRLNVLQIIEEGLrVHQPTL--SAAQREQQVIAVMEevGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPT 453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 553371603 172 AGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKV 222
Cdd:PRK15134 454 SSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEV 504
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
29-204 |
6.70e-29 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 109.52 E-value: 6.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 29 VKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAMVE-RRFGVLFQRGALFSSLTVTENVALP 107
Cdd:PRK11629 32 IGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRnQKLGFIYQFHHLLPDFTALENVAMP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 108 LIEnAGLPRSEAERLAQVKLALAGLPPgTGSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAaafDSLIR 187
Cdd:PRK11629 112 LLI-GKKKPAEINSRALEMLAAVGLEH-RANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNA---DSIFQ 186
|
170 180
....*....|....*....|.
gi 553371603 188 TLRDaLNL---TVFL-VTHDL 204
Cdd:PRK11629 187 LLGE-LNRlqgTAFLvVTHDL 206
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
23-217 |
9.46e-29 |
|
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: 113.92 E-value: 9.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 23 QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRamvERRFGVLFQRGALFSSlTVTE 102
Cdd:TIGR02857 339 RPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW---RDQIAWVPQHPFLFAG-TIAE 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 103 NVALPLIENAGLPRSEAERLAQVKLALAGLPPGTGSKY---PASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGA 179
Cdd:TIGR02857 415 NIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIgegGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETE 494
|
170 180 190
....*....|....*....|....*....|....*...
gi 553371603 180 AAFDSLIRTLRDalNLTVFLVTHDLDTLYtLCDRVAVL 217
Cdd:TIGR02857 495 AEVLEALRALAQ--GRTVLLVTHRLALAA-LADRIVVL 529
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-217 |
1.53e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 112.80 E-value: 1.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 4 DAIIQIRDLVNCF-GVQcVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSgqSRAMVE 82
Cdd:COG1129 2 EPLLEMRGISKSFgGVK-ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRS--PRDAQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 83 RRFGVLFQRGALFSSLTVTENVALP-LIENAGL-PRSEAERLAQVKLALAGL--PPGTgskyPAS-LSGGMVKRVALARA 157
Cdd:COG1129 79 AGIAIIHQELNLVPNLSVAENIFLGrEPRRGGLiDWRAMRRRARELLARLGLdiDPDT----PVGdLSVAQQQLVEIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 158 LALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDAlNLTVFLVTHDLDTLYTLCDRVAVL 217
Cdd:COG1129 155 LSRDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVL 213
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-217 |
2.00e-28 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 109.89 E-value: 2.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 5 AIIQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAmverR 84
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQ----R 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 85 FGVLFQRGALFSSLTVTENVaLPLIENAGLPRSEAERLAQVKLALAGLPPGTGSKYpASLSGGMVKRVALARALALDPDI 164
Cdd:PRK13537 82 VGVVPQFDNLDPDFTVRENL-LVFGRYFGLSAAAARALVPPLLEFAKLENKADAKV-GELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 553371603 165 LFLDEPTAGLDPIGAAAFDSLIRTLRdALNLTVFLVTHDLDTLYTLCDRVAVL 217
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVI 211
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
21-222 |
2.40e-28 |
|
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: 107.96 E-value: 2.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 21 VHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALsgqSRAMVERRFGVLFQRGALFSSlTV 100
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALA---DPAWLRRQVGVVLQENVLFNR-SI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 101 TENVALpliENAGLPRS---EAERLAQVKLALAGLPPGTGS---KYPASLSGGMVKRVALARALALDPDILFLDEPTAGL 174
Cdd:cd03252 93 RDNIAL---ADPGMSMErviEAAKLAGAHDFISELPEGYDTivgEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSAL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 553371603 175 DPIGAAAfdsLIRTLRDAL-NLTVFLVTHDLDTLYTlCDRVAVLSQKKV 222
Cdd:cd03252 170 DYESEHA---IMRNMHDICaGRTVIIIAHRLSTVKN-ADRIIVMEKGRI 214
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-223 |
3.19e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 108.67 E-value: 3.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 4 DAIIQIRDLVNCF--GVQCVhQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKdlmALSGQSRAMV 81
Cdd:PRK13647 2 DNIIEVEDLHFRYkdGTKAL-KGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGR---EVNAENEKWV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 82 ERRFGVLFQR--GALFSSlTVTENVAL-PLieNAGLPRSEAERLAQVKLALAGLPpGTGSKYPASLSGGMVKRVALARAL 158
Cdd:PRK13647 78 RSKVGLVFQDpdDQVFSS-TVWDDVAFgPV--NMGLDKDEVERRVEEALKAVRMW-DFRDKPPYHLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 553371603 159 ALDPDILFLDEPTAGLDPIGAAAfdslIRTLRDALN---LTVFLVTHDLDTLYTLCDRVAVLSQKKVL 223
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQET----LMEILDRLHnqgKTVIVATHDVDLAAEWADQVIVLKEGRVL 217
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
24-240 |
3.26e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 108.64 E-value: 3.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 24 GLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMAlsgQSRAMVERRFGVLFQR-GALFSSLTVTE 102
Cdd:PRK13642 25 GVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTA---ENVWNLRRKIGMVFQNpDNQFVGATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 103 NVALPLiENAGLPRSEA-ERLAQVKLALAGLPPGTgsKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAAA 181
Cdd:PRK13642 102 DVAFGM-ENQGIPREEMiKRVDEALLAVNMLDFKT--REPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 553371603 182 FDSLIRTLRDALNLTVFLVTHDLDTLYTlCDRVAVLSQKKVLVVDTLDKVAATDDGWIQ 240
Cdd:PRK13642 179 IMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDMVE 236
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
23-218 |
6.07e-28 |
|
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: 106.59 E-value: 6.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 23 QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRP---TDGKIHVFGKDLmalsgqSRAMVERRFGVLFQRGALFSSLT 99
Cdd:cd03234 24 NDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPR------KPDQFQKCVAYVRQDDILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 100 VTEnvALPLIENAGLPRSEAE-----RLAQVKLALAGLPPgTGSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGL 174
Cdd:cd03234 98 VRE--TLTYTAILRLPRKSSDairkkRVEDVLLRDLALTR-IGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 553371603 175 DPIGAaafDSLIRTLRD--ALNLTVFLVTHDLDT-LYTLCDRVAVLS 218
Cdd:cd03234 175 DSFTA---LNLVSTLSQlaRRNRIVILTIHQPRSdLFRLFDRILLLS 218
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
26-235 |
7.44e-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: 7.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 26 NLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLmALSGQSRAMvERRFGVLFQRGALFSSLTVTENVA 105
Cdd:COG3845 25 SLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV-RIRSPRDAI-ALGIGMVHQHFMLVPNLTVAENIV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 106 LPLIENAG--LPRSEAERLAQVKLALAGLP--PgtgSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAaa 181
Cdd:COG3845 103 LGLEPTKGgrLDRKAARARIRELSERYGLDvdP---DAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEA-- 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 553371603 182 fDSLIRTLRD--ALNLTVFLVTHDLDTLYTLCDRVAVLSQKKvlVVDTLDkVAATD 235
Cdd:COG3845 178 -DELFEILRRlaAEGKSIIFITHKLREVMAIADRVTVLRRGK--VVGTVD-TAETS 229
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
23-219 |
7.51e-28 |
|
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: 111.38 E-value: 7.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 23 QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVfgkDLMALSGQSRAMVERRFGVLFQRGALFSSlTVTE 102
Cdd:COG4618 349 RGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRL---DGADLSQWDREELGRHIGYLPQDVELFDG-TIAE 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 103 NVA-LPLIEnaglPRS--EAERLAQVKLALAGLPPGtgskY-------PASLSGGMVKRVALARALALDPDILFLDEPTA 172
Cdd:COG4618 425 NIArFGDAD----PEKvvAAAKLAGVHEMILRLPDG----YdtrigegGARLSGGQRQRIGLARALYGDPRLVVLDEPNS 496
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 553371603 173 GLDPIGAAAFDSLIRTLRDAlNLTVFLVTHDLDTLyTLCDRVAVLSQ 219
Cdd:COG4618 497 NLDDEGEAALAAAIRALKAR-GATVVVITHRPSLL-AAVDKLLVLRD 541
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
5-219 |
8.94e-28 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 109.16 E-value: 8.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 5 AIIQIRDLVNCF--GVQCVHqGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSR--AM 80
Cdd:PRK11650 2 AGLKLQAVRKSYdgKTQVIK-GIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRdiAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 81 VerrfgvlFQRGALFSSLTVTENVALPLiENAGLPRSE-AERLAQVKLALaGLPPGTGSKyPASLSGGMVKRVALARALA 159
Cdd:PRK11650 81 V-------FQNYALYPHMSVRENMAYGL-KIRGMPKAEiEERVAEAARIL-ELEPLLDRK-PRELSGGQRQRVAMGRAIV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 160 LDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQ 219
Cdd:PRK11650 151 REPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNG 210
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-222 |
1.13e-27 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 106.93 E-value: 1.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 1 MTQDAIIQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGK-----DLMALSG 75
Cdd:PRK11701 1 MMDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 76 QSRAMVER-RFGVLFQ--RGALFSSLTVTENVALPLI----ENAGLPRSEAER-LAQVKLALAGLppgtgSKYPASLSGG 147
Cdd:PRK11701 81 AERRRLLRtEWGFVHQhpRDGLRMQVSAGGNIGERLMavgaRHYGDIRATAGDwLERVEIDAARI-----DDLPTTFSGG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 553371603 148 MVKRVALARALALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKV 222
Cdd:PRK11701 156 MQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRV 230
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
9-226 |
1.23e-27 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 106.69 E-value: 1.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 9 IRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAMverrfgvl 88
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRLM-------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 89 FQRGALFSSLTVTENVALPLienAGLPRSEAER-LAQVKLAlaglppGTGSKYPASLSGGMVKRVALARALALDPDILFL 167
Cdd:PRK11247 87 FQDARLLPWKKVIDNVGLGL---KGQWRDAALQaLAAVGLA------DRANEWPAALSGGQKQRVALARALIHRPGLLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 553371603 168 DEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKV---LVVD 226
Cdd:PRK11247 158 DEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIgldLTVD 219
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-223 |
2.34e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 105.77 E-value: 2.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 5 AIIQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGL-----RRPTDGKIHVFGKDLMALSgqsRA 79
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMD---VI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 80 MVERRFGVLFQRGALFSSLTVTENVALPLIENAgLPRSEAERLAQVKLAL--AGLPPGTGSKYPA---SLSGGMVKRVAL 154
Cdd:PRK14247 79 ELRRRVQMVFQIPNPIPNLSIFENVALGLKLNR-LVKSKKELQERVRWALekAQLWDEVKDRLDApagKLSGGQQQRLCI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 553371603 155 ARALALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDalNLTVFLVTHDLDTLYTLCDRVAVLSQKKVL 223
Cdd:PRK14247 158 ARALAFQPEVLLADEPTANLDPENTAKIESLFLELKK--DMTIVLVTHFPQQAARISDYVAFLYKGQIV 224
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-222 |
2.98e-27 |
|
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: 102.89 E-value: 2.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 7 IQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSgqSRAMVERRFG 86
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAS--PRDARRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 87 VLFQrgalfssltvtenvalplienaglprseaerlaqvklalaglppgtgskypasLSGGMVKRVALARALALDPDILF 166
Cdd:cd03216 79 MVYQ-----------------------------------------------------LSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 553371603 167 LDEPTAGLDPIGAAAFDSLIRTLRDAlNLTVFLVTHDLDTLYTLCDRVAVLSQKKV 222
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
23-222 |
4.39e-27 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 109.48 E-value: 4.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 23 QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQS-RamveRRFGVLFQRGALFsSLTVT 101
Cdd:COG1132 357 KDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlR----RQIGVVPQDTFLF-SGTIR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 102 ENVALplienaGLPR-SEAE-----RLAQVKLALAGLPPG--T-----GSKypasLSGGMVKRVALARALALDPDILFLD 168
Cdd:COG1132 432 ENIRY------GRPDaTDEEveeaaKAAQAHEFIEALPDGydTvvgerGVN----LSGGQRQRIAIARALLKDPPILILD 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 553371603 169 EPTAGLDPIGAAA-FDSLIRTLRDAlnlTVFLVTHDLDTLyTLCDRVAVLSQKKV 222
Cdd:COG1132 502 EATSALDTETEALiQEALERLMKGR---TTIVIAHRLSTI-RNADRILVLDDGRI 552
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
23-224 |
5.14e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 105.45 E-value: 5.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 23 QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRamVERRFGVLFQRGAL-FSSLTVT 101
Cdd:PRK13644 19 ENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQG--IRKLVGIVFQNPETqFVGRTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 102 ENVAL-PliENAGLPRSEAERLAQVKLALAGLppgtgSKY----PASLSGGMVKRVALARALALDPDILFLDEPTAGLDP 176
Cdd:PRK13644 97 EDLAFgP--ENLCLPPIEIRKRVDRALAEIGL-----EKYrhrsPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 553371603 177 IGAAAFDSLIRTLRDAlNLTVFLVTHDLDTLYTlCDRVAVLSQKKVLV 224
Cdd:PRK13644 170 DSGIAVLERIKKLHEK-GKTIVYITHNLEELHD-ADRIIVMDRGKIVL 215
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-223 |
6.33e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 106.09 E-value: 6.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 1 MTQDAIIQIRDLVNCFGVQCVHQ-----GLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHV--------FG 67
Cdd:PRK13631 16 LSDDIILRVKNLYCVFDEKQENElvalnNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkKN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 68 KDLMALSGQSRAM-----VERRFGVLFQ--RGALFSSlTVTENVALPLIeNAGLPRSEAERLAQVKLALAGLPPGTGSKY 140
Cdd:PRK13631 96 NHELITNPYSKKIknfkeLRRRVSMVFQfpEYQLFKD-TIEKDIMFGPV-ALGVKKSEAKKLAKFYLNKMGLDDSYLERS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 141 PASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRdALNLTVFLVTHDLDTLYTLCDRVAVLSQK 220
Cdd:PRK13631 174 PFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAK-ANNKTVFVITHTMEHVLEVADEVIVMDKG 252
|
...
gi 553371603 221 KVL 223
Cdd:PRK13631 253 KIL 255
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
23-219 |
8.32e-27 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 103.80 E-value: 8.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 23 QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAMVERRFGVLFQRGALFSSLTVTE 102
Cdd:PRK10908 19 QGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQIGMIFQDHHLLMDRTVYD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 103 NVALPLIEnAGLPRSEAERLAQVKLALAGLpPGTGSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDpigaAAF 182
Cdd:PRK10908 99 NVAIPLII-AGASGDDIRRRVSAALDKVGL-LDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD----DAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 553371603 183 DSLIRTLRDALN---LTVFLVTHDLDTLYTLCDRVAVLSQ 219
Cdd:PRK10908 173 SEGILRLFEEFNrvgVTVLMATHDIGLISRRSYRMLTLSD 212
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
17-204 |
8.42e-27 |
|
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: 108.22 E-value: 8.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 17 GVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSramVERRFGVLFQRGALFS 96
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDE---VRRRVSVCAQDAHLFD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 97 SlTVTENValpLIENAGLPRSEAER-LAQVKLA--LAGLPPGTGSKY---PASLSGGMVKRVALARALALDPDILFLDEP 170
Cdd:TIGR02868 423 T-TVRENL---RLARPDATDEELWAaLERVGLAdwLRALPDGLDTVLgegGARLSGGERQRLALARALLADAPILLLDEP 498
|
170 180 190
....*....|....*....|....*....|....*
gi 553371603 171 TAGLDPIGAaafDSLIRTLRDALN-LTVFLVTHDL 204
Cdd:TIGR02868 499 TEHLDAETA---DELLEDLLAALSgRTVVLITHHL 530
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
7-217 |
1.14e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 106.07 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 7 IQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGkdlMALSGQSRAmVERRFG 86
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG---VPVPARARL-ARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 87 VLFQRGALFSSLTVTENVaLPLIENAGLPRSEAERLAQVKLALAGLPPGTGSKYpASLSGGMVKRVALARALALDPDILF 166
Cdd:PRK13536 118 VVPQFDNLDLEFTVRENL-LVFGRYFGMSTREIEAVIPSLLEFARLESKADARV-SDLSGGMKRRLTLARALINDPQLLI 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 553371603 167 LDEPTAGLDPIGAAAFDSLIRTLRdALNLTVFLVTHDLDTLYTLCDRVAVL 217
Cdd:PRK13536 196 LDEPTTGLDPHARHLIWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVL 245
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
24-217 |
2.85e-26 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 104.66 E-value: 2.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 24 GLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAMVERRFGVLFQRGalFSSL----T 99
Cdd:PRK11308 33 GVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKIQIVFQNP--YGSLnprkK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 100 VTENVALPLIENAGLPRSEAERLAQVKLALAGLPPGTGSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGA 179
Cdd:PRK11308 111 VGQILEEPLLINTSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQ 190
|
170 180 190
....*....|....*....|....*....|....*...
gi 553371603 180 AAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVL 217
Cdd:PRK11308 191 AQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVM 228
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
25-219 |
5.21e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 102.94 E-value: 5.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 25 LNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAM-VERRFGVLFQ--RGALFSSLTVT 101
Cdd:PRK13646 26 VNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRpVRKRIGMVFQfpESQLFEDTVER 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 102 ENVALPliENAGLPRSEAERLAQVKLALAGLPPGTGSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAAA 181
Cdd:PRK13646 106 EIIFGP--KNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQ 183
|
170 180 190
....*....|....*....|....*....|....*...
gi 553371603 182 FDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQ 219
Cdd:PRK13646 184 VMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKE 221
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
21-203 |
8.89e-26 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 105.96 E-value: 8.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 21 VHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAMVERR-FGVLFQRGALFSSLT 99
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRREhFGFIFQRYHLLSHLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 100 VTENVALPLIEnAGLPRSEAERLAQVKLALAGLPPGTgSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGA 179
Cdd:PRK10535 103 AAQNVEVPAVY-AGLERKQRLLRAQELLQRLGLEDRV-EYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSG 180
|
170 180
....*....|....*....|....
gi 553371603 180 AAFDSLIRTLRDALNlTVFLVTHD 203
Cdd:PRK10535 181 EEVMAILHQLRDRGH-TVIIVTHD 203
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-223 |
1.36e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 101.62 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 21 VHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKdlmALSGQSRAMVERRFGV--LFQ--RGALFS 96
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGK---PLDYSKRGLLALRQQVatVFQdpEQQIFY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 97 SlTVTENVALPLiENAGLPRSEAERlaQVKLALAGLPPGTGSKYPAS-LSGGMVKRVALARALALDPDILFLDEPTAGLD 175
Cdd:PRK13638 93 T-DIDSDIAFSL-RNLGVPEAEITR--RVDEALTLVDAQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 553371603 176 PIGAAAFDSLIRTLRDALNlTVFLVTHDLDTLYTLCDRVAVLSQKKVL 223
Cdd:PRK13638 169 PAGRTQMIAIIRRIVAQGN-HVIISSHDIDLIYEISDAVYVLRQGQIL 215
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
23-223 |
1.51e-25 |
|
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: 100.48 E-value: 1.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 23 QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKdlmaLSGQSRAMVERRFGVLF-QRGALFSSLTVT 101
Cdd:cd03267 38 KGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL----VPWKRRKKFLRRIGVVFgQKTQLWWDLPVI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 102 ENVALpLIENAGLPRSEA-ERLAQVK--LALAGLppgtgSKYPA-SLSGGMVKRVALARALALDPDILFLDEPTAGLDPI 177
Cdd:cd03267 114 DSFYL-LAAIYDLPPARFkKRLDELSelLDLEEL-----LDTPVrQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 553371603 178 GAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKVL 223
Cdd:cd03267 188 AQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
5-231 |
2.43e-25 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 100.68 E-value: 2.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 5 AIIQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAMVERR 84
Cdd:TIGR02323 2 PLLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLSEAERR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 85 F------GVLFQ--RGALFSSLTVTENVALPLIENAGLPRSEAERLAQVKLALAGLPPGTGSKYPASLSGGMVKRVALAR 156
Cdd:TIGR02323 82 RlmrtewGFVHQnpRDGLRMRVSAGANIGERLMAIGARHYGNIRATAQDWLEEVEIDPTRIDDLPRAFSGGMQQRLQIAR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 553371603 157 ALALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDTLDKV 231
Cdd:TIGR02323 162 NLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQV 236
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
23-226 |
2.65e-25 |
|
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: 99.59 E-value: 2.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 23 QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSgqsRAMVERRFGVLFQRGALFSSlTVTE 102
Cdd:cd03245 21 DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD---PADLRRNIGYVPQDVTLFYG-TLRD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 103 NVALplienaGLPRSEAERLAQVkLALAGLPPGTGsKYP-----------ASLSGGMVKRVALARALALDPDILFLDEPT 171
Cdd:cd03245 97 NITL------GAPLADDERILRA-AELAGVTDFVN-KHPngldlqigergRGLSGGQRQAVALARALLNDPPILLLDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 553371603 172 AGLDPIGAAAF-DSLIRTLRDAlnlTVFLVTHDLDTLyTLCDRVAVLSQKKvLVVD 226
Cdd:cd03245 169 SAMDMNSEERLkERLRQLLGDK---TLIIITHRPSLL-DLVDRIIVMDSGR-IVAD 219
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
26-226 |
3.16e-25 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 99.66 E-value: 3.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 26 NLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAMverrfGVLFQRGALFSSLTVTENVA 105
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPV-----SMLFQENNLFSHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 106 LPLieNAGLPRSEAERLAQVKLA-LAGLPPGTgSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAAAFDS 184
Cdd:PRK10771 94 LGL--NPGLKLNAAQREKLHAIArQMGIEDLL-ARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLT 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 553371603 185 LIRTLRDALNLTVFLVTHDLDTlytlcdrVAVLSQKKVLVVD 226
Cdd:PRK10771 171 LVSQVCQERQLTLLMVSHSLED-------AARIAPRSLVVAD 205
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
6-236 |
4.29e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 100.26 E-value: 4.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 6 IIQIRDLVNCF-GVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKdlmALSGQSRAMVERR 84
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGE---PITKENIREVRKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 85 FGVLFQR--GALFSSlTVTENVALPLIeNAGLPRSEAERLAQVKLALAGLPPgTGSKYPASLSGGMVKRVALARALALDP 162
Cdd:PRK13652 80 VGLVFQNpdDQIFSP-TVEQDIAFGPI-NLGLDEETVAHRVSSALHMLGLEE-LRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 553371603 163 DILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDTLDKVAATDD 236
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPD 230
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
5-217 |
4.61e-25 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 102.03 E-value: 4.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 5 AIIQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVfGKDLMalsgQSRAMVERR 84
Cdd:PRK11000 2 ASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFI-GEKRM----NDVPPAERG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 85 FGVLFQRGALFSSLTVTENVALPLiENAGLPRSEAE-RLAQVK--LALAGLPpgtgSKYPASLSGGMVKRVALARALALD 161
Cdd:PRK11000 77 VGMVFQSYALYPHLSVAENMSFGL-KLAGAKKEEINqRVNQVAevLQLAHLL----DRKPKALSGGQRQRVAIGRTLVAE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 553371603 162 PDILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVL 217
Cdd:PRK11000 152 PSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVL 207
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
25-222 |
7.12e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 99.78 E-value: 7.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 25 LNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVfgKDLMALSGQSRAMVERRFGVLFQR--GALFSSLtVTE 102
Cdd:PRK13633 29 VNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYV--DGLDTSDEENLWDIRNKAGMVFQNpdNQIVATI-VEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 103 NVAL-PliENAGLPRSEAERLAQVKLALAGLppgtgSKY----PASLSGGMVKRVALARALALDPDILFLDEPTAGLDPI 177
Cdd:PRK13633 106 DVAFgP--ENLGIPPEEIRERVDESLKKVGM-----YEYrrhaPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPS 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 553371603 178 GAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTlCDRVAVLSQKKV 222
Cdd:PRK13633 179 GRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKV 222
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
25-246 |
1.03e-24 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 102.63 E-value: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 25 LNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFG-------KDLMALSGQSRAMVERRFG----VLFQR-- 91
Cdd:PRK10261 35 LSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsRQVIELSEQSAAQMRHVRGadmaMIFQEpm 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 92 GALFSSLTVTENVALPLIENAGLPRSEAERLAQVKLALAGLPPGTG--SKYPASLSGGMVKRVALARALALDPDILFLDE 169
Cdd:PRK10261 115 TSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTilSRYPHQLSGGMRQRVMIAMALSCRPAVLIADE 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 553371603 170 PTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKvlvvdtldkvaATDDGWIQAYFHGP 246
Cdd:PRK10261 195 PTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGE-----------AVETGSVEQIFHAP 260
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-217 |
2.23e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 98.20 E-value: 2.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 19 QCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLR------SIVGLRRPTDGKIHVFGKDLMALSGqsrAMVERRFGVLFQRG 92
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKvlnrliEIYDSKIKVDGKVLYFGKDIFQIDA---IKLRKEVGMVFQQP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 93 ALFSSLTVTENVALPLIENAGLPRSEAERLAQVKLALAGLPPGTGSKY--PAS-LSGGMVKRVALARALALDPDILFLDE 169
Cdd:PRK14246 100 NPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLnsPASqLSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 553371603 170 PTAGLDPIGAAAFDSLIRTLRDalNLTVFLVTHDLDTLYTLCDRVAVL 217
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLITELKN--EIAIVIVSHNPQQVARVADYVAFL 225
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-215 |
2.40e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 98.19 E-value: 2.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 7 IQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRR-----PTDGKIHVFGKDLMalsgQSRAMV 81
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIY----ERRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 82 ---ERRFGVLFQRGALFSsLTVTENVALPLIENAGLPRSEAERLAQVKLALAGLPPGTGSKYPAS---LSGGMVKRVALA 155
Cdd:PRK14258 84 nrlRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIKHKIHKSaldLSGGQQQRLCIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 156 RALALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVA 215
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTA 222
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-233 |
7.85e-24 |
|
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: 99.88 E-value: 7.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 7 IQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLR--RPTDGKI--HV----------------- 65
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIiyHValcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 66 -----------FGKDLMALSGQSRAMVERRFGVLFQRG-ALFSSLTVTENVaLPLIENAGLPRSEA-----ERLAQVKLA 128
Cdd:TIGR03269 81 pcpvcggtlepEEVDFWNLSDKLRRRIRKRIAIMLQRTfALYGDDTVLDNV-LEALEEIGYEGKEAvgravDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 129 -----LAglppgtgskypASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHD 203
Cdd:TIGR03269 160 hrithIA-----------RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHW 228
|
250 260 270
....*....|....*....|....*....|
gi 553371603 204 LDTLYTLCDRVAVLSQKKVLVVDTLDKVAA 233
Cdd:TIGR03269 229 PEVIEDLSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
34-217 |
1.15e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 96.70 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 34 VLGVVGGSGTGKSVLLRSIVGLRRPTDGkiHVFGKDLMaLSGQS----RAMVE--RRFGVLFQRGALFSsLTVTENVALP 107
Cdd:PRK14271 49 VTSLMGPTGSGKTTFLRTLNRMNDKVSG--YRYSGDVL-LGGRSifnyRDVLEfrRRVGMLFQRPNPFP-MSIMDNVLAG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 108 LIENAGLPRSEAERLAQVKLALAGLPPGTG---SKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAAAFDS 184
Cdd:PRK14271 125 VRAHKLVPRKEFRGVAQARLTEVGLWDAVKdrlSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEE 204
|
170 180 190
....*....|....*....|....*....|...
gi 553371603 185 LIRTLRDalNLTVFLVTHDLDTLYTLCDRVAVL 217
Cdd:PRK14271 205 FIRSLAD--RLTVIIVTHNLAQAARISDRAALF 235
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
25-231 |
1.29e-23 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 97.64 E-value: 1.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 25 LNLDVK-----RGeVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLM-ALSGQSRAMVERRFGVLFQRGALFSSL 98
Cdd:PRK11144 13 LCLTVNltlpaQG-ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFdAEKGICLPPEKRRIGYVFQDARLFPHY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 99 TVTENValplieNAGLPRSEAERLAQVkLALAGLPPGTgSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDpig 178
Cdd:PRK11144 92 KVRGNL------RYGMAKSMVAQFDKI-VALLGIEPLL-DRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD--- 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 553371603 179 aaafdsLIR---------TLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDTLDKV 231
Cdd:PRK11144 161 ------LPRkrellpyleRLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
7-237 |
1.70e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 97.99 E-value: 1.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 7 IQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSramVERRFG 86
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARA---ASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 87 VLFQRGAL---FSSLTVTENVALPLIENAGlPRSEAERLAqVKLALAGLPPGTGSKYP-ASLSGGMVKRVALARALALDP 162
Cdd:PRK09536 81 SVPQDTSLsfeFDVRQVVEMGRTPHRSRFD-TWTETDRAA-VERAMERTGVAQFADRPvTSLSGGERQRVLLARALAQAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 163 DILFLDEPTAGLDPIGAAAFDSLIRTLRDAlNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLV------VDTLDKVAATDD 236
Cdd:PRK09536 159 PVLLLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAagppadVLTADTLRAAFD 237
|
.
gi 553371603 237 G 237
Cdd:PRK09536 238 A 238
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-235 |
2.11e-23 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 94.96 E-value: 2.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 5 AIIQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAMveRR 84
Cdd:PRK10895 2 ATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARAR--RG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 85 FGVLFQRGALFSSLTVTENVALPLIENAGLPRSEAERLAQVKLA---LAGLPPGTGSkypaSLSGGMVKRVALARALALD 161
Cdd:PRK10895 80 IGYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEefhIEHLRDSMGQ----SLSGGERRRVEIARALAAN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 553371603 162 PDILFLDEPTAGLDPIGAAAFDSLIRTLRDAlNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDTLDKVAATD 235
Cdd:PRK10895 156 PKFILLDEPFAGVDPISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDE 228
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
29-222 |
2.92e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 95.20 E-value: 2.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 29 VKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGkiHVFGKDLmALSGQSRAMVERRFGVLFQRGA-LFSSLTVTENVALP 107
Cdd:PRK13648 32 IPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSG--EIFYNNQ-AITDDNFEKLRKHIGIVFQNPDnQFVGSIVKYDVAFG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 108 LiENAGLPRSEAERLAQVKLALAGLPPGTGSKyPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAAAFDSLIR 187
Cdd:PRK13648 109 L-ENHAVPYDEMHRRVSEALKQVDMLERADYE-PNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVR 186
|
170 180 190
....*....|....*....|....*....|....*
gi 553371603 188 TLRDALNLTVFLVTHDLDTLYTlCDRVAVLSQKKV 222
Cdd:PRK13648 187 KVKSEHNITIISITHDLSEAME-ADHVIVMNKGTV 220
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
23-223 |
4.40e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 95.92 E-value: 4.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 23 QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLmalSGQSRAMVeRRFGVLF-QRGALFSSLTVT 101
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVP---FKRRKEFA-RRIGVVFgQRSQLWWDLPAI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 102 ENVALplieNA---GLPRSE-AERLAQVK--LALAGLppgtgSKYPA-SLSGGMVKRVALARALALDPDILFLDEPTAGL 174
Cdd:COG4586 115 DSFRL----LKaiyRIPDAEyKKRLDELVelLDLGEL-----LDTPVrQLSLGQRMRCELAAALLHRPKILFLDEPTIGL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 553371603 175 DPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKVL 223
Cdd:COG4586 186 DVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRII 234
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
4-220 |
1.33e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 93.31 E-value: 1.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 4 DAIIQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRS-------IVGLRrpTDGKIHVFGKDLMAlSGQ 76
Cdd:PRK14243 8 ETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrlndlIPGFR--VEGKVTFHGKNLYA-PDV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 77 SRAMVERRFGVLFQRGALFSSlTVTENVAL------------PLIENAgLPRSEAERLAQVKLALAGLppgtgskypaSL 144
Cdd:PRK14243 85 DPVEVRRRIGMVFQKPNPFPK-SIYDNIAYgaringykgdmdELVERS-LRQAALWDEVKDKLKQSGL----------SL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 553371603 145 SGGMVKRVALARALALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDalNLTVFLVTHDLDTLYTLCDRVAVLSQK 220
Cdd:PRK14243 153 SGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKE--QYTIIIVTHNMQQAARVSDMTAFFNVE 226
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
7-222 |
1.73e-22 |
|
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: 90.84 E-value: 1.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 7 IQIRDLVNCFGVQCVH--QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQsramVERR 84
Cdd:cd03247 1 LSINNVSFSYPEQEQQvlKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA----LSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 85 FGVLFQRGALFSSlTVTENVALPLienaglprseaerlaqvklalaglppgtgskypaslSGGMVKRVALARALALDPDI 164
Cdd:cd03247 77 ISVLNQRPYLFDT-TLRNNLGRRF------------------------------------SGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 553371603 165 LFLDEPTAGLDPIGAaafDSLIRTLRDAL-NLTVFLVTHDLDTLYTLcDRVAVLSQKKV 222
Cdd:cd03247 120 VLLDEPTVGLDPITE---RQLLSLIFEVLkDKTLIWITHHLTGIEHM-DKILFLENGKI 174
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
23-222 |
1.73e-22 |
|
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: 92.21 E-value: 1.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 23 QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVfgkdlmalSGQSRAMVErrFGVLFQrgalfSSLTVTE 102
Cdd:cd03220 39 KDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV--------RGRVSSLLG--LGGGFN-----PELTGRE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 103 NVALPLIENaGLPRSEAERLAQVKLALAGL------PPGTgskypasLSGGMVKRVALARALALDPDILFLDEPTAgldp 176
Cdd:cd03220 104 NIYLNGRLL-GLSRKEIDEKIDEIIEFSELgdfidlPVKT-------YSSGMKARLAFAIATALEPDILLIDEVLA---- 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 553371603 177 IGAAAF--------DSLIRTLRdalnlTVFLVTHDLDTLYTLCDRVAVLSQKKV 222
Cdd:cd03220 172 VGDAAFqekcqrrlRELLKQGK-----TVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
16-205 |
2.81e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 90.76 E-value: 2.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 16 FGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALsgqsramverrfgvLFQRGALF 95
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAY--------------VPQRSEVP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 96 SSL--TVTENVALPLIENAGLPR--------SEAERLAQVKLA-LAGLPPGTgskypasLSGGMVKRVALARALALDPDI 164
Cdd:NF040873 68 DSLplTVRDLVAMGRWARRGLWRrltrddraAVDDALERVGLAdLAGRQLGE-------LSGGQRQRALLAQGLAQEADL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 553371603 165 LFLDEPTAGLDPIGAAAFDSLIRTLRDAlNLTVFLVTHDLD 205
Cdd:NF040873 141 LLLDEPTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLE 180
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
16-222 |
3.36e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.13 E-value: 3.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 16 FGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVfGKDLmalsgqsramverRFGVLFQRGALF 95
Cdd:COG0488 8 FGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI-PKGL-------------RIGYLPQEPPLD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 96 SSLTVTENV--ALP-----------LIENAGLPRSEAERLA----------------QVKLALAGL--PPGTGSKYPASL 144
Cdd:COG0488 74 DDLTVLDTVldGDAelraleaeleeLEAKLAEPDEDLERLAelqeefealggweaeaRAEEILSGLgfPEEDLDRPVSEL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 145 SGGMVKRVALARALALDPDILFLDEPTAGLDpigaaaFDSlIRTLRDALN---LTVFLVTHDLDTLYTLCDRVAVLSQKK 221
Cdd:COG0488 154 SGGWRRRVALARALLSEPDLLLLDEPTNHLD------LES-IEWLEEFLKnypGTVLVVSHDRYFLDRVATRILELDRGK 226
|
.
gi 553371603 222 V 222
Cdd:COG0488 227 L 227
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
23-223 |
7.31e-22 |
|
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: 90.75 E-value: 7.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 23 QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALsgqSRAMVERRFGVLFQRGALFSSlTVTE 102
Cdd:cd03254 20 KDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDI---SRKSLRSMIGVVLQDTFLFSG-TIME 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 103 NVALplienaGLPRSEAERLAQVKLALAG------LP------PGTGSKYpasLSGGMVKRVALARALALDPDILFLDEP 170
Cdd:cd03254 96 NIRL------GRPNATDEEVIEAAKEAGAhdfimkLPngydtvLGENGGN---LSQGERQLLAIARAMLRDPKILILDEA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 553371603 171 TAGLDPIGAAAFDSLIRTLRDalNLTVFLVTHDLDTLYTlCDRVAVLSQKKVL 223
Cdd:cd03254 167 TSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKII 216
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
26-223 |
9.37e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 91.61 E-value: 9.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 26 NLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAM--VERRFGVLFQ--RGALFSSlTVT 101
Cdd:PRK13645 31 SLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEVkrLRKEIGLVFQfpEYQLFQE-TIE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 102 ENVALPLIeNAGLPRSEAERLAQVKLALAGLPPGTGSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAAA 181
Cdd:PRK13645 110 KDIAFGPV-NLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEED 188
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 553371603 182 FDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKVL 223
Cdd:PRK13645 189 FINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVI 230
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
23-204 |
2.55e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 89.76 E-value: 2.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 23 QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAmveRRFGVLFQ---RGAlFSSLT 99
Cdd:COG1101 23 DGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRA---KYIGRVFQdpmMGT-APSMT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 100 VTENVALPLIENA------GLPRSE----AERLAQVKLAL-------AGLppgtgskypasLSGGmvKRVALARALAL-- 160
Cdd:COG1101 99 IEENLALAYRRGKrrglrrGLTKKRrelfRELLATLGLGLenrldtkVGL-----------LSGG--QRQALSLLMATlt 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 553371603 161 DPDILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDL 204
Cdd:COG1101 166 KPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNM 209
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-215 |
3.86e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 89.06 E-value: 3.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 1 MTQdAIIQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSI--VGLRRP---TDGKIHVFGKDLMALSG 75
Cdd:PRK14239 1 MTE-PILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGHNIYSPRT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 76 QSramVERR--FGVLFQRGALFSsLTVTENVALPLIENAGLPRSEAERLAQVKLALAGLPPGTGSKYPAS---LSGGMVK 150
Cdd:PRK14239 80 DT---VDLRkeIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVKDRLHDSalgLSGGQQQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 553371603 151 RVALARALALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDalNLTVFLVTHDLDTLYTLCDRVA 215
Cdd:PRK14239 156 RVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKD--DYTMLLVTRSMQQASRISDRTG 218
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
6-231 |
3.98e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 89.30 E-value: 3.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 6 IIQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAmveRRF 85
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA---RRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 86 GVLFQRGALFSSLTVTENVAL---PLIENAGLPRSEAERLAQVKLALAGLPPgTGSKYPASLSGGMVKRVALARALALDP 162
Cdd:PRK11231 79 ALLPQHHLTPEGITVRELVAYgrsPWLSLWGRLSAEDNARVNQAMEQTRINH-LADRRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 553371603 163 DILFLDEPTAGLDPIGAAAFDSLIRTLRDAlNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDTLDKV 231
Cdd:PRK11231 158 PVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
23-223 |
4.70e-21 |
|
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: 87.61 E-value: 4.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 23 QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRP--TDGKIHVFGKDLMALSGQSR-AMVErrfgvlfQRGALFSSLT 99
Cdd:cd03213 26 KNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDKRSFRKIiGYVP-------QDDILHPTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 100 VTENVALPlienaglprseaerlAQVKlalaglppgtgskypaSLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGA 179
Cdd:cd03213 99 VRETLMFA---------------AKLR----------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 553371603 180 AAFDSLIRTLRDaLNLTVFLVTHDL-DTLYTLCDRVAVLSQKKVL 223
Cdd:cd03213 148 LQVMSLLRRLAD-TGRTIICSIHQPsSEIFELFDKLLLLSQGRVI 191
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
21-223 |
4.93e-21 |
|
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: 88.75 E-value: 4.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 21 VHQGLNLDVKRGEVLGVVGGSGTGKSvllrSIVGL-RR---PTDGKIHVFGKDLMALSGQSramVERRFGVLFQRGALFS 96
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKS----TVVSLlERfydPTSGEILLDGVDIRDLNLRW---LRSQIGLVSQEPVLFD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 97 SlTVTENVALplienaGLP-RSEAERLAQVKLALA-----GLPPG----TGSKYpASLSGGMVKRVALARALALDPDILF 166
Cdd:cd03249 91 G-TIAENIRY------GKPdATDEEVEEAAKKANIhdfimSLPDGydtlVGERG-SQLSGGQKQRIAIARALLRNPKILL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 553371603 167 LDEPTAGLDP----IGAAAFDSLIRtlrdalNLTVFLVTHDLDTLYTlCDRVAVLSQKKVL 223
Cdd:cd03249 163 LDEATSALDAesekLVQEALDRAMK------GRTTIVIAHRLSTIRN-ADLIAVLQNGQVV 216
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
26-217 |
9.16e-21 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 89.58 E-value: 9.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 26 NLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRP----TDGKIHVFGKDLMALSG-QSRAMVERRFGVLFQRGAlfSSLTV 100
Cdd:COG4170 27 SLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPrERRKIIGREIAMIFQEPS--SCLDP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 101 TENVALPLIENagLPRSEAE-----RLAQVKLALAGLPPGTGSK--------YPASLSGGMVKRVALARALALDPDILFL 167
Cdd:COG4170 105 SAKIGDQLIEA--IPSWTFKgkwwqRFKWRKKRAIELLHRVGIKdhkdimnsYPHELTEGECQKVMIAMAIANQPRLLIA 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 553371603 168 DEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVL 217
Cdd:COG4170 183 DEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVL 232
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-218 |
1.17e-20 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 87.46 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 1 MTQDAIIQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQS-RA 79
Cdd:PRK10247 2 QENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyRQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 80 MVErrfgVLFQRGALFSSlTVTENVALP-LIENAglpRSEAERLAQvKLALAGLPPGTGSKYPASLSGGMVKRVALARAL 158
Cdd:PRK10247 82 QVS----YCAQTPTLFGD-TVYDNLIFPwQIRNQ---QPDPAIFLD-DLERFALPDTILTKNIAELSGGEKQRISLIRNL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 159 ALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLyTLCDRVAVLS 218
Cdd:PRK10247 153 QFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEI-NHADKVITLQ 211
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
25-223 |
1.59e-20 |
|
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: 87.29 E-value: 1.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 25 LNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSramVERRFGVLFQRGALFSSlTVTENV 104
Cdd:cd03251 21 ISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLAS---LRRQIGLVSQDVFLFND-TVAENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 105 AlplIENAGLPRSEAERLAQVKLA---LAGLPPG-------TGSKypasLSGGMVKRVALARALALDPDILFLDEPTAGL 174
Cdd:cd03251 97 A---YGRPGATREEVEEAARAANAhefIMELPEGydtvigeRGVK----LSGGQRQRIAIARALLKDPPILILDEATSAL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 553371603 175 DPIGAAAFDSLIRTLrdALNLTVFLVTHDLDTLyTLCDRVAVLSQKKVL 223
Cdd:cd03251 170 DTESERLVQAALERL--MKNRTTFVIAHRLSTI-ENADRIVVLEDGKIV 215
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
6-223 |
1.63e-20 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 87.76 E-value: 1.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 6 IIQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGL---RRPTDGKIHVFGKDLMALSGQSRAMVE 82
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRLARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 83 RR--FGVLFQRGALFSSLTVTENVALPLIENAGLPRS-------EAERLAQVKLALAGLPPGTGSKYpASLSGGMVKRVA 153
Cdd:PRK09984 84 SRanTGYIFQQFNLVNRLSVLENVLIGALGSTPFWRTcfswftrEQKQRALQALTRVGMVHFAHQRV-STLSGGQQQRVA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 154 LARALALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKVL 223
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVF 232
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-205 |
2.07e-20 |
|
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: 87.06 E-value: 2.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 4 DAIIQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGK-IHVFGKDLMALSgqsraMVE 82
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGED-----VWE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 83 --RRFGVL-------FQRG---------ALFSSLTVTENVALPLIENAglprseAERLAQVKLA-LAGLPPGTgskypas 143
Cdd:COG1119 76 lrKRIGLVspalqlrFPRDetvldvvlsGFFDSIGLYREPTDEQRERA------RELLELLGLAhLADRPFGT------- 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 553371603 144 LSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLD 205
Cdd:COG1119 143 LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVE 204
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
21-223 |
2.52e-20 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 86.52 E-value: 2.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 21 VHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSramVERRFGVLFQRGALFSSlTV 100
Cdd:cd03253 16 VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDS---LRRAIGVVPQDTVLFND-TI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 101 TENVALplienaGLPRS------EAERLAQVKLALAGLPPG-------TGSKypasLSGGMVKRVALARALALDPDILFL 167
Cdd:cd03253 92 GYNIRY------GRPDAtdeeviEAAKAAQIHDKIMRFPDGydtivgeRGLK----LSGGEKQRVAIARAILKNPPILLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 553371603 168 DEPTAGLDPIGAAAfdsLIRTLRDAL-NLTVFLVTHDLDTLYTlCDRVAVLSQKKVL 223
Cdd:cd03253 162 DEATSALDTHTERE---IQAALRDVSkGRTTIVIAHRLSTIVN-ADKIIVLKDGRIV 214
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
21-223 |
2.82e-20 |
|
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: 86.01 E-value: 2.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 21 VHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALsgqSRAMVERRFGVLFQRGALFSSlTV 100
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKI---GLHDLRSRISIIPQDPVLFSG-TI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 101 TENVAlPLIEnaglpRSEAE-----RLAQVKLALAGLPPGTGSKY---PASLSGGMVKRVALARALALDPDILFLDEPTA 172
Cdd:cd03244 95 RSNLD-PFGE-----YSDEElwqalERVGLKEFVESLPGGLDTVVeegGENLSVGQRQLLCLARALLRKSKILVLDEATA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 553371603 173 GLDPIGaaafDSLI-RTLRDAL-NLTVFLVTHDLDTLYTlCDRVAVLSQKKVL 223
Cdd:cd03244 169 SVDPET----DALIqKTIREAFkDCTVLTIAHRLDTIID-SDRILVLDKGRVV 216
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
2-217 |
4.06e-20 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 87.86 E-value: 4.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 2 TQDAIIQIRDLVNCFG-----VQCVHqGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRP---TDGKIHVFGKDLMAL 73
Cdd:PRK09473 8 QADALLDVKDLRVTFStpdgdVTAVN-DLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 74 S-GQSRAMVERRFGVLFQ--RGALFSSLTVTENVALPLIENAGLPRSEA-----ERLAQVKLALAglppgtgSK----YP 141
Cdd:PRK09473 87 PeKELNKLRAEQISMIFQdpMTSLNPYMRVGEQLMEVLMLHKGMSKAEAfeesvRMLDAVKMPEA-------RKrmkmYP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 553371603 142 ASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVL 217
Cdd:PRK09473 160 HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVM 235
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
23-217 |
4.40e-20 |
|
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: 85.21 E-value: 4.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 23 QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKdlMALSGQSramverrfgvlfqrgALFSSLTVTE 102
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS--IAYVSQE---------------PWIQNGTIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 103 NVALplienaGLPRSEaERLAQV------KLALAGLPPG--T--GSKyPASLSGGMVKRVALARALALDPDILFLDEPTA 172
Cdd:cd03250 85 NILF------GKPFDE-ERYEKVikacalEPDLEILPDGdlTeiGEK-GINLSGGQKQRISLARAVYSDADIYLLDDPLS 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 553371603 173 GLDP-IGAAAFDSLIRTLRdALNLTVFLVTHDLDTLyTLCDRVAVL 217
Cdd:cd03250 157 AVDAhVGRHIFENCILGLL-LNNKTRILVTHQLQLL-PHADQIVVL 200
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-222 |
5.68e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 88.61 E-value: 5.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 1 MTQdAIIQIRDLVNCF----GVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRrPT------DGKIHVFGKDL 70
Cdd:PRK15134 1 MTQ-PLLAIENLSVAFrqqqTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSppvvypSGDIRFHGESL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 71 MALSGQS-RAMVERRFGVLFQRGalFSSLTVTENVALPLIENAGLPRS---EAERLAQVK-LALAGL--PPGTGSKYPAS 143
Cdd:PRK15134 79 LHASEQTlRGVRGNKIAMIFQEP--MVSLNPLHTLEKQLYEVLSLHRGmrrEAARGEILNcLDRVGIrqAAKRLTDYPHQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 553371603 144 LSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKV 222
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRC 235
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
29-217 |
8.45e-20 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 86.72 E-value: 8.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 29 VKRGEVLGVVGGSGTGKSVLLRSIVGL----RRPTDGKIHVFGKDLMALS-GQSRAMVERRFGVLFQRGalFSSLTVTEN 103
Cdd:PRK11022 30 VKQGEVVGIVGESGSGKSVSSLAIMGLidypGRVMAEKLEFNGQDLQRISeKERRNLVGAEVAMIFQDP--MTSLNPCYT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 104 VALPLIE-----NAGLPRSEAERLAQVkLALAGLPPGTG--SKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDP 176
Cdd:PRK11022 108 VGFQIMEaikvhQGGNKKTRRQRAIDL-LNQVGIPDPASrlDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDV 186
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 553371603 177 IGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVL 217
Cdd:PRK11022 187 TIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVM 227
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
7-251 |
1.35e-19 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 85.14 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 7 IQIRDLVNCFGVQCVHqGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRP----TDGKIHVFGKDLMA--LSGQSRAM 80
Cdd:PRK10418 5 IELRNIALQAAQPLVH-GVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPcaLRGRKIAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 81 VERRfgvlfQRGAlFSSLTVTENVALPLIENAGLPRSEAERLAqvKLALAGL--PPGTGSKYPASLSGGMVKRVALARAL 158
Cdd:PRK10418 84 IMQN-----PRSA-FNPLHTMHTHARETCLALGKPADDATLTA--ALEAVGLenAARVLKLYPFEMSGGMLQRMMIALAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 159 ALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKvlVVDTLDkvaatddgw 238
Cdd:PRK10418 156 LCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGR--IVEQGD--------- 224
|
250
....*....|...
gi 553371603 239 IQAYFHGPRGRAA 251
Cdd:PRK10418 225 VETLFNAPKHAVT 237
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
18-235 |
1.57e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 84.55 E-value: 1.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 18 VQCVHQgLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMalSGQSRAMVERRFGVLFQRGALFSS 97
Cdd:PRK11614 18 IQALHE-VSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDIT--DWQTAKIMREAVAIVPEGRRVFSR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 98 LTVTENVALplienaGLPRSEAERLAQVKLALAGLPP---GTGSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGL 174
Cdd:PRK11614 95 MTVEENLAM------GGFFAERDQFQERIKWVYELFPrlhERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 553371603 175 DPIGAAAFDSLIRTLRDAlNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDTLDKVAATD 235
Cdd:PRK11614 169 APIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANE 228
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
4-217 |
2.27e-19 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 87.22 E-value: 2.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 4 DAIIQIRDLVNCFGVQC---------VH--QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMA 72
Cdd:PRK10261 311 EPILQVRNLVTRFPLRSgllnrvtreVHavEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDT 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 73 LSGQSRAMVERRFGVLFQR--GALFSSLTVTENVALPLIENAGLPRSEAERLAQVKLALAGLPPGTGSKYPASLSGGMVK 150
Cdd:PRK10261 391 LSPGKLQALRRDIQFIFQDpyASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQ 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 553371603 151 RVALARALALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVL 217
Cdd:PRK10261 471 RICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVM 537
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
20-202 |
2.69e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.38 E-value: 2.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 20 CVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDlmalsgQSRAMVERRFGVLFQRGALFSSLT 99
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD------IDDPDVAEACHYLGHRNAMKPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 100 VTENVALPLIENAGLPRSEAERLAQVKLA-LAGLPPGTgskypasLSGGMVKRVALARALALDPDILFLDEPTAGLDPIG 178
Cdd:PRK13539 90 VAENLEFWAAFLGGEELDIAAALEAVGLApLAHLPFGY-------LSAGQKRRVALARLLVSNRPIWILDEPTAALDAAA 162
|
170 180
....*....|....*....|....
gi 553371603 179 AAAFDSLIRTlRDALNLTVFLVTH 202
Cdd:PRK13539 163 VALFAELIRA-HLAQGGIVIAATH 185
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
9-222 |
1.49e-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: 85.07 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 9 IRDLVNCF---GVQCVHQgLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMAlsgqSRAMVERRF 85
Cdd:TIGR01257 931 VKNLVKIFepsGRPAVDR-LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET----NLDAVRQSL 1005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 86 GVLFQRGALFSSLTVTENVaLPLIENAGLPRSEAERLAQVKLALAGLPPGTGSKyPASLSGGMVKRVALARALALDPDIL 165
Cdd:TIGR01257 1006 GMCPQHNILFHHLTVAEHI-LFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEE-AQDLSGGMQRKLSVAIAFVGDAKVV 1083
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 553371603 166 FLDEPTAGLDPIGAAAFDSLIRTLRDAlnLTVFLVTHDLDTLYTLCDRVAVLSQKKV 222
Cdd:TIGR01257 1084 VLDEPTSGVDPYSRRSIWDLLLKYRSG--RTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
7-223 |
2.39e-18 |
|
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: 80.65 E-value: 2.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 7 IQIRDL-VNCFGVQCVHqGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLR--RPTDGKIHVFGKDLMALSGQSRAmver 83
Cdd:cd03217 1 LEIKDLhVSVGGKEILK-GVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERA---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 84 RFGV--LFQrgalfssltvtENVALPLIENAGLPRSEAErlaqvklalaglppgtgskypaSLSGGMVKRVALARALALD 161
Cdd:cd03217 76 RLGIflAFQ-----------YPPEIPGVKNADFLRYVNE----------------------GFSGGEKKRNEILQLLLLE 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 553371603 162 PDILFLDEPTAGLDPIGAAAFDSLIRTLRDAlNLTVFLVTHDLDTL-YTLCDRVAVLSQKKVL 223
Cdd:cd03217 123 PDLAILDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITHYQRLLdYIKPDRVHVLYDGRIV 184
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-222 |
3.10e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 83.58 E-value: 3.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 6 IIQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVfGKDLmalsgqsramverRF 85
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV-------------KI 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 86 GVLFQ-RGALFSSLTVTENVALpliENAGLPRSEAERLaqvkLALAGLPPGTGSKYPASLSGGMVKRVALARALALDPDI 164
Cdd:COG0488 381 GYFDQhQEELDPDKTVLDELRD---GAPGGTEQEVRGY----LGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNV 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 553371603 165 LFLDEPTAGLDPigaaafDSLiRTLRDALNL---TVFLVTHDLDTLYTLCDRVAVLSQKKV 222
Cdd:COG0488 454 LLLDEPTNHLDI------ETL-EALEEALDDfpgTVLLVSHDRYFLDRVATRILEFEDGGV 507
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
16-219 |
3.66e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 81.31 E-value: 3.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 16 FGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIhvfgkdlmalsgqsRAMVERRFGVLFQRGALF 95
Cdd:PRK09544 14 FGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI--------------KRNGKLRIGYVPQKLYLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 96 SSLTVTENVALPLIENA-------GLPRSEAERLAQVKLAlaglppgtgskypaSLSGGMVKRVALARALALDPDILFLD 168
Cdd:PRK09544 80 TTLPLTVNRFLRLRPGTkkedilpALKRVQAGHLIDAPMQ--------------KLSGGETQRVLLARALLNRPQLLVLD 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 553371603 169 EPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQ 219
Cdd:PRK09544 146 EPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
7-221 |
4.47e-18 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 78.26 E-value: 4.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 7 IQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVfgkdlmalsgqsramverrfg 86
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 87 vlfqrgalfssltvtenvalplienaglprseaerlaqvklalaglPPGTGSKYPASLSGGMVKRVALARALALDPDILF 166
Cdd:cd03221 60 ----------------------------------------------GSTVKIGYFEQLSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 553371603 167 LDEPTAGLDPIGAAAfdsLIRTLRDaLNLTVFLVTHDLDTLYTLCDRVAVLSQKK 221
Cdd:cd03221 94 LDEPTNHLDLESIEA---LEEALKE-YPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
21-222 |
5.16e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 83.23 E-value: 5.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 21 VHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSramVERRFGVLFQRGALFSSlTV 100
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHY---LHRQVALVGQEPVLFSG-SV 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 101 TENVALplienaGLPRSE-AERLAQVKLALA-----GLPPG-------TGSKypasLSGGMVKRVALARALALDPDILFL 167
Cdd:TIGR00958 572 RENIAY------GLTDTPdEEIMAAAKAANAhdfimEFPNGydtevgeKGSQ----LSGGQKQRIAIARALVRKPRVLIL 641
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 553371603 168 DEPTAGLDpigaAAFDSLIRTLRDALNLTVFLVTHDLDTLYTlCDRVAVLSQKKV 222
Cdd:TIGR00958 642 DEATSALD----AECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSV 691
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
17-235 |
6.00e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 82.65 E-value: 6.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 17 GVQCVhQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSgqSRAMVERRFGVLFQRGALFS 96
Cdd:PRK11288 16 GVKAL-DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAS--TTAALAAGVAIIYQELHLVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 97 SLTVTENVALPLIENAG--LPRSEAERLAQVKLALAG--LPPGTGSKYpasLSGGMVKRVALARALALDPDILFLDEPTA 172
Cdd:PRK11288 93 EMTVAENLYLGQLPHKGgiVNRRLLNYEAREQLEHLGvdIDPDTPLKY---LSIGQRQMVEIAKALARNARVIAFDEPTS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 553371603 173 GLDPIGAAAFDSLIRTLRDAlNLTVFLVTHDLDTLYTLCDRVAVLSQKKvlVVDTLDKVAATD 235
Cdd:PRK11288 170 SLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGR--YVATFDDMAQVD 229
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
23-219 |
6.10e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 82.91 E-value: 6.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 23 QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDL------------MALSGQSRamveRRFGvlfq 90
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIsprspldavkkgMAYITESR----RDNG---- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 91 rgaLFSSLTVTENVAL-PLIENAGLP-------RSEAERLAQVKLALAGLPPGTGSKYPASLSGGMVKRVALARALALDP 162
Cdd:PRK09700 352 ---FFPNFSIAQNMAIsRSLKDGGYKgamglfhEVDEQRTAENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCP 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 553371603 163 DILFLDEPTAGLDpIGAAA-FDSLIRTLRDAlNLTVFLVTHDLDTLYTLCDRVAVLSQ 219
Cdd:PRK09700 429 EVIIFDEPTRGID-VGAKAeIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCE 484
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
24-222 |
8.14e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 80.11 E-value: 8.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 24 GLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLR--RPTDGKIHVFGKDLMALSGQSRAmverRFGVL--FQRGALFSSLT 99
Cdd:COG0396 18 GVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDERA----RAGIFlaFQYPVEIPGVS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 100 VTE--NVALPLIENAGLPRSEAERLAQVKLALAGLPPGTGSKY-PASLSGGMVKRVALARALALDPDILFLDEPTAGLDp 176
Cdd:COG0396 94 VSNflRTALNARRGEELSAREFLKLLKEKMKELGLDEDFLDRYvNEGFSGGEKKRNEILQMLLLEPKLAILDETDSGLD- 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 553371603 177 IgaaafDSL------IRTLRDAlNLTVFLVTHD---LDtlYTLCDRVAVLSQKKV 222
Cdd:COG0396 173 I-----DALrivaegVNKLRSP-DRGILIITHYqriLD--YIKPDFVHVLVDGRI 219
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-241 |
9.49e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 82.41 E-value: 9.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 1 MTQDAIIQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALS-GQSRA 79
Cdd:PRK15439 6 TTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpAKAHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 80 MverrfGVLF--QRGALFSSLTVTENVALplienaGLPRSEA--ERLAQvKLALAG--LPPGTGSkypASLSGGMVKRVA 153
Cdd:PRK15439 86 L-----GIYLvpQEPLLFPNLSVKENILF------GLPKRQAsmQKMKQ-LLAALGcqLDLDSSA---GSLEVADRQIVE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 154 LARALALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDaLNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDTLDKVaa 233
Cdd:PRK15439 151 ILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLA-QGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL-- 227
|
....*...
gi 553371603 234 TDDGWIQA 241
Cdd:PRK15439 228 STDDIIQA 235
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
27-222 |
1.28e-17 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 79.12 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 27 LDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVfgkdlmalSGQSRAMVERRFGVLFQRG--ALFSSLTVTENV 104
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKV--------AGASPGKGWRHIGYVPQRHefAWDFPISVAHTV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 105 ALPLIENAGLPR--------SEAERLAQVKLA-LAGLPPGtgskypaSLSGGMVKRVALARALALDPDILFLDEPTAGLD 175
Cdd:TIGR03771 73 MSGRTGHIGWLRrpcvadfaAVRDALRRVGLTeLADRPVG-------ELSGGQRQRVLVARALATRPSVLLLDEPFTGLD 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 553371603 176 PIGAAAFDSLIRTLRDALNlTVFLVTHDLDTLYTLCDRVAVLSQKKV 222
Cdd:TIGR03771 146 MPTQELLTELFIELAGAGT-AILMTTHDLAQAMATCDRVVLLNGRVI 191
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
25-223 |
1.41e-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: 82.09 E-value: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 25 LNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSgqsRAMVERRFGVLFQRGALFSSlTVTENV 104
Cdd:TIGR01193 493 ISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDID---RHTLRQFINYLPQEPYIFSG-SILENL 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 105 ALPLIENAGLPR-SEAERLAQVKLALAGLPPGTG---SKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAA 180
Cdd:TIGR01193 569 LLGAKENVSQDEiWAACEIAEIKDDIENMPLGYQtelSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEK 648
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 553371603 181 afdsliRTLRDALNL---TVFLVTHDLdTLYTLCDRVAVLSQKKVL 223
Cdd:TIGR01193 649 ------KIVNNLLNLqdkTIIFVAHRL-SVAKQSDKIIVLDHGKII 687
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
25-231 |
3.89e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 78.05 E-value: 3.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 25 LNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLrRPTDGKIHVFGKDLMALSGQSRAmveRRFGVLFQRGALFSSLTVTENV 104
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELA---RHRAYLSQQQTPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 105 AL--PLIENAGLPRSEAERLAQvKLALaglppgtGSKYPAS---LSGGMVKRVALARA-LALDPDI------LFLDEPTA 172
Cdd:PRK03695 91 TLhqPDKTRTEAVASALNEVAE-ALGL-------DDKLGRSvnqLSGGEWQRVRLAAVvLQVWPDInpagqlLLLDEPMN 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 553371603 173 GLDPIGAAAFDSLIRTLRdALNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDTLDKV 231
Cdd:PRK03695 163 SLDVAQQAALDRLLSELC-QQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
7-222 |
1.04e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 79.10 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 7 IQIRDLvnCFGV----QCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQS-RAMV 81
Cdd:PRK11160 339 LTLNNV--SFTYpdqpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAlRQAI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 82 errfGVLFQRGALFSSlTVTENVALplienaGLPRSEAERLAQV-------KLaLAGLPP-----GTGSKypaSLSGGMV 149
Cdd:PRK11160 417 ----SVVSQRVHLFSA-TLRDNLLL------AAPNASDEALIEVlqqvgleKL-LEDDKGlnawlGEGGR---QLSGGEQ 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 150 KRVALARALALDPDILFLDEPTAGLDPigaaafdsliRTLRDALNL--------TVFLVTHDLdTLYTLCDRVAVLSQKK 221
Cdd:PRK11160 482 RRLGIARALLHDAPLLLLDEPTEGLDA----------ETERQILELlaehaqnkTVLMITHRL-TGLEQFDRICVMDNGQ 550
|
.
gi 553371603 222 V 222
Cdd:PRK11160 551 I 551
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
25-217 |
1.78e-16 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 77.54 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 25 LNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLR----RPTDGKIHVFGKDLMALSG-QSRAMVERRFGVLFQRGAlfSSLT 99
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGVTkdnwRVTADRMRFDDIDLLRLSPrERRKLVGHNVSMIFQEPQ--SCLD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 100 VTENVALPLIENagLP----------------RSEAERLAQVKLALaglPPGTGSKYPASLSGGMVKRVALARALALDPD 163
Cdd:PRK15093 104 PSERVGRQLMQN--IPgwtykgrwwqrfgwrkRRAIELLHRVGIKD---HKDAMRSFPYELTEGECQKVMIAIALANQPR 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 553371603 164 ILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVL 217
Cdd:PRK15093 179 LLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVL 232
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
26-227 |
2.22e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 78.63 E-value: 2.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 26 NLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRamveRRFGVLFQRGALFSSLTVTENVA 105
Cdd:NF033858 286 SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATR----RRVGYMSQAFSLYGELTVRQNLE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 106 LplieNA---GLPRSE-AERLAQVkLALAGLPPGTGSKyPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAAA 181
Cdd:NF033858 362 L----HArlfHLPAAEiAARVAEM-LERFDLADVADAL-PDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDM 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 553371603 182 F-DSLIRTLRDAlNLTVFLVTHDLDTLyTLCDRVAVLSQKKVLVVDT 227
Cdd:NF033858 436 FwRLLIELSRED-GVTIFISTHFMNEA-ERCDRISLMHAGRVLASDT 480
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
25-219 |
2.71e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 77.78 E-value: 2.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 25 LNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAmverRFGVLF-----QRGALFSSLT 99
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRL----ARGLVYlpedrQSSGLYLDAP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 100 VTENVALPLIENAGL---PRSEAERLAQ------VKLALAGLPPGTgskypasLSGGMVKRVALARALALDPDILFLDEP 170
Cdd:PRK15439 358 LAWNVCALTHNRRGFwikPARENAVLERyrralnIKFNHAEQAART-------LSGGNQQKVLIAKCLEASPQLLIVDEP 430
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 553371603 171 TAGLDPIGAAAFDSLIRTLRdALNLTVFLVTHDLDTLYTLCDRVAVLSQ 219
Cdd:PRK15439 431 TRGVDVSARNDIYQLIRSIA-AQNVAVLFISSDLEEIEQMADRVLVMHQ 478
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
7-217 |
5.39e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 77.13 E-value: 5.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 7 IQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAmvERRFG 86
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAA--QLGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 87 VLFQRGALFSSLTVTENV---ALPLIENAGLP---RSEAERLAQVKLALAGLPPGTGSKYpASLSGGMVKRVALARALAL 160
Cdd:PRK09700 84 IIYQELSVIDELTVLENLyigRHLTKKVCGVNiidWREMRVRAAMMLLRVGLKVDLDEKV-ANLSISHKQMLEIAKTLML 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 553371603 161 DPDILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFlVTHDLDTLYTLCDRVAVL 217
Cdd:PRK09700 163 DAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVY-ISHKLAEIRRICDRYTVM 218
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-190 |
6.40e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 77.09 E-value: 6.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 6 IIQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDlMAlSGQSRAMVERRF 85
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGD-MA-DARHRRAVCPRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 86 GVLFQrGA---LFSSLTVTENVA----LplienAGLPRSEAERLAQVKLALAGLPPGTGSkyPAS-LSGGMVKRVALARA 157
Cdd:NF033858 79 AYMPQ-GLgknLYPTLSVFENLDffgrL-----FGQDAAERRRRIDELLRATGLAPFADR--PAGkLSGGMKQKLGLCCA 150
|
170 180 190
....*....|....*....|....*....|...
gi 553371603 158 LALDPDILFLDEPTAGLDPIGAAAFDSLIRTLR 190
Cdd:NF033858 151 LIHDPDLLILDEPTTGVDPLSRRQFWELIDRIR 183
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
24-223 |
7.33e-16 |
|
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: 76.68 E-value: 7.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 24 GLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSramVERRFGVLFQRGALFSSlTVTEN 103
Cdd:TIGR02203 350 SISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLAS---LRRQVALVSQDVVLFND-TIANN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 104 VALPliENAGLPRSEAERLAQVKLALA---GLPPG----TGSKyPASLSGGMVKRVALARALALDPDILFLDEPTAGLDP 176
Cdd:TIGR02203 426 IAYG--RTEQADRAEIERALAAAYAQDfvdKLPLGldtpIGEN-GVLLSGGQRQRLAIARALLKDAPILILDEATSALDN 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 553371603 177 IG----AAAFDSLIRtlrdalNLTVFLVTHDLDTLYTlCDRVAVLSQKKVL 223
Cdd:TIGR02203 503 ESerlvQAALERLMQ------GRTTLVIAHRLSTIEK-ADRIVVMDDGRIV 546
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
21-222 |
8.74e-16 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 74.04 E-value: 8.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 21 VHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKdlmALSGQSRAMVERRFGVLFQRGALFSSlTV 100
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGK---PISQYEHKYLHSKVSLVGQEPVLFAR-SL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 101 TENVALPLIENAGLPRSEAERLAQVKLALAGLPPG----TGSKyPASLSGGMVKRVALARALALDPDILFLDEPTAGLDP 176
Cdd:cd03248 105 QDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGydteVGEK-GSQLSGGQKQRVAIARALIRNPQVLILDEATSALDA 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 553371603 177 IGAAAFDSLIRTlrDALNLTVFLVTHDLDTLYTlCDRVAVLSQKKV 222
Cdd:cd03248 184 ESEQQVQQALYD--WPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
3-222 |
9.00e-16 |
|
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: 73.60 E-value: 9.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 3 QDAIIQIRDLVNCFG--VQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDlmaLSGQSRAM 80
Cdd:cd03369 3 EHGEIEVENLSVRYApdLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGID---ISTIPLED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 81 VERRFGVLFQRGALFSSlTVTENVAlplIENAglpRSEAERLAQVKLALAGLppgtgskypaSLSGGMVKRVALARALAL 160
Cdd:cd03369 80 LRSSLTIIPQDPTLFSG-TIRSNLD---PFDE---YSDEEIYGALRVSEGGL----------NLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 553371603 161 DPDILFLDEPTAGLDPIGAAAFDSLIRTLRDalNLTVFLVTHDLDTLYTlCDRVAVLSQKKV 222
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFT--NSTILTIAHRLRTIID-YDKILVMDAGEV 201
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
23-218 |
9.51e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 76.38 E-value: 9.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 23 QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHV-FGKDLMALSgqsramverrfgvlfQR-----GALfs 96
Cdd:COG4178 380 EDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLFLP---------------QRpylplGTL-- 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 97 sltvTENVALPLIENAglpRSEAErLAQVkLALAGLPP-----GTGSKYPASLSGGMVKRVALARALALDPDILFLDEPT 171
Cdd:COG4178 443 ----REALLYPATAEA---FSDAE-LREA-LEAVGLGHlaerlDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEAT 513
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 553371603 172 AGLDPIGAAAfdsLIRTLRDAL-NLTVFLVTHDlDTLYTLCDRVAVLS 218
Cdd:COG4178 514 SALDEENEAA---LYQLLREELpGTTVISVGHR-STLAAFHDRVLELT 557
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-235 |
1.27e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 76.55 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 17 GVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSramVERRFGVLFQRGALFS 96
Cdd:PLN03232 1247 GLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTD---LRRVLSIIPQSPVLFS 1323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 97 SlTVTENVAlPLIENAGLPRSEAERLAQVKLALAGLPPGTGSKY---PASLSGGMVKRVALARALALDPDILFLDEPTAG 173
Cdd:PLN03232 1324 G-TVRFNID-PFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVsegGENFSVGQRQLLSLARALLRRSKILVLDEATAS 1401
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 553371603 174 LDpigaAAFDSLI-RTLRDAL-NLTVFLVTHDLDTLYTlCDRVAVLSQKKVLVVDTLDKVAATD 235
Cdd:PLN03232 1402 VD----VRTDSLIqRTIREEFkSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRD 1460
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
30-222 |
1.65e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 75.85 E-value: 1.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 30 KRGEVLGVVGGSGTGKSVLLrSIVGLRRPTDGKIhvfGKDLMaLSGQ--SRAMVERRFGVLFQRGALFSSLTVTENvalp 107
Cdd:TIGR00955 49 KPGELLAVMGSSGAGKTTLM-NALAFRSPKGVKG---SGSVL-LNGMpiDAKEMRAISAYVQQDDLFIPTLTVREH---- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 108 LIENAGL--PRSEA-----ERLAQVKLALaGLPP------GTGSKYpASLSGGMVKRVALARALALDPDILFLDEPTAGL 174
Cdd:TIGR00955 120 LMFQAHLrmPRRVTkkekrERVDEVLQAL-GLRKcantriGVPGRV-KGLSGGERKRLAFASELLTDPPLLFCDEPTSGL 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 553371603 175 DPIGAAafdSLIRTLRDALN--LTVFLVTHD-LDTLYTLCDRVAVLSQKKV 222
Cdd:TIGR00955 198 DSFMAY---SVVQVLKGLAQkgKTIICTIHQpSSELFELFDKIILMAEGRV 245
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
24-187 |
1.70e-15 |
|
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: 72.78 E-value: 1.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 24 GLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLmalsGQSRAMVERRFGVLFQRGALFSSLTVTEN 103
Cdd:TIGR01189 18 GLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL----AEQRDEPHENILYLGHLPGLKPELSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 104 VALPLIENAGLPRSEAERLAQVKL-ALAGLPPgtgskypASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAAAF 182
Cdd:TIGR01189 94 LHFWAAIHGGAQRTIEDALAAVGLtGFEDLPA-------AQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALL 166
|
....*
gi 553371603 183 DSLIR 187
Cdd:TIGR01189 167 AGLLR 171
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
25-223 |
2.37e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 73.67 E-value: 2.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 25 LNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAmveRRFGVLFQRGAlfSSLTVTENV 104
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRS---QRIRMIFQDPS--TSLNPRQRI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 105 A----LPLIENAGLPRSEAERLAQVKLALAGLPPGTGSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAA 180
Cdd:PRK15112 107 SqildFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRS 186
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 553371603 181 AFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKVL 223
Cdd:PRK15112 187 QLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVV 229
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-204 |
3.12e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 72.81 E-value: 3.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 7 IQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAmveRRFG 86
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELA---KRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 87 VLFQRGALFSSLTVTENVALplienaG-LP----RSEAERLAQVKLALA--GLPPGTGsKYPASLSGGMVKRVALARALA 159
Cdd:COG4604 79 ILRQENHINSRLTVRELVAF------GrFPyskgRLTAEDREIIDEAIAylDLEDLAD-RYLDELSGGQRQRAFIAMVLA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 553371603 160 LDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDL 204
Cdd:COG4604 152 QDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDI 196
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
25-222 |
3.66e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 74.88 E-value: 3.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 25 LNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRrPTDGKIHVFGKDLMALS-GQSRamveRRFGVLFQRGALFSSlTVTEN 103
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDpESWR----KHLSWVGQNPQLPHG-TLRDN 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 104 VALplienaGLPRSEAERLAQVkLALA-----------GL--PPGTGSkypASLSGGMVKRVALARALALDPDILFLDEP 170
Cdd:PRK11174 443 VLL------GNPDASDEQLQQA-LENAwvseflpllpqGLdtPIGDQA---AGLSVGQAQRLALARALLQPCQLLLLDEP 512
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 553371603 171 TAGLDPIGAAAfdsLIRTLRDA-LNLTVFLVTHDLDTLYTlCDRVAVLSQKKV 222
Cdd:PRK11174 513 TASLDAHSEQL---VMQALNAAsRRQTTLMVTHQLEDLAQ-WDQIWVMQDGQI 561
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
32-225 |
4.04e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 74.53 E-value: 4.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 32 GEVLGVVGGSGTGKSVLLRSIVGLRRPtdgkiHVFGKDLMALSGQSRAMVERRFGVLFQRGALFSSLTVTEN---VALPL 108
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQG-----NNFTGTILANNRKPTKQILKRTGFVTQDDILYPHLTVRETlvfCSLLR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 109 IENAgLPRSEAERLAQVKLALAGLPPG----TGSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAAAFDS 184
Cdd:PLN03211 169 LPKS-LTKQEKILVAESVISELGLTKCentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVL 247
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 553371603 185 LIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVV 225
Cdd:PLN03211 248 TLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFF 288
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
23-223 |
5.28e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 72.51 E-value: 5.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 23 QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAmveRRFGVLFQRGALFSSLTVTE 102
Cdd:PRK10575 28 HPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFA---RKVAYLPQQLPAAEGMTVRE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 103 NVALPLIENAG-LPRSEAERLAQVK--LALAGLPPgTGSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGA 179
Cdd:PRK10575 105 LVAIGRYPWHGaLGRFGAADREKVEeaISLVGLKP-LAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQ 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 553371603 180 AAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKVL 223
Cdd:PRK10575 184 VDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMI 227
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
29-212 |
7.74e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.22 E-value: 7.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 29 VKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFG--------KDLMALSGQSRAmVERRFGVLfqrgalfssltV 100
Cdd:PRK15056 30 VPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGqptrqalqKNLVAYVPQSEE-VDWSFPVL-----------V 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 101 TENVALPLIENAG-LPRSEAERLAQVKLALAGLP-PGTGSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIG 178
Cdd:PRK15056 98 EDVVMMGRYGHMGwLRRAKKRDRQIVTAALARVDmVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKT 177
|
170 180 190
....*....|....*....|....*....|....
gi 553371603 179 AAAFDSLIRTLRDAlNLTVFLVTHDLDTLYTLCD 212
Cdd:PRK15056 178 EARIISLLRELRDE-GKTMLVSTHNLGSVTEFCD 210
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
23-187 |
1.99e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 69.83 E-value: 1.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 23 QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLmalsgqsRAMVERRFGVLFQRG---ALFSSLT 99
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI-------RRQRDEYHQDLLYLGhqpGIKTELT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 100 VTENV--ALPLienAGLPRSEA--ERLAQVklALAG---LPPGTgskypasLSGGMVKRVALARaLALDPDILF-LDEPT 171
Cdd:PRK13538 91 ALENLrfYQRL---HGPGDDEAlwEALAQV--GLAGfedVPVRQ-------LSAGQQRRVALAR-LWLTRAPLWiLDEPF 157
|
170
....*....|....*.
gi 553371603 172 AGLDPIGAAAFDSLIR 187
Cdd:PRK13538 158 TAIDKQGVARLEALLA 173
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-218 |
2.26e-14 |
|
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: 70.51 E-value: 2.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 28 DVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDL--------MALSGQSRAMVerrFGVLfqRGALFSSLT 99
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVsykpqyikADYEGTVRDLL---SSIT--KDFYTHPYF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 100 VTEnVALPLienaglprsEAERLAQVKLAlaglppgtgskypaSLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGA 179
Cdd:cd03237 96 KTE-IAKPL---------QIEQILDREVP--------------ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQR 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 553371603 180 AAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLS 218
Cdd:cd03237 152 LMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFE 190
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
25-213 |
4.24e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 71.54 E-value: 4.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 25 LNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVfgkDLMALSGQSRAMVERRFGVLFQRGALFSSLTVTEN- 103
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILL---DGKPVTAEQPEDYRKLFSAVFTDFHLFDQLLGPEGk 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 104 VALPLIENAGLprseaERLA-QVKLALAGlppgtGSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAAAF 182
Cdd:PRK10522 419 PANPALVEKWL-----ERLKmAHKLELED-----GRISNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREF 488
|
170 180 190
....*....|....*....|....*....|.
gi 553371603 183 DSLIRTLRDALNLTVFLVTHDlDTLYTLCDR 213
Cdd:PRK10522 489 YQVLLPLLQEMGKTIFAISHD-DHYFIHADR 518
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
16-205 |
4.86e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 70.02 E-value: 4.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 16 FGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSramVERRFGVLFQRGALF 95
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKE---VARRIGLLAQNATTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 96 SSLTVTENVA------LPLIENAglpRSEAERlaqvklALAGLPPGTGSKYPA-----SLSGGMVKRVALARALALDPDI 164
Cdd:PRK10253 94 GDITVQELVArgryphQPLFTRW---RKEDEE------AVTKAMQATGITHLAdqsvdTLSGGQRQRAWIAMVLAQETAI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 553371603 165 LFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLD 205
Cdd:PRK10253 165 MLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLN 205
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
21-187 |
5.31e-14 |
|
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: 68.67 E-value: 5.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 21 VHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLmalsGQSRAMVERRFGVLFQRGALFSSLTV 100
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL----DFQRDSIARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 101 TENVALPLIENAGLPRSEAerLAQVKLAlaglppGTGSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAA 180
Cdd:cd03231 91 LENLRFWHADHSDEQVEEA--LARVGLN------GFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
....*..
gi 553371603 181 AFDSLIR 187
Cdd:cd03231 163 RFAEAMA 169
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-217 |
1.10e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 70.34 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 3 QDAIIQIRDLVNCF-GVQCVHqGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLrRPT---DGKIHVFGKDLMAlsgQSR 78
Cdd:PRK13549 2 MEYLLEMKNITKTFgGVKALD-NVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEELQA---SNI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 79 AMVERR-FGVLFQRGALFSSLTVTENVAL-------PLIENAGLPRSEAERLAQVKLalaGLPPGTgskyPAS-LSGGMV 149
Cdd:PRK13549 77 RDTERAgIAIIHQELALVKELSVLENIFLgneitpgGIMDYDAMYLRAQKLLAQLKL---DINPAT----PVGnLGLGQQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 553371603 150 KRVALARALALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRdALNLTVFLVTHDLDTLYTLCDRVAVL 217
Cdd:PRK13549 150 QLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLK-AHGIACIYISHKLNEVKAISDTICVI 216
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
35-203 |
1.12e-13 |
|
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: 70.35 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 35 LGVVGGSGTGKSVLLRSIVGLRRPtdgkihvfgkdlmaLSGQSRAMVERRFGVLFQRGALFSSLTVTENV--ALPLIENA 112
Cdd:TIGR03719 34 IGVLGLNGAGKSTLLRIMAGVDKD--------------FNGEARPQPGIKVGYLPQEPQLDPTKTVRENVeeGVAEIKDA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 113 -----------GLPRSEAERLA------QVKLALAG----------------LPPGTGSKypASLSGGMVKRVALARALA 159
Cdd:TIGR03719 100 ldrfneisakyAEPDADFDKLAaeqaelQEIIDAADawdldsqleiamdalrCPPWDADV--TKLSGGERRRVALCRLLL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 553371603 160 LDPDILFLDEPTAGLDpigAAAFDSLIRTLRDALNlTVFLVTHD 203
Cdd:TIGR03719 178 SKPDMLLLDEPTNHLD---AESVAWLERHLQEYPG-TVVAVTHD 217
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
25-239 |
2.49e-13 |
|
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: 69.66 E-value: 2.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 25 LNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMAlsgqSRAMVERRFGVLFQRGALFSSLTVTENV 104
Cdd:TIGR01257 1958 LCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT----NISDVHQNMGYCPQFDAIDDLLTGREHL 2033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 105 ALpLIENAGLPRSEAERLAQVKLALAGLPPgTGSKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAAA-FD 183
Cdd:TIGR01257 2034 YL-YARLRGVPAEEIEKVANWSIQSLGLSL-YADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMlWN 2111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 553371603 184 SLIRTLRDAlnLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDTLDKVAAT-DDGWI 239
Cdd:TIGR01257 2112 TIVSIIREG--RAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKfGDGYI 2166
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-217 |
3.41e-13 |
|
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: 68.70 E-value: 3.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 6 IIQIRDLVNCFG-VQCVHqGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGL--RRPTDGKIHVFGKDLMALSgqSRAMVE 82
Cdd:TIGR02633 1 LLEMKGIVKTFGgVKALD-GIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASN--IRDTER 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 83 RRFGVLFQRGALFSSLTVTENVAL--------PLIENAGLPRSEAERLAQVKlalagLPPGTGSKYPASLSGGMVKRVAL 154
Cdd:TIGR02633 78 AGIVIIHQELTLVPELSVAENIFLgneitlpgGRMAYNAMYLRAKNLLRELQ-----LDADNVTRPVGDYGGGQQQLVEI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 553371603 155 ARALALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRdALNLTVFLVTHDLDTLYTLCDRVAVL 217
Cdd:TIGR02633 153 AKALNKQARLLILDEPSSSLTEKETEILLDIIRDLK-AHGVACVYISHKLNEVKAVCDTICVI 214
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
24-233 |
7.52e-13 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 67.68 E-value: 7.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 24 GLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLmalSGQSRAMVERRFGVLFQRGALFSSlTVTEN 103
Cdd:PRK13657 353 DVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDI---RTVTRASLRRNIAVVFQDAGLFNR-SIEDN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 104 VALplienaGLPR-SEAERLAQVKLALA---------GLPPGTGSKyPASLSGGMVKRVALARALALDPDILFLDEPTAG 173
Cdd:PRK13657 429 IRV------GRPDaTDEEMRAAAERAQAhdfierkpdGYDTVVGER-GRQLSGGERQRLAIARALLKDPPILILDEATSA 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 174 LDPIGAAAFDSLIRTLRDalNLTVFLVTHDLDTLYTlCDRVAVLSQKKVLVVDTLDKVAA 233
Cdd:PRK13657 502 LDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGSFDELVA 558
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
24-175 |
8.01e-13 |
|
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: 67.92 E-value: 8.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 24 GLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQS-RAMVerrfGVLFQRGALFSSlTVTE 102
Cdd:COG5265 376 GVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASlRAAI----GIVPQDTVLFND-TIAY 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 103 NVALPlieNAGLPRSE---AERLAQVKLALAGLPPG--T-----GSKypasLSGGMVKRVALARALALDPDILFLDEPTA 172
Cdd:COG5265 451 NIAYG---RPDASEEEveaAARAAQIHDFIESLPDGydTrvgerGLK----LSGGEKQRVAIARTLLKNPPILIFDEATS 523
|
...
gi 553371603 173 GLD 175
Cdd:COG5265 524 ALD 526
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
23-223 |
1.05e-12 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 65.97 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 23 QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLR--RPTDGKIHVFGKDLMALSGQSRAMvERRFgVLFQ--------RG 92
Cdd:PRK09580 18 RGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAG-EGIF-MAFQypveipgvSN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 93 ALFssLTVTENVALPLIENAGLPRSEAERLAQVKLALAGLPPGTGSK-YPASLSGGMVKRVALARALALDPDILFLDEPT 171
Cdd:PRK09580 96 QFF--LQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLLTRsVNVGFSGGEKKRNDILQMAVLEPELCILDESD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 553371603 172 AGLDPIGAAAFDSLIRTLRDAlNLTVFLVTHDLDTL-YTLCDRVAVLSQKKVL 223
Cdd:PRK09580 174 SGLDIDALKIVADGVNSLRDG-KRSFIIVTHYQRILdYIKPDYVHVLYQGRIV 225
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
25-188 |
2.13e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 64.48 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 25 LNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDlmalsgQSRAMVERRFGVLFQRGALFSSLTVTENV 104
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKT------ATRGDRSRFMAYLGHLPGLKADLSTLENL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 105 ALPlienAGLPRSEAERLAQVKLALAGLpPGTGSKYPASLSGGMVKRVALARaLALDPDILF-LDEPTAGLDPIGAAAFD 183
Cdd:PRK13543 104 HFL----CGLHGRRAKQMPGSALAIVGL-AGYEDTLVRQLSAGQKKRLALAR-LWLSPAPLWlLDEPYANLDLEGITLVN 177
|
....*
gi 553371603 184 SLIRT 188
Cdd:PRK13543 178 RMISA 182
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
7-231 |
2.23e-12 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 65.91 E-value: 2.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 7 IQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVG--GSGTGKSVLLRSIVGL---RRPTdgKIHVFGKDLMALsgqsRAMV 81
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGp*GAA**RGALPAHV*GPdagRRPW--RF*TWCANRRAL----RRTI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 82 ERRFGVLFQRGALFSSltvTENVALpLIENAGLPRSEAERLAQVKLALAGLPPGTGsKYPASLSGGMVKRVALARALALD 161
Cdd:NF000106 88 G*HRPVR*GRRESFSG---RENLYM-IGR*LDLSRKDARARADELLERFSLTEAAG-RAAAKYSGGMRRRLDLAASMIGR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 553371603 162 PDILFLDEPTAGLDP-IGAAAFDSLIRTLRDAlnLTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDTLDKV 231
Cdd:NF000106 163 PAVLYLDEPTTGLDPrTRNEVWDEVRSMVRDG--ATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-216 |
2.99e-12 |
|
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: 65.96 E-value: 2.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 28 DVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHvfgKDL------MALSGQSRAMVErrfGVLFQ-RGALFSSLTV 100
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD---EDLkisykpQYISPDYDGTVE---EFLRSaNTDDFGSSYY 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 101 TENVALPLienaGLprseaERLAQvklalaglppgtgsKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLD---PI 177
Cdd:COG1245 436 KTEIIKPL----GL-----EKLLD--------------KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqRL 492
|
170 180 190
....*....|....*....|....*....|....*....
gi 553371603 178 GAAafdSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAV 216
Cdd:COG1245 493 AVA---KAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-262 |
3.48e-12 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 66.09 E-value: 3.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 21 VHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRpTDGKIHVFGKDLMALSGQSRamvERRFGVLFQRGALFSSlTV 100
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTW---RKAFGVIPQKVFIFSG-TF 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 101 TENV----------ALPLIENAGLpRSEAERLAQvKLALAGLPPGtgskypASLSGGMVKRVALARALALDPDILFLDEP 170
Cdd:TIGR01271 1309 RKNLdpyeqwsdeeIWKVAEEVGL-KSVIEQFPD-KLDFVLVDGG------YVLSNGHKQLMCLARSILSKAKILLLDEP 1380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 171 TAGLDPIgaaAFDSLIRTLRDAL-NLTVFLVTHDLDTLYTlCDRVAVLSQKKVLVVDTLDKVAATDDGWIQAYFHGPRGR 249
Cdd:TIGR01271 1381 SAHLDPV---TLQIIRKTLKQSFsNCTVILSEHRVEALLE-CQQFLVIEGSSVKQYDSIQKLLNETSLFKQAMSAADRLK 1456
|
250
....*....|...
gi 553371603 250 aAYQAAAINSGER 262
Cdd:TIGR01271 1457 -LFPLHRRNSSKR 1468
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
21-226 |
3.55e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.82 E-value: 3.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 21 VHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVG--LRRPTDGKIHVFGKDLmalsGQSRAMVErrfgvlfqrgALFSSL 98
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVPDNQF----GREASLID----------AIGRKG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 99 TVTENValplienaglprseaERLAQVKLALAGLppgtgskY---PASLSGGMVKRVALARALALDPDILFLDEPTAGLD 175
Cdd:COG2401 111 DFKDAV---------------ELLNAVGLSDAVL-------WlrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 553371603 176 P----IGAAAFDSLIRTLRdalnLTVFLVTHDLDTLYTLC-DRVAVLSQKKVLVVD 226
Cdd:COG2401 169 RqtakRVARNLQKLARRAG----ITLVVATHHYDVIDDLQpDLLIFVGYGGVPEEK 220
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
2-222 |
3.84e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 65.62 E-value: 3.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 2 TQDAIIQIRDLvNCFGVQCVH----QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPT-DGKIHVFGKDLMALSGQ 76
Cdd:TIGR02633 253 IGDVILEARNL-TCWDVINPHrkrvDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPA 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 77 SR-----AMV-ERRfgvlfQRGALFSSLTVTENVALPLIEN-AGLPR-SEAERLAQVKLALAGLPPGTGSKY--PASLSG 146
Cdd:TIGR02633 332 QAiragiAMVpEDR-----KRHGIVPILGVGKNITLSVLKSfCFKMRiDAAAELQIIGSAIQRLKVKTASPFlpIGRLSG 406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 553371603 147 GMVKRVALARALALDPDILFLDEPTAGLDpIGAAAfdsLIRTLRDAL---NLTVFLVTHDLDTLYTLCDRVAVLSQKKV 222
Cdd:TIGR02633 407 GNQQKAVLAKMLLTNPRVLILDEPTRGVD-VGAKY---EIYKLINQLaqeGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
25-214 |
5.80e-12 |
|
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: 65.20 E-value: 5.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 25 LNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKdlmALSGQSRAMVERRFGVLFQRGALFSSLtvtenv 104
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQ---PVTADNREAYRQLFSAVFSDFHLFDRL------ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 105 alplienAGLPRSEAERLAQ---VKLALAGLPPGTGSKY-PASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAA 180
Cdd:COG4615 422 -------LGLDGEADPARARellERLELDHKVSVEDGRFsTTDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRR 494
|
170 180 190
....*....|....*....|....*....|....*
gi 553371603 181 AF-DSLIRTLRdALNLTVFLVTHDlDTLYTLCDRV 214
Cdd:COG4615 495 VFyTELLPELK-ARGKTVIAISHD-DRYFDLADRV 527
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
24-222 |
6.83e-12 |
|
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: 65.35 E-value: 6.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 24 GLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGkdlmalsgqSRAMVERRfgvlfqrgALFSSLTVTEN 103
Cdd:TIGR00957 656 GITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG---------SVAYVPQQ--------AWIQNDSLREN 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 104 VAL--PLIENAGLPRSEA-ERLAQVKLALAGLPPGTGSKyPASLSGGMVKRVALARALALDPDILFLDEPTAGLDP-IGA 179
Cdd:TIGR00957 719 ILFgkALNEKYYQQVLEAcALLPDLEILPSGDRTEIGEK-GVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAhVGK 797
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 553371603 180 AAFDSLIRTLRDALNLTVFLVTHDLDTLYTLcDRVAVLSQKKV 222
Cdd:TIGR00957 798 HIFEHVIGPEGVLKNKTRILVTHGISYLPQV-DVIIVMSGGKI 839
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
23-219 |
7.92e-12 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 62.67 E-value: 7.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 23 QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPT---DGKIHVFGKDLmalsgqsramveRRFGVLFQRGALFSS-- 97
Cdd:cd03233 24 KDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPY------------KEFAEKYPGEIIYVSee 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 98 ------LTVTEnvalpLIENAGLPRseaerlaqvklalaglppgtGSKYPASLSGGMVKRVALARALALDPDILFLDEPT 171
Cdd:cd03233 92 dvhfptLTVRE-----TLDFALRCK--------------------GNEFVRGISGGERKRVSIAEALVSRASVLCWDNST 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 553371603 172 AGLDPIGAAAFDSLIRTLRDALNLTVFL-VTHDLDTLYTLCDRVAVLSQ 219
Cdd:cd03233 147 RGLDSSTALEILKCIRTMADVLKTTTFVsLYQASDEIYDLFDKVLVLYE 195
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
23-244 |
9.62e-12 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 64.35 E-value: 9.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 23 QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQS-RAmverRFGVLFQRGALFSSlTVT 101
Cdd:PRK10789 332 ENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwRS----RLAVVSQTPFLFSD-TVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 102 ENVALPLIENAGLPRSEAERLAQVKLALAGLPPG----TGSKyPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPi 177
Cdd:PRK10789 407 NNIALGRPDATQQEIEHVARLASVHDDILRLPQGydteVGER-GVMLSGGQKQRISIARALLLNAEILILDDALSAVDG- 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 553371603 178 gaaafdsliRTLRDAL-NL-------TVFLVTHDLDTLyTLCDRVAVLSQKKVLVVDTLDKVAATdDGWIQAYFH 244
Cdd:PRK10789 485 ---------RTEHQILhNLrqwgegrTVIISAHRLSAL-TEASEILVMQHGHIAQRGNHDQLAQQ-SGWYRDMYR 548
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
5-217 |
1.03e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 64.25 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 5 AIIQIRDLVNCF-GVQCVhQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDlMALSGqSRAMVER 83
Cdd:PRK10762 3 ALLQLKGIDKAFpGVKAL-SGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKE-VTFNG-PKSSQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 84 RFGVLFQRGALFSSLTVTENVALPLIENAGLPR-------SEAERLaqvklaLAGLPPGTGSKYPAS-LSGGMVKRVALA 155
Cdd:PRK10762 80 GIGIIHQELNLIPQLTIAENIFLGREFVNRFGRidwkkmyAEADKL------LARLNLRFSSDKLVGeLSIGEQQMVEIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 553371603 156 RALALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFlVTHDLDTLYTLCDRVAVL 217
Cdd:PRK10762 154 KVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVY-ISHRLKEIFEICDDVTVF 214
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
29-222 |
1.10e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.18 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 29 VKRGEVLGVVGGSGTGKSVLLRSIVGLRR-PTDGKIHVFGKDLM------ALSgQSRAMV-ERRfgvlfQRGALFSSLTV 100
Cdd:PRK13549 285 LRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKirnpqqAIA-QGIAMVpEDR-----KRDGIVPVMGV 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 101 TENVALPLIE---NAGLPRSEAErLAQVKLALAGLPPGTGSkyP----ASLSGGMVKRVALARALALDPDILFLDEPTAG 173
Cdd:PRK13549 359 GKNITLAALDrftGGSRIDDAAE-LKTILESIQRLKVKTAS--PelaiARLSGGNQQKAVLAKCLLLNPKILILDEPTRG 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 553371603 174 LDpIGAAAfdsLIRTLRDAL---NLTVFLVTHDLDTLYTLCDRVAVLSQKKV 222
Cdd:PRK13549 436 ID-VGAKY---EIYKLINQLvqqGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
28-217 |
1.81e-11 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 61.05 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 28 DVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIhvfgkdlmalsgqsramverrfgvlfqrgalfssltvtenvALP 107
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDND-----------------------------------------EWD 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 108 LIENAGLPRSeaerlaqvklalaglppgtgskypASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAAAFDSLIR 187
Cdd:cd03222 60 GITPVYKPQY------------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIR 115
|
170 180 190
....*....|....*....|....*....|
gi 553371603 188 TLRDALNLTVFLVTHDLDTLYTLCDRVAVL 217
Cdd:cd03222 116 RLSEEGKKTALVVEHDLAVLDYLSDRIHVF 145
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
25-223 |
2.15e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 62.54 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 25 LNLDVKRGEVLGVVGGSGTGKSVLLRSIVG-LRRPTD-------GKIHVFGKDLMALSGQSRAmveRRFGVLFQRGALFS 96
Cdd:PRK13547 20 LSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGAprgarvtGDVTLNGEPLAAIDAPRLA---RLRAVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 97 SLTVTENVAL---PLIENAGLPRSEAERLAQVKLALAGLPPGTGSKYpASLSGGMVKRVALARALA---------LDPDI 164
Cdd:PRK13547 97 AFSAREIVLLgryPHARRAGALTHRDGEIAWQALALAGATALVGRDV-TTLSGGELARVQFARVLAqlwpphdaaQPPRY 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 553371603 165 LFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLSQKKVL 223
Cdd:PRK13547 176 LLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIV 234
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-251 |
2.40e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.39 E-value: 2.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 21 VHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSgqSRAMVerRFGVLF------QRGaL 94
Cdd:PRK11288 268 LREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRS--PRDAI--RAGIMLcpedrkAEG-I 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 95 FSSLTVTENVALP---------LIENAGLPRSEAERLAQ---VKLALAGLPPGTgskypasLSGGMVKRVALARALALDP 162
Cdd:PRK11288 343 IPVHSVADNINISarrhhlragCLINNRWEAENADRFIRslnIKTPSREQLIMN-------LSGGNQQKAILGRWLSEDM 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 163 DILFLDEPTAGLDpIGAAA-FDSLIRTLRDAlNLTVFLVTHDLDTLYTLCDRVAVLSQKKvlVVDTLDKVAATDDGWIQA 241
Cdd:PRK11288 416 KVILLDEPTRGID-VGAKHeIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGR--IAGELAREQATERQALSL 491
|
250
....*....|
gi 553371603 242 YFhgPRGRAA 251
Cdd:PRK11288 492 AL--PRTSAA 499
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
36-205 |
2.72e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.21 E-value: 2.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 36 GVVGGSGTGKSVLLRSIVGLRRPTDGKihvfgkdlmalsgqSRAMVERRFGVLFQRGALFSSLTVTENVALPLIE----- 110
Cdd:PRK11819 37 GVLGLNGAGKSTLLRIMAGVDKEFEGE--------------ARPAPGIKVGYLPQEPQLDPEKTVRENVEEGVAEvkaal 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 111 --------NAGLPRSEAERLA--QVKL---------------------ALaGLPPGTGSkyPASLSGGMVKRVALARALA 159
Cdd:PRK11819 103 drfneiyaAYAEPDADFDALAaeQGELqeiidaadawdldsqleiamdAL-RCPPWDAK--VTKLSGGERRRVALCRLLL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 553371603 160 LDPDILFLDEPTAGLDpigAAAFDSLIRTLRDaLNLTVFLVTHD---LD 205
Cdd:PRK11819 180 EKPDMLLLDEPTNHLD---AESVAWLEQFLHD-YPGTVVAVTHDryfLD 224
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
7-207 |
3.40e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 62.81 E-value: 3.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 7 IQIRDLVNCFGV-QCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSG----QSRAMV 81
Cdd:PRK10790 341 IDIDNVSFAYRDdNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHsvlrQGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 82 ERRFGVLfqrgalfsSLTVTENVALplienaGLPRSEA---ERLAQVKLA-LA-GLPPGTGSKYPA---SLSGGMVKRVA 153
Cdd:PRK10790 421 QQDPVVL--------ADTFLANVTL------GRDISEEqvwQALETVQLAeLArSLPDGLYTPLGEqgnNLSVGQKQLLA 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 553371603 154 LARALALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVflVTHDLDTL 207
Cdd:PRK10790 487 LARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVV--IAHRLSTI 538
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
25-202 |
3.42e-11 |
|
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: 60.25 E-value: 3.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 25 LNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHvfgkdlmalsgqsraMVERRfGVLF--QRGaLFSSLTVTE 102
Cdd:cd03223 20 LSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG---------------MPEGE-DLLFlpQRP-YLPLGTLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 103 NVALPLIENaglprseaerlaqvklalaglppgtgskypasLSGGMVKRVALARALALDPDILFLDEPTAGLDPigaAAF 182
Cdd:cd03223 83 QLIYPWDDV--------------------------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDE---ESE 127
|
170 180
....*....|....*....|
gi 553371603 183 DSLIRTLRDALnLTVFLVTH 202
Cdd:cd03223 128 DRLYQLLKELG-ITVISVGH 146
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
29-251 |
4.27e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.82 E-value: 4.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 29 VKRGEVLGVVGGSGTGKSVLLRSI----VGLRRPTDGKIHvfgkdlmaLSGQSRAMVERRFgvlfqRGAL---------F 95
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVIT--------YDGITPEEIKKHY-----RGDVvynaetdvhF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 96 SSLTVTENVAL------PLIENAGLPRSE-AERLAQVKLALAGLP----PGTGSKYPASLSGGMVKRVALARALALDPDI 164
Cdd:TIGR00956 151 PHLTVGETLDFaarcktPQNRPDGVSREEyAKHIADVYMATYGLShtrnTKVGNDFVRGVSGGERKRVSIAEASLGGAKI 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 165 LFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLvthdldTLYTlCdrvavlSQKkvlVVDTLDKVAATDDGWiQAYFh 244
Cdd:TIGR00956 231 QCWDNATRGLDSATALEFIRALKTSANILDTTPLV------AIYQ-C------SQD---AYELFDKVIVLYEGY-QIYF- 292
|
....*..
gi 553371603 245 GPRGRAA 251
Cdd:TIGR00956 293 GPADKAK 299
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
26-222 |
4.68e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.33 E-value: 4.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 26 NLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQ---SRAMV---ERRfgvlfQRGALFSSLT 99
Cdd:PRK10762 272 SFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdglANGIVyisEDR-----KRDGLVLGMS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 100 VTENVALP----LIENAGLPRSEAERLA--------QVKLALAGLPPGTgskypasLSGGMVKRVALARALALDPDILFL 167
Cdd:PRK10762 347 VKENMSLTalryFSRAGGSLKHADEQQAvsdfirlfNIKTPSMEQAIGL-------LSGGNQQKVAIARGLMTRPKVLIL 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 553371603 168 DEPTAGLDpIGAAA-FDSLIRTLRdALNLTVFLVTHDLDTLYTLCDRVAVLSQKKV 222
Cdd:PRK10762 420 DEPTRGVD-VGAKKeIYQLINQFK-AEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-218 |
7.67e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 61.75 E-value: 7.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 29 VKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIhvfGKDL------MALSGQSRAMVERrfgVLFQRGALFSSLTVTE 102
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV---DPELkisykpQYIKPDYDGTVED---LLRSITDDLGSSYYKS 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 103 NVALPLienaGLprseaERLAQvklalaglppgtgsKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLD---PIGA 179
Cdd:PRK13409 436 EIIKPL----QL-----ERLLD--------------KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqRLAV 492
|
170 180 190
....*....|....*....|....*....|....*....
gi 553371603 180 AafdSLIRTLRDALNLTVFLVTHDLDTLYTLCDRVAVLS 218
Cdd:PRK13409 493 A---KAIRRIAEEREATALVVDHDIYMIDYISDRLMVFE 528
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
25-207 |
9.20e-11 |
|
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: 60.04 E-value: 9.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 25 LNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHvFGKDLMALSGQSRAMVERRFGVLF--QRGALFSSlTVTE 102
Cdd:cd03290 20 INIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVH-WSNKNESEPSFEATRSRNRYSVAYaaQKPWLLNA-TVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 103 NVAL--PLIENAGLPRSEAERLaQVKLALagLPPGTGSKYPA---SLSGGMVKRVALARALALDPDILFLDEPTAGLDPI 177
Cdd:cd03290 98 NITFgsPFNKQRYKAVTDACSL-QPDIDL--LPFGDQTEIGErgiNLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 174
|
170 180 190
....*....|....*....|....*....|..
gi 553371603 178 GAAAF--DSLIRTLRDAlNLTVFLVTHDLDTL 207
Cdd:cd03290 175 LSDHLmqEGILKFLQDD-KRTLVLVTHKLQYL 205
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
109-175 |
1.34e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.12 E-value: 1.34e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 553371603 109 IENAGLPRSEAeRLAQVkLALAGLPPGTGSkypASLSGGMVKRVALARALALDPDILFLDEPTAGLD 175
Cdd:PRK11147 127 LDHHNLWQLEN-RINEV-LAQLGLDPDAAL---SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-215 |
1.74e-10 |
|
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: 60.72 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 4 DAIIQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAmver 83
Cdd:TIGR03719 320 DKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRD---- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 84 rfgvlfqrgALFSSLTVTENVA--LPLIENAGlpRSEAERlaqvklALAGLPPGTGS---KYPASLSGGMVKRVALARAL 158
Cdd:TIGR03719 396 ---------ALDPNKTVWEEISggLDIIKLGK--REIPSR------AYVGRFNFKGSdqqKKVGQLSGGERNRVHLAKTL 458
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 553371603 159 ALDPDILFLDEPTAGLDpigaaafdslIRTLR---DALNL---TVFLVTHDLDTLytlcDRVA 215
Cdd:TIGR03719 459 KSGGNVLLLDEPTNDLD----------VETLRaleEALLNfagCAVVISHDRWFL----DRIA 507
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-223 |
1.90e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 59.66 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 1 MTQDAIIQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGlrRP----TDGKIHVFGKDLMALSGQ 76
Cdd:CHL00131 2 NKNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPaykiLEGDILFKGESILDLEPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 77 SRAmverRFGVL--FQR-----GalfssltVTENVALPLIENA-----GLPRSEAERLAQV---KLALAGLPPGTGSKY- 140
Cdd:CHL00131 80 ERA----HLGIFlaFQYpieipG-------VSNADFLRLAYNSkrkfqGLPELDPLEFLEIineKLKLVGMDPSFLSRNv 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 141 PASLSGGMVKRVALARALALDPDILFLDEPTAGLDpigaaaFDSL------IRTLRDALNlTVFLVTHD---LDtlYTLC 211
Cdd:CHL00131 149 NEGFSGGEKKRNEILQMALLDSELAILDETDSGLD------IDALkiiaegINKLMTSEN-SIILITHYqrlLD--YIKP 219
|
250
....*....|..
gi 553371603 212 DRVAVLSQKKVL 223
Cdd:CHL00131 220 DYVHVMQNGKII 231
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-227 |
2.11e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 60.91 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 21 VHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALsgqSRAMVERRFGVLFQRGALFSSlTV 100
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKF---GLMDLRKVLGIIPQAPVLFSG-TV 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 101 TENVAlPLIENAGLPRSEAERLAQVKLALAGLPPGTG---SKYPASLSGGMVKRVALARALALDPDILFLDEPTAGLDpi 177
Cdd:PLN03130 1330 RFNLD-PFNEHNDADLWESLERAHLKDVIRRNSLGLDaevSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVD-- 1406
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 553371603 178 gaAAFDSLI-RTLRDAL-NLTVFLVTHDLDTLYTlCDRVAVLSQKKVLVVDT 227
Cdd:PLN03130 1407 --VRTDALIqKTIREEFkSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDT 1455
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
25-207 |
2.43e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 60.42 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 25 LNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSramVERRFGVLFQRGALFSSlTVTENV 104
Cdd:PRK11176 362 INFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLAS---LRNQVALVSQNVHLFND-TIANNI 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 105 ALPliENAGLPRSEAERLAQVKLALA-------GLPPGTGSKyPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPI 177
Cdd:PRK11176 438 AYA--RTEQYSREQIEEAARMAYAMDfinkmdnGLDTVIGEN-GVLLSGGQRQRIAIARALLRDSPILILDEATSALDTE 514
|
170 180 190
....*....|....*....|....*....|
gi 553371603 178 GAAAFDSLIRTLRDalNLTVFLVTHDLDTL 207
Cdd:PRK11176 515 SERAIQAALDELQK--NRTSLVIAHRLSTI 542
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
7-247 |
3.02e-10 |
|
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: 59.10 E-value: 3.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 7 IQIRDLVNCF--GVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRpTDGKIHVFGkdlmaLSGQSRAMVERR 84
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDG-----VSWNSVPLQKWR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 85 --FGVLFQRGALFSSlTVTENV----------ALPLIENAGLpRSEAERLAQvKLALAGLPPGtgskypASLSGGMVKRV 152
Cdd:cd03289 77 kaFGVIPQKVFIFSG-TFRKNLdpygkwsdeeIWKVAEEVGL-KSVIEQFPG-QLDFVLVDGG------CVLSHGHKQLM 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 153 ALARALALDPDILFLDEPTAGLDPIgaaAFDSLIRTLRDAL-NLTVFLVTHDLDTLYTlCDRVAVLSQKKVLVVDTLDKV 231
Cdd:cd03289 148 CLARSVLSKAKILLLDEPSAHLDPI---TYQVIRKTLKQAFaDCTVILSEHRIEAMLE-CQRFLVIEENKVRQYDSIQKL 223
|
250
....*....|....*.
gi 553371603 232 AATDDGWIQAYFHGPR 247
Cdd:cd03289 224 LNEKSHFKQAISPSDR 239
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
15-219 |
4.04e-10 |
|
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: 58.71 E-value: 4.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 15 CFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKdlMALSGQSramverrfgvlfqrgAL 94
Cdd:cd03291 46 CLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--ISFSSQF---------------SW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 95 FSSLTVTENVALPLIENAGLPRS--EAERLAQVKLALA---GLPPGTGSkypASLSGGMVKRVALARALALDPDILFLDE 169
Cdd:cd03291 109 IMPGTIKENIIFGVSYDEYRYKSvvKACQLEEDITKFPekdNTVLGEGG---ITLSGGQRARISLARAVYKDADLYLLDS 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 553371603 170 PTAGLDPIGAAA-FDSLIRTLrdALNLTVFLVTHDLDTLyTLCDRVAVLSQ 219
Cdd:cd03291 186 PFGYLDVFTEKEiFESCVCKL--MANKTRILVTSKMEHL-KKADKILILHE 233
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
29-192 |
4.55e-10 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 57.64 E-value: 4.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 29 VKRGEVLGVVGGSGTGKSVLLRSIVGlrRPTDGKIhvfGKDLMaLSGQSRAM-VERRFGVLFQRGALFSSLTVTEnvalp 107
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLDVLAG--RKTAGVI---TGEIL-INGRPLDKnFQRSTGYVEQQDVHSPNLTVRE----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 108 lienaglprseaerlaqvklALaglppgtgsKYPASLSGGMV---KRVALARALALDPDILFLDEPTAGLDPIGAAAFDS 184
Cdd:cd03232 99 --------------------AL---------RFSALLRGLSVeqrKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVR 149
|
....*...
gi 553371603 185 LIRTLRDA 192
Cdd:cd03232 150 FLKKLADS 157
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
144-217 |
2.33e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.51 E-value: 2.33e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 553371603 144 LSGGMVKRVALARALALDPDILFLDEPTAGLD---PIGAAafdSLIRTLrdALNLTVFLVTHDLDTLYTLCDRVAVL 217
Cdd:PRK13409 213 LSGGELQRVAIAAALLRDADFYFFDEPTSYLDirqRLNVA---RLIREL--AEGKYVLVVEHDLAVLDYLADNVHIA 284
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
23-227 |
2.68e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.05 E-value: 2.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 23 QGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSR-----AMV--ERRfgvlfqRGALF 95
Cdd:PRK10982 265 RDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAinhgfALVteERR------STGIY 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 96 SSLTVTENvalPLIENAGLPRSEAERLAQVKL---------ALAGLPPGTGSKYpASLSGGMVKRVALARALALDPDILF 166
Cdd:PRK10982 339 AYLDIGFN---SLISNIRNYKNKVGLLDNSRMksdtqwvidSMRVKTPGHRTQI-GSLSGGNQQKVIIGRWLLTQPEILM 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 553371603 167 LDEPTAGLDpIGaAAFD--SLIRTLRDAlNLTVFLVTHDLDTLYTLCDRVAVLSQKKVL-VVDT 227
Cdd:PRK10982 415 LDEPTRGID-VG-AKFEiyQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLVAgIVDT 475
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-207 |
3.62e-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: 57.23 E-value: 3.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 21 VHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKdlMALSGQSRAMVERrfgvlfqrgalfsslTV 100
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR--ISFSPQTSWIMPG---------------TI 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 101 TENVALPLIENAGLPRSeAERLAQVKLALAGLPP------GTGSkypASLSGGMVKRVALARALALDPDILFLDEPTAGL 174
Cdd:TIGR01271 504 KDNIIFGLSYDEYRYTS-VIKACQLEEDIALFPEkdktvlGEGG---ITLSGGQRARISLARAVYKDADLYLLDSPFTHL 579
|
170 180 190
....*....|....*....|....*....|....
gi 553371603 175 DPIGAAA-FDSLIRTLrdALNLTVFLVTHDLDTL 207
Cdd:TIGR01271 580 DVVTEKEiFESCLCKL--MSNKTRILVTSKLEHL 611
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-222 |
4.22e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 56.88 E-value: 4.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 17 GVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSramVERRFGVLFQRGALFS 96
Cdd:TIGR00957 1297 DLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHD---LRFKITIIPQDPVLFS 1373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 97 SlTVTENVAlPLIENAGLPRSEAERLAQVKLALAGLPPGTG---SKYPASLSGGMVKRVALARALALDPDILFLDEPTAG 173
Cdd:TIGR00957 1374 G-SLRMNLD-PFSQYSDEEVWWALELAHLKTFVSALPDKLDhecAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAA 1451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 553371603 174 LDPIGAAAFDSLIRTLRDalNLTVFLVTHDLDTL--YTlcdRVAVLSQKKV 222
Cdd:TIGR00957 1452 VDLETDNLIQSTIRTQFE--DCTVLTIAHRLNTImdYT---RVIVLDKGEV 1497
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
143-217 |
8.03e-09 |
|
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: 55.56 E-value: 8.03e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 553371603 143 SLSGGMVKRVALARALALDPDILFLDEPTAGLD---PIGAAafdSLIRTLRDAlNLTVFLVTHDLDTLYTLCDRVAVL 217
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiyqRLNVA---RLIRELAEE-GKYVLVVEHDLAILDYLADYVHIL 285
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
6-230 |
9.65e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 55.57 E-value: 9.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 6 IIQIRDLVNCF-GVQCVhQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLrRPT---DGKIHVFGKdlmalsgqsramv 81
Cdd:NF040905 1 ILEMRGITKTFpGVKAL-DDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHgsyEGEILFDGE------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 82 ERRFG-----------VLFQRGALFSSLTVTENVALplienaGLPRS--------EAERLAQVKLALAGL--PPGTGSKy 140
Cdd:NF040905 66 VCRFKdirdsealgivIIHQELALIPYLSIAENIFL------GNERAkrgvidwnETNRRARELLAKVGLdeSPDTLVT- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 141 paSLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRdALNLTVFLVTHDLDTLYTLCDRVAVLSQK 220
Cdd:NF040905 139 --DIGVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELK-AQGITSIIISHKLNEIRRVADSITVLRDG 215
|
250
....*....|
gi 553371603 221 KvlVVDTLDK 230
Cdd:NF040905 216 R--TIETLDC 223
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
85-242 |
1.25e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.42 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 85 FGVLFQRGALFSsLTVTENVALPLiENAGLPR-SEAERLAQVKLALAGLPPGTGSK---YPASLSGGMVKRVALARALAL 160
Cdd:PTZ00265 1298 FSIVSQEPMLFN-MSIYENIKFGK-EDATREDvKRACKFAAIDEFIESLPNKYDTNvgpYGKSLSGGQKQRIAIARALLR 1375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 161 DPDILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLVTHDLDTLyTLCDRVAVLSQKK-----VLVVDTLDKVAATD 235
Cdd:PTZ00265 1376 EPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASI-KRSDKIVVFNNPDrtgsfVQAHGTHEELLSVQ 1454
|
....*..
gi 553371603 236 DGWIQAY 242
Cdd:PTZ00265 1455 DGVYKKY 1461
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
32-175 |
1.59e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.87 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 32 GEVLGVVGGSGTGKSVLLR-----SIVGLrrPTDGKI-----HVFGKDLMALSGQSRAMVERRFGV-----LFQRGALFS 96
Cdd:PLN03073 203 GRHYGLVGRNGTGKTTFLRymamhAIDGI--PKNCQIlhveqEVVGDDTTALQCVLNTDIERTQLLeeeaqLVAQQRELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 97 SLTVTENVALPliENAGLPR-SEAERLAQV--KLA--------------LAGLP--PGTGSKYPASLSGGMVKRVALARA 157
Cdd:PLN03073 281 FETETGKGKGA--NKDGVDKdAVSQRLEEIykRLElidaytaearaasiLAGLSftPEMQVKATKTFSGGWRMRIALARA 358
|
170
....*....|....*...
gi 553371603 158 LALDPDILFLDEPTAGLD 175
Cdd:PLN03073 359 LFIEPDLLLLDEPTNHLD 376
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
29-192 |
1.61e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.11 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 29 VKRGEVLGVVGGSGTGKSVLLRSIVGlrRPTDGkihVFGKDLMALSGQSR-AMVERRFGVLFQRGALFSSLTVTENV--A 105
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLNVLAE--RVTTG---VITGGDRLVNGRPLdSSFQRSIGYVQQQDLHLPTSTVRESLrfS 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 106 LPLIENAGLPRSEAER----------LAQVKLALAGLPpGTGskypasLSGGMVKRVALARALALDPD-ILFLDEPTAGL 174
Cdd:TIGR00956 861 AYLRQPKSVSKSEKMEyveeviklleMESYADAVVGVP-GEG------LNVEQRKRLTIGVELVAKPKlLLFLDEPTSGL 933
|
170
....*....|....*...
gi 553371603 175 DPIGAAAFDSLIRTLRDA 192
Cdd:TIGR00956 934 DSQTAWSICKLMRKLADH 951
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
19-202 |
2.45e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 52.64 E-value: 2.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 19 QCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLmalsGQSRAMVERRFGVLFQRGALFSSL 98
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTYQKQLCFVGHRSGINPYL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 99 TVTENVALPLIENAG-LPRSEAERLAQVKLALaglppgtgsKYPAS-LSGGMVKRVALARALALDPDILFLDEPTAGLDP 176
Cdd:PRK13540 90 TLRENCLYDIHFSPGaVGITELCRLFSLEHLI---------DYPCGlLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDE 160
|
170 180
....*....|....*....|....*.
gi 553371603 177 IGAAAFDSLIRTLRdALNLTVFLVTH 202
Cdd:PRK13540 161 LSLLTIITKIQEHR-AKGGAVLLTSH 185
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
7-237 |
2.74e-08 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 53.37 E-value: 2.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 7 IQIRDLVNCF--GVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSramVERR 84
Cdd:cd03288 20 IKIHDLCVRYenNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHT---LRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 85 FGVLFQRGALFSSlTVTENVAlPLIENAGLPRSEAERLAQVKLALAGLPPGTG---SKYPASLSGGMVKRVALARALALD 161
Cdd:cd03288 97 LSIILQDPILFSG-SIRFNLD-PECKCTDDRLWEALEIAQLKNMVKSLPGGLDavvTEGGENFSVGQRQLFCLARAFVRK 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 553371603 162 PDILFLDEPTAGLDpigAAAFDSLIRTLRDAL-NLTVFLVTHDLDTLYTlCDRVAVLSQKKVLVVDTLDKVAATDDG 237
Cdd:cd03288 175 SSILIMDEATASID---MATENILQKVVMTAFaDRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQEDG 247
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
7-177 |
3.00e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.87 E-value: 3.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 7 IQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGlRRPTDgkihvFGKDLMaLSGQSRAMVERRFG 86
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQG-----YSNDLT-LFGRRRGSGETIWD 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 87 VLFQRGALFSSL-------TVTENVALP-LIENAGLPR--SEAER-LAQVKLALAGLPPGTGSKYPASLSGGMVKRVALA 155
Cdd:PRK10938 334 IKKHIGYVSSSLhldyrvsTSVRNVILSgFFDSIGIYQavSDRQQkLAQQWLDILGIDKRTADAPFHSLSWGQQRLALIV 413
|
170 180
....*....|....*....|..
gi 553371603 156 RALALDPDILFLDEPTAGLDPI 177
Cdd:PRK10938 414 RALVKHPTLLILDEPLQGLDPL 435
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
131-214 |
3.51e-08 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 54.06 E-value: 3.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 131 GLPPGTGSKYPASLSGGMVKRVALARALA--LDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDALNlTVFLVTHDlDTLY 208
Cdd:PRK00635 464 GLPYLTPERALATLSGGEQERTALAKHLGaeLIGITYILDEPSIGLHPQDTHKLINVIKKLRDQGN-TVLLVEHD-EQMI 541
|
....*.
gi 553371603 209 TLCDRV 214
Cdd:PRK00635 542 SLADRI 547
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
19-217 |
3.70e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 52.75 E-value: 3.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 19 QCVHQ-GLN------LDVKR-GEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKI-----------HVFGKDLM-----ALS 74
Cdd:cd03236 5 EPVHRyGPNsfklhrLPVPReGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeildEFRGSELQnyftkLLE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 75 GQSRAMVERRFGVLFQRgalfsslTVTENVALpLIENAglprSEAERLAQV--KLALAGLPpgtgSKYPASLSGGMVKRV 152
Cdd:cd03236 85 GDVKVIVKPQYVDLIPK-------AVKGKVGE-LLKKK----DERGKLDELvdQLELRHVL----DRNIDQLSGGELQRV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 553371603 153 ALARALALDPDILFLDEPTAGLD---PIGAAAfdsLIRTLRDALNlTVFLVTHDLDTLYTLCDRVAVL 217
Cdd:cd03236 149 AIAAALARDADFYFFDEPSSYLDikqRLNAAR---LIRELAEDDN-YVLVVEHDLAVLDYLSDYIHCL 212
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
21-221 |
5.39e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.49 E-value: 5.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 21 VHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVfgKDLMALSGQSRAMVERRFGVLFQRGALFS---- 96
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIII--NDSHNLKDINLKWWRSKIGVVSQDPLLFSnsik 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 97 --------SLTVTENVALPLIENAGLPRSEAERLAQVKLALAG------------------------------------- 131
Cdd:PTZ00265 478 nnikyslySLKDLEALSNYYNEDGNDSQENKNKRNSCRAKCAGdlndmsnttdsneliemrknyqtikdsevvdvskkvl 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 132 -------LPPG----TGSKyPASLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDALNLTVFLV 200
Cdd:PTZ00265 558 ihdfvsaLPDKyetlVGSN-ASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIII 636
|
250 260
....*....|....*....|.
gi 553371603 201 THDLDTLyTLCDRVAVLSQKK 221
Cdd:PTZ00265 637 AHRLSTI-RYANTIFVLSNRE 656
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
22-242 |
5.68e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 53.36 E-value: 5.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 22 HQGLN---LDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGK-DLMALSgqsramverrfgvlfqrGALFSS 97
Cdd:PRK13545 37 HYALNnisFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSaALIAIS-----------------SGLNGQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 98 LTVTENVALPLIEnAGLPRSEAERLAQVKLALAGLppGTGSKYPA-SLSGGMVKRVALARALALDPDILFLDEPTAgldp 176
Cdd:PRK13545 100 LTGIENIELKGLM-MGLTKEKIKEIIPEIIEFADI--GKFIYQPVkTYSSGMKSRLGFAISVHINPDILVIDEALS---- 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 553371603 177 IGAAAFdslIRTLRDALN------LTVFLVTHDLDTLYTLCDRVAVLSQKKVLVVDTLDKVAATDDGWIQAY 242
Cdd:PRK13545 173 VGDQTF---TKKCLDKMNefkeqgKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHYDEFLKKY 241
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
31-207 |
9.24e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 50.06 E-value: 9.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 31 RGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFgkdlmalsgqsramverrfgvlfqrgalfssltvtenvalplie 110
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYI-------------------------------------------- 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 111 naglprsEAERLAQVKLALAGLPPGTGSKYpaSLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAAAFDSLIRTLR 190
Cdd:smart00382 37 -------DGEDILEEVLDQLLLIIVGGKKA--SGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRL 107
|
170 180
....*....|....*....|..
gi 553371603 191 DAL-----NLTVFLVTHDLDTL 207
Cdd:smart00382 108 LLLlksekNLTVILTTNDEKDL 129
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
25-175 |
9.73e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.86 E-value: 9.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 25 LNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGkihvfgkdlmalsgqsRAMVERRFGVLFQRgALFSSLTVTENV 104
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEG----------------RVWAERSIAYVPQQ-AWIMNATVRGNI 741
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 553371603 105 ALPLIENAGlPRSEAERLAQVKLALAGLPPG----TGSKyPASLSGGMVKRVALARALALDPDILFLDEPTAGLD 175
Cdd:PTZ00243 742 LFFDEEDAA-RLADAVRVSQLEADLAQLGGGleteIGEK-GVNLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
26-217 |
2.04e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.27 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 26 NLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDL------MAL-SGQSraMVERRFGVLFQRgalfssl 98
Cdd:PRK10982 18 NLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfksskEALeNGIS--MVHQELNLVLQR------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 99 TVTENVALPLIENAGLPRSEAERLAQVKLALAGLPPGTGSKYP-ASLSGGMVKRVALARALALDPDILFLDEPTAGLDPI 177
Cdd:PRK10982 89 SVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKvATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 553371603 178 GAAAFDSLIRTLRDAlNLTVFLVTHDLDTLYTLCDRVAVL 217
Cdd:PRK10982 169 EVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITIL 207
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
25-222 |
2.42e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 51.66 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 25 LNLDVKRGEVLGVVGGSGTGKSVLLRSIVGlrrptdgkihvfgkDLMALSGQSrAMVERRFGVLFQRGALFSSlTVTENV 104
Cdd:PLN03130 636 INLDVPVGSLVAIVGSTGEGKTSLISAMLG--------------ELPPRSDAS-VVIRGTVAYVPQVSWIFNA-TVRDNI 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 105 ALPLIENAglPRSE-AERLAQVKLALAGLPPG----TGSKyPASLSGGMVKRVALARALALDPDILFLDEPTAGLDP-IG 178
Cdd:PLN03130 700 LFGSPFDP--ERYErAIDVTALQHDLDLLPGGdlteIGER-GVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAhVG 776
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 553371603 179 AAAFDSLIrtlRDAL-NLTVFLVTHDLDTLYTLcDRVAVLSQKKV 222
Cdd:PLN03130 777 RQVFDKCI---KDELrGKTRVLVTNQLHFLSQV-DRIILVHEGMI 817
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
10-203 |
3.30e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.72 E-value: 3.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 10 RDLVNCFGVQcvhqglnldVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSRAmverrfgvlf 89
Cdd:PRK11147 332 KQLVKDFSAQ---------VQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRA---------- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 90 qrgALFSSLTVTENVA--LPLIENAGLPRSeaerlaqvklALAGL-----PPGTGSKYPASLSGGMVKRVALARaLALDP 162
Cdd:PRK11147 393 ---ELDPEKTVMDNLAegKQEVMVNGRPRH----------VLGYLqdflfHPKRAMTPVKALSGGERNRLLLAR-LFLKP 458
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 553371603 163 -DILFLDEPTAGLDpigaaafdslIRTLR------DALNLTVFLVTHD 203
Cdd:PRK11147 459 sNLLILDEPTNDLD----------VETLElleellDSYQGTVLLVSHD 496
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
24-222 |
3.73e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.63 E-value: 3.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 24 GLNLDVKrgevLGVVGGSGTGKSVLLRSIVGLRRPTDG--------KIHVFGK---DLMALSGQSRAMVERRF-GVLFQR 91
Cdd:PLN03073 531 GIDLDSR----IAMVGPNGIGKSTILKLISGELQPSSGtvfrsakvRMAVFSQhhvDGLDLSSNPLLYMMRCFpGVPEQK 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 92 -GALFSSLTVTENVALPlienaglprseaerlaqvklalaglppgtgSKYpaSLSGGMVKRVALARALALDPDILFLDEP 170
Cdd:PLN03073 607 lRAHLGSFGVTGNLALQ------------------------------PMY--TLSGGQKSRVAFAKITFKKPHILLLDEP 654
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 553371603 171 TAGLDpigAAAFDSLIRTLRdALNLTVFLVTHDLDTLYTLCDRVAVLSQKKV 222
Cdd:PLN03073 655 SNHLD---LDAVEALIQGLV-LFQGGVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-217 |
4.55e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.55 E-value: 4.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 17 GVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVFGKDLMALSGQSramVERRFGVLFQRGALFS 96
Cdd:PTZ00243 1321 GLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRE---LRRQFSMIPQDPVLFD 1397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 97 SlTVTENVAlPLIEnaglpRSEAERLAqvKLALAGLppgtgSKYPASLSGGMVKRV---------------ALARA-LAL 160
Cdd:PTZ00243 1398 G-TVRQNVD-PFLE-----ASSAEVWA--ALELVGL-----RERVASESEGIDSRVleggsnysvgqrqlmCMARAlLKK 1463
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 553371603 161 DPDILFLDEPTAGLDPigaaAFDSLIR-TLRDAL-NLTVFLVTHDLDTLyTLCDRVAVL 217
Cdd:PTZ00243 1464 GSGFILMDEATANIDP----ALDRQIQaTVMSAFsAYTVITIAHRLHTV-AQYDKIIVM 1517
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
125-207 |
4.65e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 48.86 E-value: 4.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 125 VKLALAGLPPGtgsKYPASLSGGMVKRVALARALALDP-DILF-LDEPTAGLDPIGAAAFDSLIRTLRDaLNLTVFLVTH 202
Cdd:cd03238 72 IDVGLGYLTLG---QKLSTLSGGELQRVKLASELFSEPpGTLFiLDEPSTGLHQQDINQLLEVIKGLID-LGNTVILIEH 147
|
....*
gi 553371603 203 DLDTL 207
Cdd:cd03238 148 NLDVL 152
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
122-249 |
1.01e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.46 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 122 LAQVKLALAGLPPGTGskypasLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAAAfdsLIRTLRDalnlTVflvt 201
Cdd:PLN03140 1004 LDNLKDAIVGLPGVTG------LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAI---VMRTVRN----TV---- 1066
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 553371603 202 hdlDTLYTLcdrVAVLSQKKVLVVDTLDKVAATDDGWiQAYFHGPRGR 249
Cdd:PLN03140 1067 ---DTGRTV---VCTIHQPSIDIFEAFDELLLMKRGG-QVIYSGPLGR 1107
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
131-207 |
1.23e-06 |
|
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: 48.02 E-value: 1.23e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 553371603 131 GLPPGTGSKYPASLSGGMVKRVALARAL--ALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDALNlTVFLVTHDLDTL 207
Cdd:cd03270 125 GLGYLTLSRSAPTLSGGEAQRIRLATQIgsGLTGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGN-TVLVVEHDEDTI 202
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
151-215 |
1.38e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 48.73 E-value: 1.38e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 553371603 151 RVALARALALDPDILFLDEPTAGLDpigaaaFDSlIRTLRDALN---LTVFLVTHDLDTLYTLCDRVA 215
Cdd:PRK15064 163 RVLLAQALFSNPDILLLDEPTNNLD------INT-IRWLEDVLNernSTMIIISHDRHFLNSVCTHMA 223
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
25-219 |
1.61e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 49.20 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 25 LNLDVKRGEVLGVVGGSGTGKSVLLRSIVGlrrptdgkihvfgkdlmALSGQSRAMVERRFGVLF--QRGALFSSlTVTE 102
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISAMLG-----------------ELSHAETSSVVIRGSVAYvpQVSWIFNA-TVRE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 103 NVALPlienaglPRSEAERLAQVKLALA-----GLPPGTG----SKYPASLSGGMVKRVALARALALDPDILFLDEPTAG 173
Cdd:PLN03232 698 NILFG-------SDFESERYWRAIDVTAlqhdlDLLPGRDlteiGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSA 770
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 553371603 174 LDP-IGAAAFDSLIRtlRDALNLTVFLVTHDLDTLyTLCDRVAVLSQ 219
Cdd:PLN03232 771 LDAhVAHQVFDSCMK--DELKGKTRVLVTNQLHFL-PLMDRIILVSE 814
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
21-219 |
4.24e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.48 E-value: 4.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 21 VHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGlR---RPTDGKIHVFGKDLmALSGQSRA-------MVERR--FG-V 87
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFG-RsygRNISGTVFKDGKEV-DVSTVSDAidaglayVTEDRkgYGlN 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 88 LFQrgalfsslTVTENV---ALPLIENAGLPRSEAERLA--QVKLALAGLPPGTGSKYpASLSGGMVKRVALARALALDP 162
Cdd:NF040905 353 LID--------DIKRNItlaNLGKVSRRGVIDENEEIKVaeEYRKKMNIKTPSVFQKV-GNLSGGNQQKVVLSKWLFTDP 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 553371603 163 DILFLDEPTAGLDpIGaAAFD--SLIRTLRDAlNLTVFLVTHDLDTLYTLCDRVAVLSQ 219
Cdd:NF040905 424 DVLILDEPTRGID-VG-AKYEiyTIINELAAE-GKGVIVISSELPELLGMCDRIYVMNE 479
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
144-205 |
7.41e-06 |
|
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: 45.04 E-value: 7.41e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 553371603 144 LSGGMVKRVALARALAL---DPDILF-LDEPTAGLDPIGAAAFDSLIRTLRDaLNLTVFLVTHDLD 205
Cdd:cd03227 78 LSGGEKELSALALILALaslKPRPLYiLDEIDRGLDPRDGQALAEAILEHLV-KGAQVIVITHLPE 142
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-193 |
8.25e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 46.65 E-value: 8.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 4 DAIIQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKIHVfGKDL-MALSGQSRAmve 82
Cdd:PRK11819 322 DKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVkLAYVDQSRD--- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 83 rrfgvlfqrgALFSSLTVTENVA--LPLIenaglprseaeRLAQVKL---ALAGLPPGTGS---KYPASLSGGMVKRVAL 154
Cdd:PRK11819 398 ----------ALDPNKTVWEEISggLDII-----------KVGNREIpsrAYVGRFNFKGGdqqKKVGVLSGGERNRLHL 456
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 553371603 155 ARALALDPDILFLDEPTAGLDpigaaafdslIRTLR---DAL 193
Cdd:PRK11819 457 AKTLKQGGNVLLLDEPTNDLD----------VETLRaleEAL 488
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
37-203 |
8.31e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 45.29 E-value: 8.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 37 VVGGSGTGKSVLLRSIV----GLRRPTdgKIHVFGKDLMALSGQSRAMVERRFGVLFQRgalfsSLTVTENvaLPLIENA 112
Cdd:cd03240 27 IVGQNGAGKTTIIEALKyaltGELPPN--SKGGAHDPKLIREGEVRAQVKLAFENANGK-----KYTITRS--LAILENV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 113 GLPRSEAERlaqvKLALagLPPGT---GSKYPASLSggmvKRVALARALALDPDILFLDEPTAGLDP--IgAAAFDSLIR 187
Cdd:cd03240 98 IFCHQGESN----WPLL--DMRGRcsgGEKVLASLI----IRLALAETFGSNCGILALDEPTTNLDEenI-EESLAEIIE 166
|
170
....*....|....*.
gi 553371603 188 TLRDALNLTVFLVTHD 203
Cdd:cd03240 167 ERKSQKNFQLIVITHD 182
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
139-217 |
1.12e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.16 E-value: 1.12e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 553371603 139 KYpasLSGGMVKRVALARALALDPDILFLDEPTAGLDPIGAAAFDSLIRTLRDAlNLTVFLVTHDLDTLYTLCDRVAVL 217
Cdd:PRK10938 134 KY---LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVL 208
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
52-204 |
2.30e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 41.61 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 52 IVGLRRPTDGKIHVFGKDLMALSGQSRamveRRFGVLFQRGALFSSLTVTENVALPLIENAGLPRSEAERLAQVKLALAG 131
Cdd:pfam13304 139 ISGLLLLSIISPLSFLLLLDEGLLLED----WAVLDLAADLALFPDLKELLQRLVRGLKLADLNLSDLGEGIEKSLLVDD 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 132 LPPGTGSKY----------PASLSGGMVKRVALARALALD---PDILFLDEPTAGLDPigaaafdSLIRTLRDALNLT-- 196
Cdd:pfam13304 215 RLRERGLILlenggggelpAFELSDGTKRLLALLAALLSAlpkGGLLLIDEPESGLHP-------KLLRRLLELLKELsr 287
|
170
....*....|..
gi 553371603 197 ----VFLVTHDL 204
Cdd:pfam13304 288 ngaqLILTTHSP 299
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
143-222 |
2.39e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.08 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 143 SLSGGMVKRVALARALALDPDILFLDEPTAGLDpigaaaFDSLI---RTLRdALNLTVFLVTHDLDTLYTLCDRVAVLSQ 219
Cdd:PRK10636 149 DFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD------LDAVIwleKWLK-SYQGTLILISHDRDFLDPIVDKIIHIEQ 221
|
...
gi 553371603 220 KKV 222
Cdd:PRK10636 222 QSL 224
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
131-207 |
3.96e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.54 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 131 GLPPGTGSKYPASLSGGMVKRVALARAL--ALDPDILFLDEPTAGLDPIGAaafDSLIRTLRDALNL--TVFLVTHDLDT 206
Cdd:TIGR00630 476 GLDYLSLSRAAGTLSGGEAQRIRLATQIgsGLTGVLYVLDEPSIGLHQRDN---RRLINTLKRLRDLgnTLIVVEHDEDT 552
|
.
gi 553371603 207 L 207
Cdd:TIGR00630 553 I 553
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
142-214 |
8.87e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.39 E-value: 8.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 142 ASLSGGMVKRVALARAL--ALdPDILF-LDEPTAGLDP------IGAaafdslIRTLRDALNlTVFLVTHDLDTLYTlCD 212
Cdd:COG0178 484 GTLSGGEAQRIRLATQIgsGL-VGVLYvLDEPSIGLHQrdndrlIET------LKRLRDLGN-TVIVVEHDEDTIRA-AD 554
|
..
gi 553371603 213 RV 214
Cdd:COG0178 555 YI 556
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
7-222 |
1.01e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 40.26 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 7 IQIRDLVNCFGVQCVHQGLNLDVKRGEVLGVVGGSGTGKSVLLRSIVGLRRPTDGKI----------------HVFGKD- 69
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwsenanigyyaqdhaYDFENDl 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 70 -LMALSGQSRA------MVERRFGVLfqrgaLFSSltvtenvalplienaglprSEAERLAQVklalaglppgtgskypa 142
Cdd:PRK15064 400 tLFDWMSQWRQegddeqAVRGTLGRL-----LFSQ-------------------DDIKKSVKV----------------- 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553371603 143 sLSGGMVKRVALARALALDPDILFLDEPTAGLDpigaaaFDSlIRTLRDALNL---TVFLVTHDLDTLYTLCDRVAVLSQ 219
Cdd:PRK15064 439 -LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMD------MES-IESLNMALEKyegTLIFVSHDREFVSSLATRIIEITP 510
|
...
gi 553371603 220 KKV 222
Cdd:PRK15064 511 DGV 513
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
137-205 |
2.38e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 39.26 E-value: 2.38e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 553371603 137 GSKYPASLsggmVKRVALARALALDPDILFLDEPTAGLDPIG----AAAFDSLIRTLRDALNLTVFLVTHDLD 205
Cdd:TIGR00606 1203 GQKVLASL----IIRLALAETFCLNCGIIALDEPTTNLDRENieslAHALVEIIKSRSQQRNFQLLVITHDED 1271
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
143-205 |
3.74e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.46 E-value: 3.74e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 553371603 143 SLSGGMVKRVALARAL---ALDPDILFLDEPTAGLDpigaaaFD------SLIRTLRDALNlTVFLVTHDLD 205
Cdd:TIGR00630 829 TLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLH------FDdikkllEVLQRLVDKGN-TVVVIEHNLD 893
|
|
| |
